logo CaMPDB: Calpain for Modulatory Proteolysis Database

SB0110 : Caspase-7

[ CaMP Format ]

* Basic Information

OrganismHomo sapiens (human)
Protein Namescaspase-7 isoform alpha precursor [Homo sapiens]; caspase-7 isoform alpha precursor; caspase 7, apoptosis-related cysteine protease; ICE-like apoptotic protease 3; apoptotic protease MCH-3; Caspase-7; CASP-7;; Apoptotic protease Mch-3; CMH-1; ICE-LAP3; Caspase-7 subunit p20; Caspase-7 subunit p11
Gene NamesCASP7; MCH3; caspase 7, apoptosis-related cysteine peptidase
Gene Locus10q25; chromosome 10
GO FunctionNot available
Entrez Protein Entrez Nucleotide Entrez Gene UniProt OMIM HGNC HPRD KEGG
NP_001218 NM_001227 840 P55210 601761 HGNC:1508 03457 hsa:840

* Information From OMIM

Description: Programmed cell death (apoptosis) is associated with the hierarchical activation of a number of cysteine proteinases with cleavage preference after asparagine residues, comprising the caspase family C14 of clan CD (Barrett and Rawlings, 2001). Based on their position within this proteolytic cascade, caspases are subdivided into initiator caspases, which include caspase-8 (OMIM:601763) and caspase-9 (OMIM:602234), and executioner caspases, which include caspase-3 (OMIM:600636, also called CPP32), caspase-6 (OMIM:601532, also called MCH2), and caspase-7, as well as a third group of caspases involved in cytokine activation, namely, caspase-1 (OMIM:147678, also called ICE), caspase-4 (OMIM:602664), and caspase-5 (OMIM:602665). In apoptosis, the upstream caspases triggered by cofactor-mediated transactivation activate the downstream executioner caspases by limited proteolysis. These executioners, in turn, cleave distinct intracellular proteins involved in promoting the apoptotic phenotype.

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* Structure Information

1. Primary Information

Length: 303 aa

Average Mass: 34.276 kDa

Monoisotopic Mass: 34.255 kDa

2. Domain Information

Annotated Domains: interpro / pfam / smart / prosite

Computationally Assigned Domains (Pfam+HMMER):

domain namebeginendscoree-value
--- cleavage 36 ---
Caspase domain 1. 683011.00.0

3. Sequence Information

Fasta Sequence: SB0110.fasta

Amino Acid Sequence and Secondary Structures (PsiPred):

4. 3D Information

Known Structures in PDB: 1F1J (X-ray; 235 A; A/B=2-303), 1GQF (X-ray; 290 A; A/B=47-303), 1I4O (X-ray; 240 A; A/B=24-303), 1I51 (X-ray; 245 A; A/C=51-198, B/D=199-303), 1K86 (X-ray; 260 A; A/B=51-303), 1K88 (X-ray; 270 A; A/B=51-303), 1KMC (X-ray; 290 A; A/B=1-303), 1MIA (Model; -; A=57-193, B=211-303), 1SHJ (X-ray; 280 A; A/B=50-303), 1SHL (X-ray; 300 A; A/B=57-303), 2QL5 (X-ray; 234 A; A/C=24-196, B/D=207-303), 2QL7 (X-ray; 240 A; A/C=24-196, B/D=207-303), 2QL9 (X-ray; 214 A; A/C=24-196, B/D=207-303), 2QLB (X-ray; 225 A; A/C=24-196, B/D=207-303), 2QLF (X-ray; 280 A; A/C=24-196, B/D=207-303), 2QLJ (X-ray; 260 A; A/C=24-196, B/D=207-303), 3EDR (X-ray; 245 A; A/C=24-196, B/D=207-303), 3H1P (X-ray; 261 A; A/B=50-303), 3IBC (X-ray; 275 A; A/C=24-196, B/D=207-303), 3IBF (X-ray; 250 A; A/C=24-196, B/D=207-303), 3R5K (X-ray; 286 A; A/B=1-303), 4FDL (X-ray; 280 A; A/B=2-303), 4FEA (X-ray; 379 A; A/B=57-303), 4HQ0 (X-ray; 300 A; A/B=47-303), 4HQR (X-ray; 300 A; A/B=47-303), 4JB8 (X-ray; 170 A; A=24-198, B=207-303), 4JJ8 (X-ray; 294 A; A/B=57-303), 4JR1 (X-ray; 215 A; A/B=57-303), 4JR2 (X-ray; 165 A; A/B=57-303), 4LSZ (X-ray; 226 A; A/C=24-198, B/D=207-303)

* Cleavage Information

1 [sites] cleaved by Calpain 1

Source Reference: [PubMed ID: 19617626] Gafni J, Cong X, Chen SF, Gibson BW, Ellerby LM, Calpain-1 cleaves and activates caspase-7. J Biol Chem. 2009 Sep 11;284(37):25441-9. doi: 10.1074/jbc.M109.038174. Epub 2009

Cleavage sites (±10aa)


Phe36 Ser

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'

Sequence conservation (by blast)

* References

[PubMed ID: 24434142] Wakao K, Watanabe T, Takadama T, Ui S, Shigemi Z, Kagawa H, Higashi C, Ohga R, Taira T, Fujimuro M, Sangivamycin induces apoptosis by suppressing Erk signaling in primary effusion lymphoma cells. Biochem Biophys Res Commun. 2014 Feb 7;444(2):135-40. doi:

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