Caspase 2

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Caspase 2, apoptosis-related cysteine peptidase (neural precursor cell expressed, developmentally down-regulated 2)
PDB rendering based on 1pyo.
Available structures: 1pyo, 2p2c
Identifiers
Symbol(s)	CASP2; CASP-2; ICH-1L; ICH-1L/1S; ICH1; NEDD2
External IDs	OMIM: 600639 MGI: 97295 HomoloGene: 7254
EC number	3.4.22.55
Gene ontology Molecular Function: • protein binding • cysteine-type peptidase activity • enzyme binding • caspase activity Cellular Component: • cellular_component • intracellular • nucleus Biological Process: • proteolysis • anti-apoptosis • apoptotic program • regulation of apoptosis
RNA expression pattern
More reference expression data
Orthologs
	Human	Mouse
Entrez	835	12366
Ensembl	ENSG00000106144	ENSMUSG00000029863
Uniprot	P42575	P29594
Refseq	NM_032982 (mRNA) NP_116764 (protein)	NM_007610 (mRNA) NP_031636 (protein)
Location	Chr 7: 142.7 - 142.71 Mb	Chr 6: 42.19 - 42.21 Mb
Pubmed search	[1]	[2]

Caspase 2 is an enzyme that proteolytically cleaves other proteins. It belongs to a family of cysteine proteases called caspases that only cleave proteins at an amino acid following a aspartic acid residue. Within this family, caspase 2 is part of the Ich-1 subfamily. It is one of the most conserved caspases in different species of animal. Caspase 2 has a similar amino acid sequence to initiator caspases, including caspase 1, caspase 4, caspase 5 and caspase 9. It is produced as a zymogen, which contains a long pro-domain that is similar to that of caspase 9 and contains a protein interaction domain known as a CARD domain. Pro-caspase-2 contains two subunits, p19 and p12. It has been shown to associate with several proteins involved in apoptosis using its CARD domain, including RIP-associated Ich-1/Ced-3-homologue protein with a death domain (RAIDD), apoptosis repressor with caspase recruitment domain (ARC) and death effector filament-forming Ced-4 like apoptosis protein (DEFCAP).^[1]

[edit] References

1. ^ Zhivotovsky B, Orrenius S (2005). "Caspase-2 function in response to DNA damage". Biochem. Biophys. Res. Commun. 331 (3): 859–67. doi:10.1016/j.bbrc.2005.03.191. PMID 15865942. 

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