Caspase 7

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Caspase 7, apoptosis-related cysteine peptidase
Protein CASP7 PDB 1f1j.png
PDB rendering based on 1f1j.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols CASP7 ; CASP-7; CMH-1; ICE-LAP3; LICE2; MCH3
External IDs OMIM601761 MGI109383 HomoloGene11168 ChEMBL: 3468 GeneCards: CASP7 Gene
EC number
RNA expression pattern
PBB GE CASP7 207181 s at tn.png
More reference expression data
Species Human Mouse
Entrez 840 12369
Ensembl ENSG00000165806 ENSMUSG00000025076
UniProt P55210 P97864
RefSeq (mRNA) NM_001227 NM_007611
RefSeq (protein) NP_001218 NP_031637
Location (UCSC) Chr 10:
113.68 – 113.73 Mb
Chr 19:
56.4 – 56.44 Mb
PubMed search [1] [2]

Caspase-7, apoptosis-related cysteine peptidase, also known as CASP7, is a human protein encoded by the CASP7 gene. CASP7 orthologs [1] have been identified in nearly all mammals for which complete genome data are available. Unique orthologs are also present in birds, lizards, lissamphibians, and teleosts.


Caspase-7 is a member of the caspase (cysteine aspartate protease) family of proteins, and has been shown to be an executioner protein of apoptosis. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes that undergo proteolytic processing by upstream caspases (caspase-8, -9) at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme in the form of a heterotetramer. The precursor of this caspase is cleaved by caspase 3, caspase 10, and caspase 9. It is activated upon cell death stimuli and induces apoptosis. Alternative splicing results in four transcript variants, encoding three distinct isoforms.[2]


Caspase 7 has been shown to interact with:

See also[edit]


  1. ^ "OrthoMaM phylogenetic marker: CASP7 coding sequence". 
  2. ^ "Entrez Gene: CASP7 caspase 7, apoptosis-related cysteine peptidase". 
  3. ^ Guo Y, Srinivasula SM, Druilhe A, Fernandes-Alnemri T, Alnemri ES (Apr 2002). "Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria". J. Biol. Chem. 277 (16): 13430–7. doi:10.1074/jbc.M108029200. PMID 11832478. 
  4. ^ Srinivasula SM, Ahmad M, Fernandes-Alnemri T, Litwack G, Alnemri ES (Dec 1996). "Molecular ordering of the Fas-apoptotic pathway: the Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases". Proc. Natl. Acad. Sci. U.S.A. 93 (25): 14486–91. doi:10.1073/pnas.93.25.14486. PMC 26159. PMID 8962078. 
  5. ^ Tamm I, Wang Y, Sausville E, Scudiero DA, Vigna N, Oltersdorf T, Reed JC (Dec 1998). "IAP-family protein survivin inhibits caspase activity and apoptosis induced by Fas (CD95), Bax, caspases, and anticancer drugs". Cancer Res. 58 (23): 5315–20. PMID 9850056. 
  6. ^ Shin S, Sung BJ, Cho YS, Kim HJ, Ha NC, Hwang JI, Chung CW, Jung YK, Oh BH (Jan 2001). "An anti-apoptotic protein human survivin is a direct inhibitor of caspase-3 and -7". Biochemistry 40 (4): 1117–23. doi:10.1021/bi001603q. PMID 11170436. 
  7. ^ Riedl SJ, Renatus M, Schwarzenbacher R, Zhou Q, Sun C, Fesik SW, Liddington RC, Salvesen GS (Mar 2001). "Structural basis for the inhibition of caspase-3 by XIAP". Cell 104 (5): 791–800. doi:10.1016/S0092-8674(01)00274-4. PMID 11257232. 
  8. ^ Roy N, Deveraux QL, Takahashi R, Salvesen GS, Reed JC (Dec 1997). "The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases". EMBO J. 16 (23): 6914–25. doi:10.1093/emboj/16.23.6914. PMC 1170295. PMID 9384571. 
  9. ^ Deveraux QL, Takahashi R, Salvesen GS, Reed JC (Jul 1997). "X-linked IAP is a direct inhibitor of cell-death proteases". Nature 388 (6639): 300–4. doi:10.1038/40901. PMID 9230442. 
  10. ^ Suzuki Y, Nakabayashi Y, Nakata K, Reed JC, Takahashi R (Jul 2001). "X-linked inhibitor of apoptosis protein (XIAP) inhibits caspase-3 and -7 in distinct modes". J. Biol. Chem. 276 (29): 27058–63. doi:10.1074/jbc.M102415200. PMID 11359776. 

Further reading[edit]

External links[edit]

  • The MEROPS online database for peptidases and their inhibitors: C14.004