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Caspase-2 (CASP-2) (EC 3.4.22.55) (Neural precursor cell expressed developmentally down-regulated protein 2) (NEDD-2) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12]

 CASP2_HUMAN             Reviewed;         452 AA.
P42575; A8K5F9; D3DXD6; E9PDN0; P42576; Q59F21; Q7KZL6; Q86UJ3;
Q9BUP7; Q9BZK9; Q9BZL0;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 2.
30-AUG-2017, entry version 182.
RecName: Full=Caspase-2;
Short=CASP-2;
EC=3.4.22.55;
AltName: Full=Neural precursor cell expressed developmentally down-regulated protein 2;
Short=NEDD-2;
AltName: Full=Protease ICH-1;
Contains:
RecName: Full=Caspase-2 subunit p18;
Contains:
RecName: Full=Caspase-2 subunit p13;
Contains:
RecName: Full=Caspase-2 subunit p12;
Flags: Precursor;
Name=CASP2; Synonyms=ICH1, NEDD2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [MRNA]
OF 14-452 (ISOFORM 1).
TISSUE=Fetal brain;
PubMed=8087842; DOI=10.1016/S0092-8674(94)90422-7;
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 78:739-750(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF
32-108 (ISOFORMS 1/2), AND ALTERNATIVE SPLICING.
PubMed=11156409;
Droin N., Beauchemin M., Solary E., Bertrand R.;
"Identification of a caspase-2 isoform that behaves as an endogenous
inhibitor of the caspase cascade.";
Cancer Res. 60:7039-7047(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-172; ALA-178 AND
GLY-441.
NIEHS SNPs program;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
LEU-172.
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 18-452 (ISOFORM 1), AND
VARIANT LEU-172.
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 194-452.
TISSUE=Spleen;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[11]
CLEAVAGE SITES.
PubMed=8654923; DOI=10.1101/gad.10.9.1073;
Xue D., Shaham S., Horvitz H.R.;
"The Caenorhabditis elegans cell-death protein CED-3 is a cysteine
protease with substrate specificities similar to those of the human
CPP32 protease.";
Genes Dev. 10:1073-1083(1996).
[12]
INTERACTION WITH NOL3.
PubMed=9560245; DOI=10.1073/pnas.95.9.5156;
Koseki T., Inohara N., Chen S., Nunez G.;
"ARC, an inhibitor of apoptosis expressed in skeletal muscle and heart
that interacts selectively with caspases.";
Proc. Natl. Acad. Sci. U.S.A. 95:5156-5160(1998).
[13]
INTERACTION WITH LRDD.
PubMed=15073321; DOI=10.1126/science.1095432;
Tinel A., Tschopp J.;
"The PIDDosome, a protein complex implicated in activation of caspase-
2 in response to genotoxic stress.";
Science 304:843-846(2004).
[14]
INTERACTION WITH LRDD.
PubMed=16652156; DOI=10.1038/sj.onc.1209569;
Vakifahmetoglu H., Olsson M., Orrenius S., Zhivotovsky B.;
"Functional connection between p53 and caspase-2 is essential for
apoptosis induced by DNA damage.";
Oncogene 25:5683-5692(2006).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 167-452 IN COMPLEX WITH
INHIBITOR, SUBUNIT, AND DISULFIDE BOND.
PubMed=12920126; DOI=10.1074/jbc.M304895200;
Schweizer A., Briand C., Grutter M.G.;
"Crystal structure of caspase-2, apical initiator of the intrinsic
apoptotic pathway.";
J. Biol. Chem. 278:42441-42447(2003).
-!- FUNCTION: Involved in the activation cascade of caspases
responsible for apoptosis execution. Might function by either
activating some proteins required for cell death or inactivating
proteins necessary for cell survival.
-!- CATALYTIC ACTIVITY: Strict requirement for an Asp residue at P1,
with 316-asp being essential for proteolytic activity and has a
preferred cleavage sequence of Val-Asp-Val-Ala-Asp-|-.
-!- SUBUNIT: Heterotetramer that consists of two anti-parallel
arranged heterodimers, each one formed by a p18 subunit and a p12
subunit. Interacts with LRDD. Interacts with NOL3 (via CARD
domain); inhibits CASP2 activity in a phosphorylation-dependent
manner. {ECO:0000250|UniProtKB:P55215,
ECO:0000269|PubMed:12920126, ECO:0000269|PubMed:15073321,
ECO:0000269|PubMed:16652156, ECO:0000269|PubMed:9560245}.
