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Caspase-8 (CASP-8) (EC 3.4.22.61) (Apoptotic cysteine protease) (Apoptotic protease Mch-5) (CAP4) (FADD-homologous ICE/ced-3-like protease) (FADD-like ICE) (FLICE) (ICE-like apoptotic protease 5) (MORT1-associated ced-3 homolog) (MACH) [Cleaved into: Caspase-8 subunit p18; Caspase-8 subunit p10]

 CASP8_HUMAN             Reviewed;         479 AA.
Q14790; O14676; Q14791; Q14792; Q14793; Q14794; Q14795; Q14796;
Q15780; Q15806; Q53TT5; Q8TDI1; Q8TDI2; Q8TDI3; Q8TDI4; Q8TDI5;
Q96T22; Q9C0K4; Q9UQ81;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
03-JUL-2019, entry version 231.
RecName: Full=Caspase-8;
Short=CASP-8;
EC=3.4.22.61;
AltName: Full=Apoptotic cysteine protease;
AltName: Full=Apoptotic protease Mch-5;
AltName: Full=CAP4;
AltName: Full=FADD-homologous ICE/ced-3-like protease;
AltName: Full=FADD-like ICE;
Short=FLICE;
AltName: Full=ICE-like apoptotic protease 5;
AltName: Full=MORT1-associated ced-3 homolog;
Short=MACH;
Contains:
RecName: Full=Caspase-8 subunit p18;
Contains:
RecName: Full=Caspase-8 subunit p10;
Flags: Precursor;
Name=CASP8; Synonyms=MCH5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 5; 6; 7 AND 8).
TISSUE=B-cell, and Thymus;
PubMed=8681376; DOI=10.1016/S0092-8674(00)81265-9;
Boldin M.P., Goncharov T.M., Goltsev Y.V., Wallach D.;
"Involvement of MACH, a novel MORT1/FADD-interacting protease, in
Fas/APO-1- and TNF receptor-induced cell death.";
Cell 85:803-815(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
PubMed=8681377; DOI=10.1016/S0092-8674(00)81266-0;
Muzio M., Chinnaiyan A.M., Kischkel F.C., O'Rourke K., Shevchenko A.,
Ni J., Scaffidi C., Bretz J.D., Zhang M., Gentz R., Mann M.,
Krammer P.H., Peter M.E., Dixit V.M.;
"FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited
to the CD95 (Fas/APO-1) death-inducing signaling complex.";
Cell 85:817-827(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND VARIANT HIS-285.
TISSUE=T-cell;
PubMed=8755496; DOI=10.1073/pnas.93.15.7464;
Fernandes-Alnemri T., Armstrong R.C., Krebs J.F., Srinivasula S.M.,
Wang L., Bullrich F., Fritz L.C., Trapani J.A., Tomaselli K.J.,
Litwack G., Alnemri E.S.;
"In vitro activation of CPP32 and Mch3 by Mch4, a novel human
apoptotic cysteine protease containing two FADD-like domains.";
Proc. Natl. Acad. Sci. U.S.A. 93:7464-7469(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT HIS-285.
PubMed=9228018; DOI=10.1074/jbc.272.30.18542;
Srinivasula S.M., Ahmad M., Ottilie S., Bullrich F., Banks S.,
Wang Y., Fernandes-Alnemri T., Croce C.M., Litwack G., Tomaselli K.J.,
Armstrong R.C., Alnemri E.S.;
"FLAME-1, a novel FADD-like anti-apoptotic molecule that regulates
Fas/TNFR1-induced apoptosis.";
J. Biol. Chem. 272:18542-18545(1997).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9931493; DOI=10.1016/S0378-1119(98)00565-4;
Grenet J., Teitz T., Wei T., Valentine V., Kidd V.J.;
"Structure and chromosome localization of the human CASP8 gene.";
Gene 226:225-232(1999).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HIS-285.
PubMed=11161814; DOI=10.1006/geno.2000.6392;
Hadano S., Yanagisawa Y., Skaug J., Fichter K., Nasir J.,
Martindale D., Koop B.F., Scherer S.W., Nicholson D.W., Rouleau G.A.,
Ikeda J.-E., Hayden M.R.;
"Cloning and characterization of three novel genes, ALS2CR1, ALS2CR2,
and ALS2CR3, in the juvenile amyotrophic lateral sclerosis (ALS2)
critical region at chromosome 2q33-q34: candidate genes for ALS2.";
Genomics 71:200-213(2001).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), AND FUNCTION (ISOFORM 7).
TISSUE=Leukocyte;
PubMed=12010809; DOI=10.1182/blood.V99.11.4070;
Himeji D., Horiuchi T., Tsukamoto H., Hayashi K., Watanabe T.,
Harada M.;
"Characterization of caspase-8L: a novel isoform of caspase-8 that
behaves as an inhibitor of the caspase cascade.";
Blood 99:4070-4078(2002).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 9), AND INTERACTION OF
ISOFORM 9 WITH BCAP31 AT THE ENDOPLASMIC RETICULUM.
PubMed=11917123; DOI=10.1073/pnas.072088099;
Breckenridge D.G., Nguyen M., Kuppig S., Reth M., Shore G.C.;
"The procaspase-8 isoform, procaspase-8L, recruited to the BAP31
complex at the endoplasmic reticulum.";
Proc. Natl. Acad. Sci. U.S.A. 99:4331-4336(2002).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-219 AND HIS-285.
NIEHS SNPs program;
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
TISSUE=Leukocyte;
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).
[12]
PARTIAL PROTEIN SEQUENCE, AND PROTEOLYTIC PROCESSING.
PubMed=8962078; DOI=10.1073/pnas.93.25.14486;
Srinivasula S.M., Ahmad M., Fernandes-Alnemri T., Litwack G.,
Alnemri E.S.;
"Molecular ordering of the Fas-apoptotic pathway: the Fas/APO-1
protease Mch5 is a CrmA-inhibitable protease that activates multiple
Ced-3/ICE-like cysteine proteases.";
Proc. Natl. Acad. Sci. U.S.A. 93:14486-14491(1996).
[13]
FUNCTION.
PubMed=9006941; DOI=10.1074/jbc.272.5.2952;
Muzio M., Salvesen G.S., Dixit V.M.;
"FLICE induced apoptosis in a cell-free system. Cleavage of caspase
zymogens.";
J. Biol. Chem. 272:2952-2956(1997).
[14]
PROTEOLYTIC PROCESSING.
PubMed=9184224; DOI=10.1093/emboj/16.10.2794;
Medema J.P., Scaffidi C., Kischkel F.C., Shevchenko A., Mann M.,
Krammer P.H., Peter M.E.;
"FLICE is activated by association with the CD95 death-inducing
signaling complex (DISC).";
EMBO J. 16:2794-2804(1997).
[15]
CHARACTERIZATION (ISOFORM 7).
PubMed=10860845; DOI=10.1006/bbrc.2000.2841;
Horiuchi T., Himeji D., Tsukamoto H., Harashima S., Hashimura C.,
Hayashi K.;
"Dominant expression of a novel splice variant of caspase-8 in human
peripheral blood lymphocytes.";
Biochem. Biophys. Res. Commun. 272:877-881(2000).
