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BRENDA support

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

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 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.49 separase

Source Tissue

Source Tissue on EC 3.4.22.49 - separase

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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
overexpressed in numerous human cancers including breast, bone, brain, and prostate
Manually annotated by BRENDA team
-
in a murine model of absent securin expression, the PTTG knock-out mouse, separase and Rad21 are over-expressed in multiple brain regions. Furthermore, Rad21 mRNA expression is highly correlated with that of securin, separase, cyclin C and sestrin 2 in fetal brains
Manually annotated by BRENDA team
overexpressed in numerous human cancers including breast, bone, brain, and prostate
Manually annotated by BRENDA team
-
highly expressed in human fetal cerebral cortex compared with adult
Manually annotated by BRENDA team
-
separase expression is very high in both normal nonneoplastic and neoplastic colons
Manually annotated by BRENDA team
-
separase localizes to the ingressing furrow and midbody during cytokinesis in the Caenorhabditis elegans embryo
Manually annotated by BRENDA team
-
diploid FSK3 mouse mammary epithelial cells
Manually annotated by BRENDA team
-
increased expression of separase
Manually annotated by BRENDA team
-
increased expression of separase
Manually annotated by BRENDA team
overexpressed in numerous human cancers including breast, bone, brain, and prostate
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team