-!- INTERACTION:
Self; NbExp=6; IntAct=EBI-520342, EBI-520342;
P42575-1:CASP2; NbExp=2; IntAct=EBI-520342, EBI-520357;
P78560:CRADD; NbExp=16; IntAct=EBI-520342, EBI-520375;
P78527:PRKDC; NbExp=4; IntAct=EBI-520342, EBI-352053;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Isoforms differ in the N- and C-termini.;
Name=1; Synonyms=ICH-1L;
IsoId=P42575-1; Sequence=Displayed;
Note=Acts as a positive regulator of apoptosis.;
Name=2; Synonyms=ICH-1S;
IsoId=P42575-2; Sequence=VSP_000801, VSP_000802;
Note=Acts as a negative regulator of apoptosis.;
Name=3; Synonyms=Casp-2L-Pro;
IsoId=P42575-3; Sequence=VSP_046280, VSP_046281, VSP_046282;
Note=May function as an endogenous apoptosis inhibitor that
antagonizes caspase activation and cell death.;
-!- TISSUE SPECIFICITY: Expressed at higher levels in the embryonic
lung, liver and kidney than in the heart and brain. In adults,
higher level expression is seen in the placenta, lung, kidney, and
pancreas than in the heart, brain, liver and skeletal muscle.
-!- PTM: The mature protease can process its own propeptide, but not
that of other caspases. {ECO:0000269|PubMed:8654923}.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA58959.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAO25653.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAP22346.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAP22349.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAD92877.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/casp2/";
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EMBL; U13021; AAA58959.1; ALT_INIT; mRNA.
EMBL; U13022; AAA58960.1; -; mRNA.
EMBL; AF314174; AAK00299.1; -; mRNA.
EMBL; AF314175; AAK00300.1; -; mRNA.
EMBL; CR541748; CAG46548.1; -; mRNA.
EMBL; AK291274; BAF83963.1; -; mRNA.
EMBL; AY219042; AAO25653.1; ALT_INIT; Genomic_DNA.
EMBL; AC073342; AAP22346.1; ALT_INIT; Genomic_DNA.
EMBL; AC073342; AAP22347.1; -; Genomic_DNA.
EMBL; AC073342; AAP22348.1; -; Genomic_DNA.
EMBL; AC073342; AAP22349.1; ALT_INIT; Genomic_DNA.
EMBL; CH471198; EAW51863.1; -; Genomic_DNA.
EMBL; CH471198; EAW51867.1; -; Genomic_DNA.
EMBL; CH471198; EAW51870.1; -; Genomic_DNA.
EMBL; BC002427; AAH02427.2; -; mRNA.
EMBL; BT007240; AAP35904.1; -; mRNA.
EMBL; AB209640; BAD92877.1; ALT_INIT; mRNA.
CCDS; CCDS5879.1; -. [P42575-1]
PIR; A54821; A54821.
RefSeq; NP_001215.1; NM_001224.4.
RefSeq; NP_116764.2; NM_032982.3. [P42575-1]
RefSeq; NP_116765.2; NM_032983.3.
UniGene; Hs.368982; -.
PDB; 1PYO; X-ray; 1.65 A; A/C=167-333, B/D=348-452.
PDB; 2P2C; X-ray; 3.24 A; A/C/E/G/I/K=167-333, B/D/F/H/J/L=348-452.
PDB; 3R5J; X-ray; 1.77 A; A/C=175-333, B/D=349-452.
PDB; 3R6G; X-ray; 2.07 A; A/C=175-333, B/D=349-452.
PDB; 3R6L; X-ray; 1.90 A; A/C=175-333, B/D=349-452.
PDB; 3R7B; X-ray; 1.80 A; A/C=175-333, B/D=349-452.
PDB; 3R7N; X-ray; 2.33 A; A/C=175-333, B/D=349-452.
PDB; 3R7S; X-ray; 2.25 A; A/C=175-333, B/D=349-452.
PDB; 3RJM; X-ray; 2.55 A; A/C=167-333, B/D=348-452.
PDBsum; 1PYO; -.
PDBsum; 2P2C; -.
PDBsum; 3R5J; -.
PDBsum; 3R6G; -.
PDBsum; 3R6L; -.
PDBsum; 3R7B; -.
PDBsum; 3R7N; -.
PDBsum; 3R7S; -.
PDBsum; 3RJM; -.
ProteinModelPortal; P42575; -.
SMR; P42575; -.
BioGrid; 107285; 32.
IntAct; P42575; 12.
MINT; MINT-150255; -.
STRING; 9606.ENSP00000312664; -.
BindingDB; P42575; -.
ChEMBL; CHEMBL4884; -.
GuidetoPHARMACOLOGY; 1618; -.
MEROPS; C14.006; -.
iPTMnet; P42575; -.