[16]
INTERACTION WITH BCL2; BCL2L1 AND BCAP31.
PubMed=9334338; DOI=10.1083/jcb.139.2.327;
Ng F.W.H., Nguyen M., Kwan T., Branton P.E., Nicholson D.W.,
Cromlish J.A., Shore G.C.;
"p28 Bap31, a Bcl-2/Bcl-XL- and procaspase-8-associated protein in the
endoplasmic reticulum.";
J. Cell Biol. 139:327-338(1997).
[17]
INTERACTION WITH PEA15.
PubMed=10442631; DOI=10.1038/sj.onc.1202831;
Condorelli G., Vigliotta G., Cafieri A., Trencia A., Andalo P.,
Oriente F., Miele C., Caruso M., Formisano P., Beguinot F.;
"PED/PEA-15: an anti-apoptotic molecule that regulates FAS/TNFR1-
induced apoptosis.";
Oncogene 18:4409-4415(1999).
[18]
INTERACTION WITH HUMAN CYTOMEGALOVIRUS/HHV-5 PROTEIN UL36 (MICROBIAL
INFECTION).
PubMed=11427719; DOI=10.1073/pnas.141108798;
Skaletskaya A., Bartle L.M., Chittenden T., McCormick A.L.,
Mocarski E.S., Goldmacher V.S.;
"A cytomegalovirus-encoded inhibitor of apoptosis that suppresses
caspase-8 activation.";
Proc. Natl. Acad. Sci. U.S.A. 98:7829-7834(2001).
[19]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[20]
INTERACTION WITH NOL3.
PubMed=15509781; DOI=10.1128/MCB.24.22.9763-9770.2004;
Jo D.G., Jun J.I., Chang J.W., Hong Y.M., Song S., Cho D.H.,
Shim S.M., Lee H.J., Cho C., Kim D.H., Jung Y.K.;
"Calcium binding of ARC mediates regulation of caspase 8 and cell
death.";
Mol. Cell. Biol. 24:9763-9770(2004).
[21]
INTERACTION WITH RFFL AND RNF34.
PubMed=15069192; DOI=10.1073/pnas.0307459101;
McDonald E.R. III, El-Deiry W.S.;
"Suppression of caspase-8- and -10-associated RING proteins results in
sensitization to death ligands and inhibition of tumor cell growth.";
Proc. Natl. Acad. Sci. U.S.A. 101:6170-6175(2004).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-334, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[23]
MUTAGENESIS OF ASP-73.
PubMed=15592525; DOI=10.1038/sj.onc.1208186;
Jun J.-I., Chung C.-W., Lee H.-J., Pyo J.-O., Lee K.N., Kim N.-S.,
Kim Y.S., Yoo H.-S., Lee T.-H., Kim E., Jung Y.-K.;
"Role of FLASH in caspase-8-mediated activation of NF-kappaB:
dominant-negative function of FLASH mutant in NF-kappaB signaling
pathway.";
Oncogene 24:688-696(2005).
[24]
INTERACTION WITH MOLLUSCUM CONTAGIOSUM VIRUS PROTEIN MC160 (MICROBIAL
INFECTION).
PubMed=16378960; DOI=10.1128/JVI.80.2.578-586.2006;
Nichols D.B., Shisler J.L.;
"The MC160 protein expressed by the dermatotropic poxvirus molluscum
contagiosum virus prevents tumor necrosis factor alpha-induced NF-
kappaB activation via inhibition of I kappa kinase complex
formation.";
J. Virol. 80:578-586(2006).
[25]
INTERACTION WITH CASP8P2.
PubMed=17245429; DOI=10.1038/sj.emboj.7601504;
Milovic-Holm K., Krieghoff E., Jensen K., Will H., Hofmann T.G.;
"FLASH links the CD95 signaling pathway to the cell nucleus and
nuclear bodies.";
EMBO J. 26:391-401(2007).
[26]
PHOSPHORYLATION AT SER-387 BY CDK1.
PubMed=20937773; DOI=10.1128/MCB.00731-10;
Matthess Y., Raab M., Sanhaji M., Lavrik I.N., Strebhardt K.;
"Cdk1/cyclin B1 controls Fas-mediated apoptosis by regulating caspase-
8 activity.";
Mol. Cell. Biol. 30:5726-5740(2010).
[27]
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).
[28]
INTERACTION WITH E.COLI NLEF (MICROBIAL INFECTION), CATALYTIC
ACTIVITY, FUNCTION, AND ACTIVITY REGULATION.
PubMed=23516580; DOI=10.1371/journal.pone.0058937;
Blasche S., Mortl M., Steuber H., Siszler G., Nisa S., Schwarz F.,
Lavrik I., Gronewold T.M., Maskos K., Donnenberg M.S., Ullmann D.,
Uetz P., Kogl M.;
"The E. coli effector protein NleF is a caspase inhibitor.";
PLoS ONE 8:E58937-E58937(2013).
[29]
INTERACTION WITH UBR2, AND MUTAGENESIS OF CYS-360.
PubMed=28602583; DOI=10.1016/j.devcel.2017.05.013;
Weaver B.P., Weaver Y.M., Mitani S., Han M.;
"Coupled Caspase and N-End Rule Ligase Activities Allow Recognition
and Degradation of Pluripotency Factor LIN-28 during Non-Apoptotic
Development.";
Dev. Cell 41:665-673(2017).
[30]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
PubMed=10508784; DOI=10.1016/S0969-2126(99)80179-8;
Blanchard H., Kodandapani L., Mittl P.R.E., Di Marco S., Krebs J.F.,
Wu J.C., Tomaselli K.J., Gruetter M.G.;
"The three-dimensional structure of caspase-8: an initiator enzyme in
apoptosis.";
Structure 7:1125-1133(1999).
[31]
X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 211-479, AND SUBUNIT.
PubMed=10508785; DOI=10.1016/S0969-2126(99)80180-4;
Watt W., Koeplinger K.A., Mildner A.M., Heinrikson R.L.,
Tomasselli A.G., Watenpaugh K.D.;
"The atomic-resolution structure of human caspase-8, a key activator
of apoptosis.";
Structure 7:1135-1143(1999).
[32]
VARIANT CASP8D TRP-248.
PubMed=12353035; DOI=10.1038/nature01063;
Chun H.J., Zheng L., Ahmad M., Wang J., Speirs C.K., Siegel R.M.,
Dale J.K., Puck J., Davis J., Hall C.G., Skoda-Smith S.,
Atkinson T.P., Straus S.E., Lenardo M.J.;
"Pleiotropic defects in lymphocyte activation caused by caspase-8
mutations lead to human immunodeficiency.";
Nature 419:395-399(2002).
[33]
VARIANT HIS-285, AND PROTECTION AGAINST BREAST CANCER.
PubMed=15601643; DOI=10.1093/jnci/dji001;
MacPherson G., Healey C.S., Teare M.D., Balasubramanian S.P.,
Reed M.W.R., Pharoah P.D., Ponder B.A.J., Meuth M.,
Bhattacharyya N.P., Cox A.;
"Association of a common variant of the CASP8 gene with reduced risk
of breast cancer.";
J. Natl. Cancer Inst. 96:1866-1869(2004).
[34]
VARIANT HIS-285, AND PROTECTION AGAINST BREAST CANCER.
