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C14: Caspase C

Unless otherwise stated all data on this page refer to the human proteins. Gene information is provided for human (Hs), mouse (Mm) and rat (Rn).

Overview

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Caspases, (E.C. 3.4.22.-) which derive their name from Cysteine ASPartate-specific proteASES, include at least two families; initiator caspases (caspases 2, 8, 9 and 10), which are able to hydrolyse and activate a second family of effector caspases (caspases 3, 6 and 7), which themselves are able to hydrolyse further cellular proteins to bring about programmed cell death. Caspases are heterotetrameric, being made up of two pairs of subunits, generated by a single gene product, which is proteolysed to form the mature protein. Members of the mammalian inhibitors of apoptosis proteins (IAP) are able to bind the procaspases, thereby preventing maturation to active proteinases.

Enzymes

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Caspase 1 Show summary » More detailed page go icon to follow link

Caspase 2 Show summary » More detailed page go icon to follow link

Caspase 3 Show summary » More detailed page go icon to follow link

Caspase 4 Show summary » More detailed page go icon to follow link

Caspase 5 Show summary » More detailed page go icon to follow link

Caspase 6 Show summary » More detailed page go icon to follow link

Caspase 7 Show summary » More detailed page go icon to follow link

Caspase 8 Show summary » More detailed page go icon to follow link

Caspase 9 Show summary » More detailed page go icon to follow link

Caspase 10 Show summary » More detailed page go icon to follow link

Caspase 14 Show summary » More detailed page go icon to follow link

Comments

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References

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How to cite this family page

Database page citation:

C14: Caspase. Accessed on 04/12/2024. IUPHAR/BPS Guide to PHARMACOLOGY, http://www.guidetopharmacology.org/GRAC/FamilyDisplayForward?familyId=734.

Concise Guide to PHARMACOLOGY citation:

Alexander SPH, Fabbro D, Kelly E, Mathie AA, Peters JA, Veale EL, Armstrong JF, Faccenda E, Harding SD, Davies JA et al. (2023) The Concise Guide to PHARMACOLOGY 2023/24: Enzymes. Br J Pharmacol. 180 Suppl 2:S289-373.