PhosphoSitePlus; P42575; -.
BioMuta; CASP2; -.
DMDM; 83300977; -.
EPD; P42575; -.
MaxQB; P42575; -.
PaxDb; P42575; -.
PeptideAtlas; P42575; -.
PRIDE; P42575; -.
DNASU; 835; -.
Ensembl; ENST00000310447; ENSP00000312664; ENSG00000106144. [P42575-1]
GeneID; 835; -.
KEGG; hsa:835; -.
UCSC; uc003wco.3; human. [P42575-1]
CTD; 835; -.
DisGeNET; 835; -.
GeneCards; CASP2; -.
HGNC; HGNC:1503; CASP2.
HPA; CAB012175; -.
HPA; HPA050678; -.
MIM; 600639; gene.
neXtProt; NX_P42575; -.
OpenTargets; ENSG00000106144; -.
PharmGKB; PA26086; -.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00760000118912; -.
HOVERGEN; HBG103962; -.
InParanoid; P42575; -.
KO; K02186; -.
OMA; VMVLMTH; -.
OrthoDB; EOG091G05YD; -.
PhylomeDB; P42575; -.
TreeFam; TF102023; -.
BRENDA; 3.4.22.55; 2681.
Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
Reactome; R-HSA-205025; NADE modulates death signalling.
Reactome; R-HSA-6803207; TP53 Regulates Transcription of Caspase Activators and Caspases.
SIGNOR; P42575; -.
ChiTaRS; CASP2; human.
EvolutionaryTrace; P42575; -.
GeneWiki; Caspase_2; -.
GenomeRNAi; 835; -.
PMAP-CutDB; P42575; -.
PRO; PR:P42575; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000106144; -.
CleanEx; HS_CASP2; -.
ExpressionAtlas; P42575; baseline and differential.
Genevisible; P42575; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016020; C:membrane; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005634; C:nucleus; TAS:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IBA:GO_Central.
GO; GO:0019899; F:enzyme binding; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0019904; F:protein domain specific binding; IPI:BHF-UCL.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; TAS:Reactome.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
GO; GO:0097190; P:apoptotic signaling pathway; TAS:UniProtKB.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; IMP:UniProtKB.
GO; GO:0035234; P:ectopic germ cell programmed cell death; IEA:Ensembl.
GO; GO:0097194; P:execution phase of apoptosis; TAS:UniProtKB.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; TAS:UniProtKB.
GO; GO:0001554; P:luteolysis; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; NAS:UniProtKB.
GO; GO:0003407; P:neural retina development; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0016485; P:protein processing; IDA:BHF-UCL.
GO; GO:0042981; P:regulation of apoptotic process; TAS:Reactome.
CDD; cd00032; CASc; 1.
InterPro; IPR001315; CARD.
InterPro; IPR029030; Caspase-like_dom.
InterPro; IPR033139; Caspase_cys_AS.
InterPro; IPR016129; Caspase_his_AS.
InterPro; IPR011029; DEATH-like_dom.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
Pfam; PF00619; CARD; 1.
PRINTS; PR00376; IL1BCENZYME.
SMART; SM00114; CARD; 1.
SMART; SM00115; CASc; 1.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF52129; SSF52129; 1.
PROSITE; PS50209; CARD; 1.
PROSITE; PS01122; CASPASE_CYS; 1.
PROSITE; PS01121; CASPASE_HIS; 1.
PROSITE; PS50207; CASPASE_P10; 1.
PROSITE; PS50208; CASPASE_P20; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
Complete proteome; Hydrolase; Phosphoprotein; Polymorphism; Protease;
Reference proteome; Thiol protease; Zymogen.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
PROPEP 2 169
/FTId=PRO_0000004541.
CHAIN 170 325 Caspase-2 subunit p18.
/FTId=PRO_0000004542.
PROPEP 326 333
/FTId=PRO_0000004543.
CHAIN 334 452 Caspase-2 subunit p13.
/FTId=PRO_0000004544.
CHAIN 348 452 Caspase-2 subunit p12.
/FTId=PRO_0000004545.
DOMAIN 32 121 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
ACT_SITE 277 277 {ECO:0000250}.
ACT_SITE 320 320 {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 157 157 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 340 340 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
VAR_SEQ 1 31 Missing (in isoform 2).
{ECO:0000303|PubMed:8087842,
ECO:0000303|Ref.3}.
/FTId=VSP_000801.
VAR_SEQ 1 17 Missing (in isoform 3).
{ECO:0000303|PubMed:11156409}.
/FTId=VSP_046280.
VAR_SEQ 107 108 RE -> HS (in isoform 3).