PubMed=17293864; DOI=10.1038/ng1981;
The Kathleen Cunningham foundation consortium for research into familial breast cancer;
Breast cancer association consortium;
Cox A., Dunning A.M., Garcia-Closas M., Balasubramanian S.,
Reed M.W.R., Pooley K.A., Scollen S., Baynes C., Ponder B.A.J.,
Chanock S., Lissowska J., Brinton L., Peplonska B., Southey M.C.,
Hopper J.L., McCredie M.R.E., Giles G.G., Fletcher O., Johnson N.,
dos Santos Silva I., Gibson L., Bojesen S.E., Nordestgaard B.G.,
Axelsson C.K., Torres D., Hamann U., Justenhoven C., Brauch H.,
Chang-Claude J., Kropp S., Risch A., Wang-Gohrke S., Schuermann P.,
Bogdanova N., Doerk T., Fagerholm R., Aaltonen K., Blomqvist C.,
Nevanlinna H., Seal S., Renwick A., Stratton M.R., Rahman N.,
Sangrajrang S., Hughes D., Odefrey F., Brennan P., Spurdle A.B.,
Chenevix-Trench G., Beesley J., Mannermaa A., Hartikainen J.,
Kataja V., Kosma V.M., Couch F.J., Olson J.E., Goode E.L., Broeks A.,
Schmidt M.K., Hogervorst F.B.L., Van't Veer L.J., Kang D., Yoo K.-Y.,
Noh D.-Y., Ahn S.-H., Wedren S., Hall P., Low Y.-L., Liu J.,
Milne R.L., Ribas G., Gonzalez-Neira A., Benitez J., Sigurdson A.J.,
Stredrick D.L., Alexander B.H., Struewing J.P., Pharoah P.D.P.,
Easton D.F.;
"A common coding variant in CASP8 is associated with breast cancer
risk.";
Nat. Genet. 39:352-358(2007).
[35]
ERRATUM.
The Kathleen Cunningham foundation consortium for research into familial breast cancer;
Breast cancer association consortium;
Cox A., Dunning A.M., Garcia-Closas M., Balasubramanian S.,
Reed M.W.R., Pooley K.A., Scollen S., Baynes C., Ponder B.A.J.,
Chanock S., Lissowska J., Brinton L., Peplonska B., Southey M.C.,
Hopper J.L., McCredie M.R.E., Giles G.G., Fletcher O., Johnson N.,
dos Santos Silva I., Gibson L., Bojesen S.E., Nordestgaard B.G.,
Axelsson C.K., Torres D., Hamann U., Justenhoven C., Brauch H.,
Chang-Claude J., Kropp S., Risch A., Wang-Gohrke S., Schuermann P.,
Bogdanova N., Doerk T., Fagerholm R., Aaltonen K., Blomqvist C.,
Nevanlinna H., Seal S., Renwick A., Stratton M.R., Rahman N.,
Sangrajrang S., Hughes D., Odefrey F., Brennan P., Spurdle A.B.,
Chenevix-Trench G., Beesley J., Mannermaa A., Hartikainen J.,
Kataja V., Kosma V.M., Couch F.J., Olson J.E., Goode E.L., Broeks A.,
Schmidt M.K., Hogervorst F.B.L., Van't Veer L.J., Kang D., Yoo K.-Y.,
Noh D.-Y., Ahn S.-H., Wedren S., Hall P., Low Y.-L., Liu J.,
Milne R.L., Ribas G., Gonzalez-Neira A., Benitez J., Sigurdson A.J.,
Stredrick D.L., Alexander B.H., Struewing J.P., Pharoah P.D.P.,
Easton D.F.;
Nat. Genet. 39:688-688(2007).
[36]
INVOLVEMENT IN PROTECTION AGAINST LUNG CANCER.
PubMed=17450141; DOI=10.1038/ng2030;
Sun T., Gao Y., Tan W., Ma S., Shi Y., Yao J., Guo Y., Yang M.,
Zhang X., Zhang Q., Zeng C., Lin D.;
"A six-nucleotide insertion-deletion polymorphism in the CASP8
promoter is associated with susceptibility to multiple cancers.";
Nat. Genet. 39:605-613(2007).
[37]
VARIANT HIS-285, AND RISK FACTOR FOR CUTANEOUS MELANOMA.
PubMed=18563783; DOI=10.1002/humu.20803;
Li C., Zhao H., Hu Z., Liu Z., Wang L.-E., Gershenwald J.E.,
Prieto V.G., Lee J.E., Duvic M., Grimm E.A., Wei Q.;
"Genetic variants and haplotypes of the caspase-8 and caspase-10 genes
contribute to susceptibility to cutaneous melanoma.";
Hum. Mutat. 29:1443-1451(2008).
-!- FUNCTION: Most upstream protease of the activation cascade of
caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A
induced cell death. Binding to the adapter molecule FADD recruits
it to either receptor. The resulting aggregate called death-
inducing signaling complex (DISC) performs CASP8 proteolytic
activation. The active dimeric enzyme is then liberated from the
DISC and free to activate downstream apoptotic proteases.
Proteolytic fragments of the N-terminal propeptide (termed CAP3,
CAP5 and CAP6) are likely retained in the DISC. Cleaves and
activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May
participate in the GZMB apoptotic pathways. Cleaves ADPRT.
Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC.
Likely target for the cowpox virus CRMA death inhibitory protein.
Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic
site and may interfere with the pro-apoptotic activity of the
complex. {ECO:0000269|PubMed:23516580,
ECO:0000269|PubMed:9006941}.
-!- CATALYTIC ACTIVITY:
Reaction=Strict requirement for Asp at position P1 and has a
preferred cleavage sequence of (Leu/Asp/Val)-Glu-Thr-Asp-|-
(Gly/Ser/Ala).; EC=3.4.22.61;
Evidence={ECO:0000269|PubMed:23516580};
-!- ACTIVITY REGULATION: Inhibited by the effector protein NleF that
is produced by pathogenic E.coli; this inhibits apoptosis.
{ECO:0000269|PubMed:23516580}.
-!- SUBUNIT: Heterotetramer that consists of two anti-parallel
arranged heterodimers, each one formed by a 18 kDa (p18) and a 10
kDa (p10) subunit (PubMed:10508784). Interacts with FADD, CFLAR
and PEA15 (PubMed:10442631). Isoform 9 interacts at the
endoplasmic reticulum with a complex containing BCAP31, BAP29,
BCL2 and/or BCL2L1 (PubMed:11917123, PubMed:9334338). Interacts
with TNFAIP8L2 (By similarity). Interacts with CASP8AP2
(PubMed:16378960). Interacts with RFFL and RNF34; negatively
regulate CASP8 through proteasomal degradation (PubMed:15069192).
