EC                Enzyme                                 

neural precursor cell expressed developmentally down-regulated protein 2;
NEDD2 protein
Acting on peptide bonds (peptidases);
Cysteine endopeptidases
BRITE hierarchy
Strict requirement for an Asp residue at P1, with Asp316 being essential for proteolytic activity and has a preferred cleavage sequence of Val-Asp-Val-Ala-Asp!
Caspase-2 is an initiator caspase, as are caspase-8 (EC, caspase-9 (EC and caspase-10 (EC [6]. Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation [6]. Two forms of caspase-2 with antagonistic effects exist: caspase-2L induces programmed cell death and caspase-2S suppresses cell death [2,3,5]. Caspase-2 is activated by caspase-3 (EC, or by a caspase-3-like protease. Activation involves cleavage of the N-terminal prodomain, followed by self-proteolysis between the large and small subunits of pro-caspase-2 and further proteolysis into smaller fragments [3]. Proteolysis occurs at Asp residues and the preferred substrate for this enzyme is a pentapeptide rather than a tetrapeptide [5]. Apart from itself, the enzyme can cleave golgin-16, which is present in the Golgi complex and has a cleavage site that is unique for caspase-2 [4,5]. alphaII-Spectrin, a component of the membrane cytoskeleton, is a substrate of the large isoform of pro-caspase-2 (caspase-2L) but not of the short isoform (caspase-2S). Belongs in peptidase family C14.
EC created 2007
K02186  caspase 2
HSA: 835(CASP2)
PTR: 463804(CASP2)
PPS: 100984572(CASP2)
GGO: 101128958(CASP2)
PON: 100454928(CASP2)
NLE: 100599260(CASP2)
MCC: 704339(CASP2)
MCF: 102128712(CASP2)
CSAB: 103227412(CASP2)
RRO: 104674919(CASP2)
RBB: 108544234(CASP2)
CJC: 100402493(CASP2)
SBQ: 101040888(CASP2)
MMU: 12366(Casp2)
RNO: 64314(Casp2)
CGE: 100689445(Casp2)
NGI: 103730398(Casp2)
HGL: 101712106(Casp2)
CCAN: 109697479(Casp2)
OCU: 100101590(CASP2)
TUP: 102498970(CASP2)
CFA: 482737(CASP2)
AML: 100474060(CASP2)
UMR: 103668980(CASP2)
ORO: 101384305(CASP2)
FCA: 101088318(CASP2)
PTG: 102948856(CASP2)
AJU: 106980767(CASP2)
BTA: 531419(CASP2)
BOM: 102272786(CASP2)
BIU: 109557747(CASP2)
PHD: 102317813(CASP2)
CHX: 102183569(CASP2)
OAS: 101115025(CASP2)
SSC: 100521118(CASP2)
CFR: 102508934(CASP2)
CDK: 105105559(CASP2)
BACU: 103017857(CASP2)
LVE: 103085195(CASP2)
OOR: 101271768(CASP2)
ECB: 100050611(CASP2)
EPZ: 103562808(CASP2)
EAI: 106833854(CASP2)
MYB: 102264102(CASP2)
MYD: 102774985(CASP2)
HAI: 109376369(CASP2)
RSS: 109436648(CASP2)
PALE: 102895485(CASP2)
LAV: 100661506(CASP2)
TMU: 101361957
MDO: 100011923(CASP2)
SHR: 100919881(CASP2)
OAA: 100074924(CASP2)
GGA: 395857(CASP2)
MGP: 100544010(CASP2)
CJO: 107319105(CASP2)
APLA: 101794734(CASP2)
ACYG: 106048728(CASP2)
TGU: 100221143(CASP2)
GFR: 102043378(CASP2)
FAB: 101805629(CASP2)
PHI: 102108085(CASP2)
PMAJ: 107210261(CASP2)
CCW: 104687148(CASP2)
FPG: 101915905(CASP2)
FCH: 102048179(CASP2)
CLV: 102095337(CASP2)
EGZ: 104126551(CASP2)
AAM: 106497280(CASP2)
ASN: 102377638(CASP2)
AMJ: 102558644(CASP2)
PSS: 102463164(CASP2)
CMY: 102929343(CASP2)
CPIC: 101938497(CASP2)
ACS: 100567806(casp2)
PVT: 110091477(CASP2)
PBI: 103051794(CASP2)
GJA: 107115535(CASP2)
XLA: 108697326 397817(casp2.L) 398436
XTR: 100486813(casp2)
NPR: 108784894(CASP2)
DRE: 373118(casp2)
SANH: 107685580 107699940(casp2)
SGH: 107569996(casp2) 107596737
IPU: 108268399(casp2)
AMEX: 103030250(casp2)
TRU: 101072588(casp2)
LCO: 104929017(casp2)
NCC: 104954509
MZE: 101470507(casp2)
OLA: 101171774(casp2)
XMA: 102216745(casp2)
PRET: 103478021(casp2)
NFU: 107379433(casp2)
CSEM: 103387931(casp2)
LCF: 108887338(casp2)
HCQ: 109515309(casp2)
BPEC: 110163095(casp2)
ELS: 105019056(casp2)
SFM: 108924035(casp2)
LCM: 102349624(CASP2)
BMY: Bm1_42735
SHX: MS3_04628
ADF: 107345198
 » show all
1  [PMID:7958843]
Kumar S, Kinoshita M, Noda M, Copeland NG, Jenkins NA.
Induction of apoptosis by the mouse Nedd2 gene, which encodes a protein similar to the product of the Caenorhabditis elegans cell death gene ced-3 and the mammalian IL-1 beta-converting enzyme.
Genes. Dev. 8 (1994) 1613-26.
2  [PMID:8087842]
Wang L, Miura M, Bergeron L, Zhu H, Yuan J.
Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death.
Cell. 78 (1994) 739-50.
3  [PMID:9261102]
Li H, Bergeron L, Cryns V, Pasternack MS, Zhu H, Shi L, Greenberg A, Yuan J.
Activation of caspase-2 in apoptosis.
J. Biol. Chem. 272 (1997) 21010-7.
4  [PMID:10791974]
Mancini M, Machamer CE, Roy S, Nicholson DW, Thornberry NA, Casciola-Rosen LA, Rosen A.
Caspase-2 is localized at the Golgi complex and cleaves golgin-160 during apoptosis.
J. Cell. Biol. 149 (2000) 603-12.
5  [PMID:15865942]
Zhivotovsky B, Orrenius S.
Caspase-2 function in response to DNA damage.
Biochem. Biophys. Res. Commun. 331 (2005) 859-67.
6  [PMID:11104820]
Chang HY, Yang X.
Proteases for cell suicide: functions and regulation of caspases.
Microbiol. Mol. Biol. Rev. 64 (2000) 821-46.
Other DBs
ExplorEnz - The Enzyme Database:
IUBMB Enzyme Nomenclature:
ExPASy - ENZYME nomenclature database:
BRENDA, the Enzyme Database:
CAS: 182372-14-1

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