{ECO:0000303|PubMed:11156409}.
/FTId=VSP_046281.
VAR_SEQ 109 452 Missing (in isoform 3).
{ECO:0000303|PubMed:11156409}.
/FTId=VSP_046282.
VAR_SEQ 323 452 DETDRGVDQQDGKNHAGSPGCEESDAGKEKLPKMRLPTRSD
MICGYACLKGTAAMRNTKRGSWYIEALAQVFSERACDMHVA
DMLVKVNALIKDREGYAPGTEFHRCKEMSEYCSTLCRHLYL
FPGHPPT -> GGAIGSLGHLLLFTAATASLAL (in
isoform 2). {ECO:0000303|PubMed:8087842,
ECO:0000303|Ref.3}.
/FTId=VSP_000802.
VARIANT 105 105 A -> G (in dbSNP:rs4647298).
/FTId=VAR_055621.
VARIANT 172 172 V -> L (in dbSNP:rs4647297).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.5, ECO:0000269|Ref.9}.
/FTId=VAR_016334.
VARIANT 178 178 P -> A (in dbSNP:rs4647298).
{ECO:0000269|Ref.5}.
/FTId=VAR_016335.
VARIANT 441 441 R -> G (in dbSNP:rs4647338).
{ECO:0000269|Ref.5}.
/FTId=VAR_016336.
MUTAGEN 320 320 C->S: Loss of function.
MUTAGEN 369 369 A->T: Loss of function.
CONFLICT 309 322 QNKPKMFFIQACRG -> EEVTSLSILSAFVT (in Ref.
10; BAD92877). {ECO:0000305}.
HELIX 181 187 {ECO:0000244|PDB:1PYO}.
HELIX 188 190 {ECO:0000244|PDB:1PYO}.
STRAND 197 206 {ECO:0000244|PDB:1PYO}.
STRAND 212 214 {ECO:0000244|PDB:1PYO}.
HELIX 222 235 {ECO:0000244|PDB:1PYO}.
STRAND 238 245 {ECO:0000244|PDB:1PYO}.
HELIX 248 259 {ECO:0000244|PDB:1PYO}.
HELIX 262 265 {ECO:0000244|PDB:1PYO}.
STRAND 267 276 {ECO:0000244|PDB:1PYO}.
STRAND 282 284 {ECO:0000244|PDB:1PYO}.
STRAND 290 292 {ECO:0000244|PDB:1PYO}.
HELIX 293 299 {ECO:0000244|PDB:1PYO}.
TURN 302 304 {ECO:0000244|PDB:1PYO}.
HELIX 306 308 {ECO:0000244|PDB:1PYO}.
STRAND 313 319 {ECO:0000244|PDB:1PYO}.
STRAND 321 324 {ECO:0000244|PDB:1PYO}.
STRAND 363 370 {ECO:0000244|PDB:1PYO}.
STRAND 377 379 {ECO:0000244|PDB:3R5J}.
TURN 380 382 {ECO:0000244|PDB:1PYO}.
HELIX 385 397 {ECO:0000244|PDB:1PYO}.
TURN 398 400 {ECO:0000244|PDB:1PYO}.
HELIX 403 415 {ECO:0000244|PDB:1PYO}.
TURN 425 428 {ECO:0000244|PDB:1PYO}.
STRAND 434 437 {ECO:0000244|PDB:1PYO}.
STRAND 440 442 {ECO:0000244|PDB:3R7S}.
SEQUENCE 452 AA; 50685 MW; 6EF0ED05EF808385 CRC64;
MAAPSAGSWS TFQHKELMAA DRGRRILGVC GMHPHHQETL KKNRVVLAKQ LLLSELLEHL
LEKDIITLEM RELIQAKVGS FSQNVELLNL LPKRGPQAFD AFCEALRETK QGHLEDMLLT
TLSGLQHVLP PLSCDYDLSL PFPVCESCPL YKKLRLSTDT VEHSLDNKDG PVCLQVKPCT
PEFYQTHFQL AYRLQSRPRG LALVLSNVHF TGEKELEFRS GGDVDHSTLV TLFKLLGYDV
HVLCDQTAQE MQEKLQNFAQ LPAHRVTDSC IVALLSHGVE GAIYGVDGKL LQLQEVFQLF
DNANCPSLQN KPKMFFIQAC RGDETDRGVD QQDGKNHAGS PGCEESDAGK EKLPKMRLPT
RSDMICGYAC LKGTAAMRNT KRGSWYIEAL AQVFSERACD MHVADMLVKV NALIKDREGY
APGTEFHRCK EMSEYCSTLC RHLYLFPGHP PT


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