Interacts with NOL3; decreases CASP8 activity in a mitochondria
localization- and phosphorylation-dependent manner and this
interaction is dissociated by calcium (PubMed:15509781). Interacts
with UBR2 (PubMed:28602583). {ECO:0000250|UniProtKB:O89110,
ECO:0000250|UniProtKB:Q9JHX4, ECO:0000269|PubMed:10442631,
ECO:0000269|PubMed:10508784, ECO:0000269|PubMed:11917123,
ECO:0000269|PubMed:15069192, ECO:0000269|PubMed:15509781,
ECO:0000269|PubMed:16378960, ECO:0000269|PubMed:28602583,
ECO:0000269|PubMed:9334338}.
-!- SUBUNIT: (Microbial infection) Interacts with human
cytomegalovirus/HHV-5 protein vICA/UL36; this interaction inhibits
CASP8 activation. {ECO:0000269|PubMed:11427719}.
-!- SUBUNIT: (Microbial infection) Interacts with NleF from pathogenic
E.coli. {ECO:0000269|PubMed:23516580}.
-!- SUBUNIT: (Microbial infection) Interacts with molluscum
contagiosum virus protein MC160. {ECO:0000269|PubMed:16378960}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-78060, EBI-78060;
P10275:AR; NbExp=3; IntAct=EBI-78060, EBI-608057;
P51572:BCAP31; NbExp=3; IntAct=EBI-78060, EBI-77683;
Q92851:CASP10; NbExp=3; IntAct=EBI-78060, EBI-495095;
Q9UKL3:CASP8AP2; NbExp=3; IntAct=EBI-78060, EBI-2339650;
O15519:CFLAR; NbExp=9; IntAct=EBI-78060, EBI-514941;
O15519-1:CFLAR; NbExp=3; IntAct=EBI-15777741, EBI-4567563;
Q13618:CUL3; NbExp=6; IntAct=EBI-78060, EBI-456129;
Q13158:FADD; NbExp=44; IntAct=EBI-78060, EBI-494804;
P25445:FAS; NbExp=14; IntAct=EBI-78060, EBI-494743;
P25445-1:FAS; NbExp=3; IntAct=EBI-78060, EBI-15749113;
P48023:FASLG; NbExp=5; IntAct=EBI-78060, EBI-495538;
Q13418:ILK; NbExp=2; IntAct=EBI-78060, EBI-747644;
Q9UDY8:MALT1; NbExp=10; IntAct=EBI-78060, EBI-1047372;
O60936:NOL3; NbExp=3; IntAct=EBI-78060, EBI-740992;
P29350:PTPN6; NbExp=3; IntAct=EBI-78060, EBI-78260;
Q13546:RIPK1; NbExp=27; IntAct=EBI-78060, EBI-358507;
Q969K3:RNF34; NbExp=3; IntAct=EBI-78060, EBI-2340642;
P21580:TNFAIP3; NbExp=3; IntAct=EBI-78060, EBI-527670;
O00220:TNFRSF10A; NbExp=9; IntAct=EBI-78060, EBI-518861;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=9;
Name=1; Synonyms=Alpha-1;
IsoId=Q14790-1; Sequence=Displayed;
Name=2; Synonyms=Alpha-2, MCH5-beta;
IsoId=Q14790-2; Sequence=VSP_000810;
Name=3; Synonyms=Alpha-3;
IsoId=Q14790-3; Sequence=VSP_000813;
Name=4; Synonyms=Alpha-4;
IsoId=Q14790-4; Sequence=VSP_000809, VSP_000810;
Name=5; Synonyms=Beta-1;
IsoId=Q14790-5; Sequence=VSP_000814, VSP_000815;
Name=6; Synonyms=Beta-2;
IsoId=Q14790-6; Sequence=VSP_000811, VSP_000812;
Name=7; Synonyms=Beta-3, 8L;
IsoId=Q14790-7; Sequence=VSP_000816, VSP_000817;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=8; Synonyms=Beta-4;
IsoId=Q14790-8; Sequence=VSP_000810, VSP_000816, VSP_000817;
Name=9; Synonyms=8L;
IsoId=Q14790-9; Sequence=VSP_000808;
Note=Ref.8 (AAL87628) sequence is in conflict in position:
14:K->R. {ECO:0000305};
-!- TISSUE SPECIFICITY: Isoform 1, isoform 5 and isoform 7 are
expressed in a wide variety of tissues. Highest expression in
peripheral blood leukocytes, spleen, thymus and liver. Barely
detectable in brain, testis and skeletal muscle.
-!- DOMAIN: Isoform 9 contains a N-terminal extension that is required
for interaction with the BCAP31 complex.
-!- PTM: Generation of the subunits requires association with the
death-inducing signaling complex (DISC), whereas additional
processing is likely due to the autocatalytic activity of the
activated protease. GZMB and CASP10 can be involved in these
processing events. {ECO:0000269|PubMed:8962078,
ECO:0000269|PubMed:9184224}.
-!- PTM: Phosphorylation on Ser-387 during mitosis by CDK1 inhibits
activation by proteolysis and prevents apoptosis. This
phosphorylation occurs in cancer cell lines, as well as in primary
breast tissues and lymphocytes. {ECO:0000269|PubMed:20937773}.
-!- POLYMORPHISM: Genetic variations in CASP8 are associated with
reduced risk of lung cancer [MIM:211980] in a population of Han
Chinese subjects. Genetic variations are also associated with
decreased risk of cancer of various other forms including
esophageal, gastric, colorectal, cervical, and breast, acting in
an allele dose-dependent manner. {ECO:0000269|PubMed:17450141}.
-!- DISEASE: Caspase-8 deficiency (CASP8D) [MIM:607271]: Disorder
resembling autoimmune lymphoproliferative syndrome (ALPS). It is
characterized by lymphadenopathy, splenomegaly, and defective
CD95-induced apoptosis of peripheral blood lymphocytes (PBLs). It
leads to defects in activation of T-lymphocytes, B-lymphocytes,
and natural killer cells leading to immunodeficiency characterized
by recurrent sinopulmonary and herpes simplex virus infections and
poor responses to immunization. {ECO:0000269|PubMed:12353035}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA66858.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
Sequence=CAA66859.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=CASP8base; Note=CASP8 mutation db;
URL="http://structure.bmc.lu.se/idbase/CASP8base/";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/casp8/";
-----------------------------------------------------------------------
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EMBL; X98172; CAA66853.1; -; mRNA.
EMBL; X98173; CAA66854.1; -; mRNA.
EMBL; X98174; CAA66855.1; -; mRNA.
EMBL; X98175; CAA66856.1; -; mRNA.
EMBL; X98176; CAA66857.1; -; mRNA.
EMBL; X98177; CAA66858.1; ALT_SEQ; mRNA.
EMBL; X98178; CAA66859.1; ALT_SEQ; mRNA.
EMBL; U58143; AAC50602.1; -; mRNA.
EMBL; U60520; AAC50645.1; -; mRNA.
EMBL; AF009620; AAB70913.1; -; mRNA.
EMBL; AF102146; AAD24962.1; -; Genomic_DNA.
EMBL; AF102139; AAD24962.1; JOINED; Genomic_DNA.
EMBL; AF102140; AAD24962.1; JOINED; Genomic_DNA.
