Caspase 2

CASP2
Gene ontology
Molecular function	cysteine-type peptidase activity protein domain specific binding peptidase activity protein binding enzyme binding hydrolase activity identical protein binding cysteine-type endopeptidase activity involved in apoptotic process cysteine-type endopeptidase activity cysteine-type endopeptidase activity involved in execution phase of apoptosis
Cellular component	cytoplasm cytosol membrane mitochondrion nucleus
Biological process	DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest execution phase of apoptosis protein processing human ageing positive regulation of apoptotic signaling pathway luteolysis cellular response to mechanical stimulus positive regulation of neuron apoptotic process brain development intrinsic apoptotic signaling pathway in response to DNA damage extrinsic apoptotic signaling pathway in absence of ligand positive regulation of apoptotic process ectopic germ cell programmed cell death apoptotic signaling pathway neural retina development apoptotic process regulation of apoptotic process proteolysis negative regulation of apoptotic process
Sources:Amigo / QuickGO

Ensembl				ENSG00000106144	ENSMUSG00000029863
UniProt	P42575	P29594
RefSeq (mRNA)	NM_032983 NM_001224 NM_032982 NM_032984	NM_007610
RefSeq (protein)	NP_001215 NP_116764 NP_116765	NP_031636
Location (UCSC)	Chr 7: 143.29 – 143.31 Mb	Chr 6: 42.24 – 42.26 Mb
PubMed search	[3]	[4]

Wikidata

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Caspase 2 also known as CASP2 is an

.

Function

Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes that undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. The proteolytic cleavage of this protein is induced by a variety of apoptotic stimuli.^[7]

Caspase 2

. 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).^[8] Together with RAIDD and p53-induced protein with a death domain ([PIDD])(LRDD), caspase 2 has been shown to form the so-called PIDDosome,^[9] which may serve as an activation platform for the protease, although it may also be activated in the absence of PIDD.^[10] Overall, caspase 2 appears to be a very versatile caspase with multiple functions beyond cell death induction.^[11][12]

Interactions

Caspase 2 has been shown to

with:

• BH3 interacting domain death agonist,^[13][14]
• CRADD,^[9][15][16] and
• Caspase 8.^[13][17]

See also

• The Proteolysis Map
• Caspase

References

External links

• The MEROPS online database for peptidases and their inhibitors: C14.006^{[permanent dead link]}
• Overview of all the structural information available in the PDB for UniProt: P42575 (Human Caspase-2) at the PDBe-KB.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.