EMBL; AF102141; AAD24962.1; JOINED; Genomic_DNA.
EMBL; AF102142; AAD24962.1; JOINED; Genomic_DNA.
EMBL; AF102143; AAD24962.1; JOINED; Genomic_DNA.
EMBL; AF102144; AAD24962.1; JOINED; Genomic_DNA.
EMBL; AF102145; AAD24962.1; JOINED; Genomic_DNA.
EMBL; AB038985; BAB32555.1; -; Genomic_DNA.
EMBL; AF380342; AAK57437.1; -; mRNA.
EMBL; AF422925; AAL87628.1; -; mRNA.
EMBL; AF422926; AAL87629.1; -; mRNA.
EMBL; AF422927; AAL87630.1; -; mRNA.
EMBL; AF422928; AAL87631.1; -; mRNA.
EMBL; AF422929; AAL87632.1; -; mRNA.
EMBL; DQ355026; ABC67468.1; -; Genomic_DNA.
EMBL; AC007256; AAY24225.1; -; Genomic_DNA.
EMBL; BC028223; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS2342.1; -. [Q14790-1]
CCDS; CCDS2343.1; -. [Q14790-2]
CCDS; CCDS2345.1; -. [Q14790-5]
CCDS; CCDS42798.1; -. [Q14790-9]
CCDS; CCDS42799.1; -. [Q14790-4]
RefSeq; NP_001073593.1; NM_001080124.1. [Q14790-2]
RefSeq; NP_001073594.1; NM_001080125.1. [Q14790-9]
RefSeq; NP_001219.2; NM_001228.4. [Q14790-4]
RefSeq; NP_203519.1; NM_033355.3. [Q14790-1]
RefSeq; NP_203520.1; NM_033356.3. [Q14790-2]
RefSeq; NP_203522.1; NM_033358.3. [Q14790-5]
RefSeq; XP_005246943.1; XM_005246886.1. [Q14790-1]
RefSeq; XP_005246944.1; XM_005246887.1. [Q14790-1]
RefSeq; XP_005246945.1; XM_005246888.1. [Q14790-1]
RefSeq; XP_005246946.1; XM_005246889.1. [Q14790-1]
RefSeq; XP_005246947.1; XM_005246890.3. [Q14790-1]
RefSeq; XP_005246948.1; XM_005246891.4. [Q14790-1]
RefSeq; XP_005246949.1; XM_005246892.1. [Q14790-2]
RefSeq; XP_006712852.1; XM_006712789.1. [Q14790-1]
RefSeq; XP_006712853.1; XM_006712790.3. [Q14790-1]
RefSeq; XP_006712856.1; XM_006712793.2. [Q14790-5]
PDB; 1F9E; X-ray; 2.90 A; A/C/E/G/I/K=222-374, B/D/F/H/J/L=390-478.
PDB; 1I4E; X-ray; 3.00 A; B=222-479.
PDB; 1QDU; X-ray; 2.80 A; A/C/E/G/I/K=222-374, B/D/F/H/J/L=390-477.
PDB; 1QTN; X-ray; 1.20 A; A=211-374, B=385-479.
PDB; 2C2Z; X-ray; 1.95 A; A=218-374, B=376-479.
PDB; 2FUN; X-ray; 3.00 A; B/D=222-479.
PDB; 2K7Z; NMR; -; A=217-479.
PDB; 2Y1L; X-ray; 1.80 A; A/C=218-374, B/D=376-479.
PDB; 3H11; X-ray; 1.90 A; B=217-479.
PDB; 3KJN; X-ray; 1.80 A; A=211-374, B=385-479.
PDB; 3KJQ; X-ray; 1.80 A; A=211-374, B=385-479.
PDB; 4JJ7; X-ray; 1.18 A; A=217-479.
PDB; 4PRZ; X-ray; 2.12 A; A=217-479.
PDB; 4PS1; X-ray; 1.73 A; A/B/C/D=217-479.
PDB; 4ZBW; X-ray; 2.20 A; A/B=2-188.
PDB; 5H31; X-ray; 3.17 A; A/B/C/D=1-188.
PDB; 5H33; X-ray; 3.60 A; A/B=1-188.
PDB; 5JQE; X-ray; 3.16 A; A=1-186.
PDB; 5L08; EM; 4.60 A; A/B/C/D/E/F/G/H/I=1-184.
PDBsum; 1F9E; -.
PDBsum; 1I4E; -.
PDBsum; 1QDU; -.
PDBsum; 1QTN; -.
PDBsum; 2C2Z; -.
PDBsum; 2FUN; -.
PDBsum; 2K7Z; -.
PDBsum; 2Y1L; -.
PDBsum; 3H11; -.
PDBsum; 3KJN; -.
PDBsum; 3KJQ; -.
PDBsum; 4JJ7; -.
PDBsum; 4PRZ; -.
PDBsum; 4PS1; -.
PDBsum; 4ZBW; -.
PDBsum; 5H31; -.
PDBsum; 5H33; -.
PDBsum; 5JQE; -.
PDBsum; 5L08; -.
SMR; Q14790; -.
BioGrid; 107291; 154.
ComplexPortal; CPX-1907; Ripoptosome.
ComplexPortal; CPX-975; Caspase-8 complex.
CORUM; Q14790; -.
DIP; DIP-30915N; -.
ELM; Q14790; -.
IntAct; Q14790; 122.
MINT; Q14790; -.
STRING; 9606.ENSP00000351273; -.
BindingDB; Q14790; -.
ChEMBL; CHEMBL3776; -.
GuidetoPHARMACOLOGY; 1624; -.
MEROPS; C14.009; -.
iPTMnet; Q14790; -.
PhosphoSitePlus; Q14790; -.
SwissPalm; Q14790; -.
BioMuta; CASP8; -.
DMDM; 2493531; -.
EPD; Q14790; -.
jPOST; Q14790; -.
MaxQB; Q14790; -.
PaxDb; Q14790; -.
PeptideAtlas; Q14790; -.
PRIDE; Q14790; -.
ProteomicsDB; 60172; -.
ProteomicsDB; 60173; -. [Q14790-2]
ProteomicsDB; 60174; -. [Q14790-3]
ProteomicsDB; 60175; -. [Q14790-4]
ProteomicsDB; 60176; -. [Q14790-5]
ProteomicsDB; 60177; -. [Q14790-6]
ProteomicsDB; 60178; -. [Q14790-7]
ProteomicsDB; 60179; -. [Q14790-8]
ProteomicsDB; 60180; -. [Q14790-9]
DNASU; 841; -.
Ensembl; ENST00000264274; ENSP00000264274; ENSG00000064012. [Q14790-3]
Ensembl; ENST00000264275; ENSP00000264275; ENSG00000064012. [Q14790-4]
Ensembl; ENST00000323492; ENSP00000325722; ENSG00000064012. [Q14790-2]
Ensembl; ENST00000358485; ENSP00000351273; ENSG00000064012. [Q14790-9]
Ensembl; ENST00000392258; ENSP00000376087; ENSG00000064012. [Q14790-5]
Ensembl; ENST00000392263; ENSP00000376091; ENSG00000064012. [Q14790-2]
Ensembl; ENST00000432109; ENSP00000412523; ENSG00000064012. [Q14790-1]
GeneID; 841; -.
KEGG; hsa:841; -.
UCSC; uc002uxo.2; human. [Q14790-1]
CTD; 841; -.
DisGeNET; 841; -.
GeneCards; CASP8; -.
HGNC; HGNC:1509; CASP8.
HPA; CAB002047; -.
HPA; HPA001302; -.
HPA; HPA005688; -.
HPA; HPA006191; -.
MalaCards; CASP8; -.
MIM; 211980; phenotype.
MIM; 601763; gene.
MIM; 607271; phenotype.
neXtProt; NX_Q14790; -.
OpenTargets; ENSG00000064012; -.
Orphanet; 210159; Adult hepatocellular carcinoma.
Orphanet; 275517; Autoimmune lymphoproliferative syndrome with recurrent viral infections.
PharmGKB; PA26092; -.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00940000160319; -.
InParanoid; Q14790; -.
KO; K04398; -.
OMA; CLYNIGE; -.
OrthoDB; 939331at2759; -.
PhylomeDB; Q14790; -.
TreeFam; TF102023; -.
BRENDA; 3.4.22.61; 2681.
Reactome; R-HSA-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-HSA-140534; Caspase activation via Death Receptors in the presence of ligand.
Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
Reactome; R-HSA-2562578; TRIF-mediated programmed cell death.
Reactome; R-HSA-264870; Caspase-mediated cleavage of cytoskeletal proteins.
Reactome; R-HSA-3371378; Regulation by c-FLIP.
Reactome; R-HSA-5213460; RIPK1-mediated regulated necrosis.
Reactome; R-HSA-5218900; CASP8 activity is inhibited.
Reactome; R-HSA-5357786; TNFR1-induced proapoptotic signaling.
Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
Reactome; R-HSA-5660668; CLEC7A/inflammasome pathway.
Reactome; R-HSA-5675482; Regulation of necroptotic cell death.
Reactome; R-HSA-69416; Dimerization of procaspase-8.
Reactome; R-HSA-75108; Activation, myristolyation of BID and translocation to mitochondria.
Reactome; R-HSA-75153; Apoptotic execution phase.
Reactome; R-HSA-75157; FasL/ CD95L signaling.
Reactome; R-HSA-75158; TRAIL signaling.
Reactome; R-HSA-9013957; TLR3-mediated TICAM1-dependent programmed cell death.
Reactome; R-HSA-933543; NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
SignaLink; Q14790; -.
SIGNOR; Q14790; -.
ChiTaRS; CASP8; human.
EvolutionaryTrace; Q14790; -.
GeneWiki; Caspase_8; -.
GenomeRNAi; 841; -.
PMAP-CutDB; Q14790; -.
PRO; PR:Q14790; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000064012; Expressed in 196 organ(s), highest expression level in small intestine Peyer's patch.
ExpressionAtlas; Q14790; baseline and differential.
Genevisible; Q14790; HS.
GO; GO:0031265; C:CD95 death-inducing signaling complex; IDA:UniProtKB.
GO; GO:0044297; C:cell body; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0031264; C:death-inducing signaling complex; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; TAS:ProtInc.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0032991; C:protein-containing complex; IDA:ARUK-UCL.
GO; GO:0097342; C:ripoptosome; IDA:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
GO; GO:0097199; F:cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0008234; F:cysteine-type peptidase activity; TAS:ProtInc.
GO; GO:0035877; F:death effector domain binding; IPI:UniProtKB.
GO; GO:0005123; F:death receptor binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008233; F:peptidase activity; IDA:BHF-UCL.
GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
GO; GO:0097110; F:scaffold protein binding; IPI:ParkinsonsUK-UCL.
GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; IDA:BHF-UCL.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0097296; P:activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; TAS:Reactome.
GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
GO; GO:0097190; P:apoptotic signaling pathway; IMP:BHF-UCL.
GO; GO:0042113; P:B cell activation; TAS:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:Reactome.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0071550; P:death-inducing signaling complex assembly; TAS:Reactome.
GO; GO:0097194; P:execution phase of apoptosis; IMP:UniProtKB.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IBA:GO_Central.
GO; GO:0030225; P:macrophage differentiation; IBA:GO_Central.
GO; GO:0030101; P:natural killer cell activation; TAS:UniProtKB.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; TAS:Reactome.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IMP:ARUK-UCL.
GO; GO:0045651; P:positive regulation of macrophage differentiation; IMP:UniProtKB.
GO; GO:1901216; P:positive regulation of neuron death; IEA:Ensembl.
GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
GO; GO:0045862; P:positive regulation of proteolysis; IDA:BHF-UCL.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IMP:BHF-UCL.
GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; TAS:Reactome.
GO; GO:0060544; P:regulation of necroptotic process; TAS:Reactome.
GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0032025; P:response to cobalt ion; IEA:Ensembl.
GO; GO:0009409; P:response to cold; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0034612; P:response to tumor necrosis factor; IMP:BHF-UCL.
GO; GO:0039650; P:suppression by virus of host cysteine-type endopeptidase activity involved in apoptotic process; TAS:Reactome.
GO; GO:0060715; P:syncytiotrophoblast cell differentiation involved in labyrinthine layer development; TAS:UniProtKB.
GO; GO:0042110; P:T cell activation; TAS:UniProtKB.
GO; GO:0034138; P:toll-like receptor 3 signaling pathway; TAS:Reactome.
GO; GO:0036462; P:TRAIL-activated apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome.
CDD; cd00032; CASc; 1.
InterPro; IPR029030; Caspase-like_dom_sf.
InterPro; IPR033139; Caspase_cys_AS.
InterPro; IPR016129; Caspase_his_AS.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR001875; DED_dom.
InterPro; IPR002398; Pept_C14.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
PANTHER; PTHR10454; PTHR10454; 1.
Pfam; PF01335; DED; 2.
PRINTS; PR00376; IL1BCENZYME.
SMART; SM00115; CASc; 1.
SMART; SM00031; DED; 2.
SUPFAM; SSF47986; SSF47986; 2.
SUPFAM; SSF52129; SSF52129; 1.
PROSITE; PS01122; CASPASE_CYS; 1.
PROSITE; PS01121; CASPASE_HIS; 1.
PROSITE; PS50207; CASPASE_P10; 1.
PROSITE; PS50208; CASPASE_P20; 1.
PROSITE; PS50168; DED; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
Complete proteome; Cytoplasm; Direct protein sequencing;
Disease mutation; Host-virus interaction; Hydrolase; Phosphoprotein;
Polymorphism; Protease; Reference proteome; Repeat; Thiol protease;
Zymogen.
PROPEP 1 216
/FTId=PRO_0000004628.
CHAIN 217 374 Caspase-8 subunit p18.
/FTId=PRO_0000004629.
PROPEP 375 384
/FTId=PRO_0000004630.
CHAIN 385 479 Caspase-8 subunit p10.
/FTId=PRO_0000004631.
DOMAIN 2 80 DED 1. {ECO:0000255|PROSITE-
ProRule:PRU00065}.
DOMAIN 100 177 DED 2. {ECO:0000255|PROSITE-
ProRule:PRU00065}.
ACT_SITE 317 317
ACT_SITE 360 360
MOD_RES 188 188 Phosphoserine.
{ECO:0000250|UniProtKB:O89110}.
MOD_RES 211 211 Phosphoserine.
{ECO:0000250|UniProtKB:O89110}.
MOD_RES 224 224 N6-acetyllysine.
{ECO:0000250|UniProtKB:O89110}.
MOD_RES 334 334 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 387 387 Phosphoserine; by CDK1.
{ECO:0000269|PubMed:20937773}.
VAR_SEQ 1 1 M -> MEGGRRARVVIESKRNFFLGAFPTPFPAEHVELGRL
GDSETAMVPGKGGADYILLPFKKM (in isoform 9).
{ECO:0000303|PubMed:11917123}.
/FTId=VSP_000808.
VAR_SEQ 102 102 R -> RFHFCRMSWAEANSQCQTQSVPFWRRVDHLLIR
(in isoform 4).
{ECO:0000303|PubMed:8755496}.
/FTId=VSP_000809.
VAR_SEQ 184 267 Missing (in isoform 3).
{ECO:0000303|PubMed:8681376}.
/FTId=VSP_000813.
VAR_SEQ 184 220 ERSSSLEGSPDEFSNGEELCGVMTISDSPREQDSESQ ->
DFGQSLPNEKQTSGILSDHQQSQFCKSTGESAQTSQH (in
isoform 6). {ECO:0000303|PubMed:8681376}.
/FTId=VSP_000811.
VAR_SEQ 184 198 Missing (in isoform 2, isoform 4 and
isoform 8). {ECO:0000303|PubMed:11917123,
ECO:0000303|PubMed:8681376,
ECO:0000303|PubMed:8755496,
ECO:0000303|PubMed:9228018}.
/FTId=VSP_000810.
VAR_SEQ 199 235 GEELCGVMTISDSPREQDSESQTLDKVYQMKSKPRGY ->
DFGQSLPNEKQTSGILSDHQQSQFCKSTGESAQTSQH (in
isoform 5). {ECO:0000303|PubMed:8681376}.
/FTId=VSP_000814.
VAR_SEQ 221 479 Missing (in isoform 6).
{ECO:0000303|PubMed:8681376}.
/FTId=VSP_000812.
VAR_SEQ 236 479 Missing (in isoform 5).
{ECO:0000303|PubMed:8681376}.
/FTId=VSP_000815.
VAR_SEQ 269 276 ALTTTFEE -> TVEPKREK (in isoform 7 and
isoform 8). {ECO:0000303|PubMed:12010809,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8681376}.
/FTId=VSP_000816.
VAR_SEQ 277 479 Missing (in isoform 7 and isoform 8).
{ECO:0000303|PubMed:12010809,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8681376}.
/FTId=VSP_000817.
VARIANT 219 219 S -> T (in dbSNP:rs35976359).
{ECO:0000269|Ref.9}.
/FTId=VAR_025816.
VARIANT 248 248 R -> W (in CASP8D; dbSNP:rs17860424).
{ECO:0000269|PubMed:12353035}.
/FTId=VAR_014204.
VARIANT 285 285 D -> H (associated with protection
against breast cancer; also associated
with a lower risk of cutaneous melanoma;
dbSNP:rs1045485).
{ECO:0000269|PubMed:11161814,
ECO:0000269|PubMed:15601643,
ECO:0000269|PubMed:17293864,
ECO:0000269|PubMed:18563783,
ECO:0000269|PubMed:8755496,
ECO:0000269|PubMed:9228018,
ECO:0000269|Ref.9}.
/FTId=VAR_020127.
MUTAGEN 73 73 D->A: Abolishes binding to FLASH. Induces
NF-kappa-B activation.
{ECO:0000269|PubMed:15592525}.
MUTAGEN 360 360 C->S: Abolishes interaction with UBR2.
{ECO:0000269|PubMed:28602583}.
MUTAGEN 387 387 S->A: Impaired CDK1-mediated
phosphorylation and enhanced apoptosis.
CONFLICT 294 294 E -> D (in Ref. 5; AAD24962).
{ECO:0000305}.
CONFLICT 331 331 A -> P (in Ref. 2; AAC50602 and 5;
AAD24962). {ECO:0000305}.
CONFLICT 343 344 LK -> FG (in Ref. 8; AAL87631).
{ECO:0000305}.
HELIX 3 13 {ECO:0000244|PDB:4ZBW}.
HELIX 16 25 {ECO:0000244|PDB:4ZBW}.
TURN 26 29 {ECO:0000244|PDB:4ZBW}.
HELIX 32 34 {ECO:0000244|PDB:4ZBW}.
TURN 35 37 {ECO:0000244|PDB:5H31}.
HELIX 41 50 {ECO:0000244|PDB:4ZBW}.
STRAND 53 55 {ECO:0000244|PDB:4ZBW}.
HELIX 60 68 {ECO:0000244|PDB:4ZBW}.
HELIX 72 79 {ECO:0000244|PDB:4ZBW}.
HELIX 83 91 {ECO:0000244|PDB:4ZBW}.
TURN 93 95 {ECO:0000244|PDB:4ZBW}.
HELIX 100 111 {ECO:0000244|PDB:4ZBW}.
HELIX 114 127 {ECO:0000244|PDB:4ZBW}.
HELIX 139 148 {ECO:0000244|PDB:4ZBW}.
STRAND 151 153 {ECO:0000244|PDB:5JQE}.
HELIX 158 165 {ECO:0000244|PDB:4ZBW}.
HELIX 169 180 {ECO:0000244|PDB:4ZBW}.
STRAND 230 232 {ECO:0000244|PDB:3H11}.
STRAND 235 240 {ECO:0000244|PDB:4JJ7}.
HELIX 245 250 {ECO:0000244|PDB:4JJ7}.
HELIX 252 254 {ECO:0000244|PDB:4JJ7}.
STRAND 255 257 {ECO:0000244|PDB:2K7Z}.
HELIX 263 276 {ECO:0000244|PDB:4JJ7}.
STRAND 280 286 {ECO:0000244|PDB:4JJ7}.
HELIX 289 301 {ECO:0000244|PDB:4JJ7}.
HELIX 304 306 {ECO:0000244|PDB:1QDU}.
STRAND 310 316 {ECO:0000244|PDB:4JJ7}.
STRAND 322 324 {ECO:0000244|PDB:4JJ7}.
STRAND 326 328 {ECO:0000244|PDB:1I4E}.
STRAND 330 332 {ECO:0000244|PDB:4JJ7}.
HELIX 333 337 {ECO:0000244|PDB:4JJ7}.
HELIX 338 340 {ECO:0000244|PDB:4JJ7}.
TURN 342 344 {ECO:0000244|PDB:4JJ7}.
HELIX 346 348 {ECO:0000244|PDB:4JJ7}.
STRAND 353 359 {ECO:0000244|PDB:4JJ7}.
STRAND 361 364 {ECO:0000244|PDB:4JJ7}.
STRAND 369 371 {ECO:0000244|PDB:1QDU}.
STRAND 377 379 {ECO:0000244|PDB:2K7Z}.
STRAND 392 394 {ECO:0000244|PDB:1QDU}.
TURN 395 398 {ECO:0000244|PDB:4JJ7}.
STRAND 399 405 {ECO:0000244|PDB:4JJ7}.
STRAND 412 414 {ECO:0000244|PDB:3H11}.
TURN 415 417 {ECO:0000244|PDB:4JJ7}.
HELIX 420 432 {ECO:0000244|PDB:4JJ7}.
HELIX 433 435 {ECO:0000244|PDB:4JJ7}.
HELIX 439 450 {ECO:0000244|PDB:4JJ7}.
TURN 456 459 {ECO:0000244|PDB:4JJ7}.
STRAND 465 468 {ECO:0000244|PDB:4JJ7}.
STRAND 471 473 {ECO:0000244|PDB:1QDU}.
SEQUENCE 479 AA; 55391 MW; 7A5FEAA6B39B582F CRC64;
MDFSRNLYDI GEQLDSEDLA SLKFLSLDYI PQRKQEPIKD ALMLFQRLQE KRMLEESNLS
FLKELLFRIN RLDLLITYLN TRKEEMEREL QTPGRAQISA YRVMLYQISE EVSRSELRSF
KFLLQEEISK CKLDDDMNLL DIFIEMEKRV ILGEGKLDIL KRVCAQINKS LLKIINDYEE
FSKERSSSLE GSPDEFSNGE ELCGVMTISD SPREQDSESQ TLDKVYQMKS KPRGYCLIIN
NHNFAKAREK VPKLHSIRDR NGTHLDAGAL TTTFEELHFE IKPHDDCTVE QIYEILKIYQ
LMDHSNMDCF ICCILSHGDK GIIYGTDGQE APIYELTSQF TGLKCPSLAG KPKVFFIQAC
QGDNYQKGIP VETDSEEQPY LEMDLSSPQT RYIPDEADFL LGMATVNNCV SYRNPAEGTW
YIQSLCQSLR ERCPRGDDIL TILTEVNYEV SNKDDKKNMG KQMPQPTFTL RKKLVFPSD


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Related Genes :
[CASP8 MCH5] Caspase-8 (CASP-8) (EC 3.4.22.61) (Apoptotic cysteine protease) (Apoptotic protease Mch-5) (CAP4) (FADD-homologous ICE/ced-3-like protease) (FADD-like ICE) (FLICE) (ICE-like apoptotic protease 5) (MORT1-associated ced-3 homolog) (MACH) [Cleaved into: Caspase-8 subunit p18; Caspase-8 subunit p10]
[CASP10 MCH4] Caspase-10 (CASP-10) (EC 3.4.22.63) (Apoptotic protease Mch-4) (FAS-associated death domain protein interleukin-1B-converting enzyme 2) (FLICE2) (ICE-like apoptotic protease 4) [Cleaved into: Caspase-10 subunit p23/17; Caspase-10 subunit p12]
[CASP7 MCH3] Caspase-7 (CASP-7) (EC 3.4.22.60) (Apoptotic protease Mch-3) (CMH-1) (ICE-like apoptotic protease 3) (ICE-LAP3) [Cleaved into: Caspase-7 subunit p20; Caspase-7 subunit p11]
[CASP6 MCH2] Caspase-6 (CASP-6) (EC 3.4.22.59) (Apoptotic protease Mch-2) [Cleaved into: Caspase-6 subunit p18; Caspase-6 subunit p11]
[Casp6] Caspase-6 (CASP-6) (EC 3.4.22.59) (Apoptotic protease Mch-2) [Cleaved into: Caspase-6 subunit p18; Caspase-6 subunit p11]
[CASP4 ICH2] Caspase-4 (CASP-4) (EC 3.4.22.57) (ICE and Ced-3 homolog 2) (ICH-2) (ICE(rel)-II) (Mih1) (Protease TX) [Cleaved into: Caspase-4 subunit 1; Caspase-4 subunit 2]
[CFLAR CASH CASP8AP1 CLARP MRIT] CASP8 and FADD-like apoptosis regulator (Caspase homolog) (CASH) (Caspase-eight-related protein) (Casper) (Caspase-like apoptosis regulatory protein) (CLARP) (Cellular FLICE-like inhibitory protein) (c-FLIP) (FADD-like antiapoptotic molecule 1) (FLAME-1) (Inhibitor of FLICE) (I-FLICE) (MACH-related inducer of toxicity) (MRIT) (Usurpin) [Cleaved into: CASP8 and FADD-like apoptosis regulator subunit p43; CASP8 and FADD-like apoptosis regulator subunit p12]
[Casp7 Lice2 Mch3] Caspase-7 (CASP-7) (EC 3.4.22.60) (Apoptotic protease Mch-3) (Cysteine protease LICE2) [Cleaved into: Caspase-7 subunit p20; Caspase-7 subunit p11]
[Casp6 Mch2] Caspase-6 (CASP-6) (EC 3.4.22.59) (Apoptotic protease Mch-2) [Cleaved into: Caspase-6 subunit p18; Caspase-6 subunit p11]
[Casp2 Ich1 Nedd-2 Nedd2] 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]
[Casp4 Casp11 Caspl Ich3] Caspase-4 (CASP-4) (EC 3.4.22.64) (Caspase-11) (CASP-11) (Protease ICH-3) [Cleaved into: Caspase-4 subunit p10; Caspase-4 subunit p20]
[Dredd DCP2 CG7486] Caspase-8 (EC 3.4.22.61) (Death-related ced-3/NEDD2-like protein) [Cleaved into: Caspase-8 subunit p15; Caspase-8 subunit p10]
[Cflar Cash] CASP8 and FADD-like apoptosis regulator (Caspase homolog) (CASH) (Caspase-eight-related protein) (Casper) (Caspase-like apoptosis regulatory protein) (CLARP) (Cellular FLICE-like inhibitory protein) (c-FLIP) (FADD-like antiapoptotic molecule 1) (FLAME-1) (Inhibitor of FLICE) (I-FLICE) (MACH-related inducer of toxicity) (MRIT) (Usurpin) [Cleaved into: CASP8 and FADD-like apoptosis regulator subunit p43; CASP8 and FADD-like apoptosis regulator subunit p12]
[CASP3 CPP32] Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[CASP2 ICH1 NEDD2] 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]
[Casp3 Cpp32] Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (LICE) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[Casp2 Ich1] Caspase-2 (CASP-2) (EC 3.4.22.55) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12]
[Casp3 Cpp32] Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (IRP) (LICE) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[CASP14] Caspase-14 (CASP-14) (EC 3.4.22.-) [Cleaved into: Caspase-14 subunit p17, mature form; Caspase-14 subunit p10, mature form; Caspase-14 subunit p20, intermediate form; Caspase-14 subunit p8, intermediate form]
[Drice ICE CG7788] Caspase (EC 3.4.22.-) (drICE) [Cleaved into: Caspase subunit p21; Caspase subunit p12]
[ced-3 C48D1.2] Cell death protein 3 (EC 3.4.22.60) (Caspase ced-3) [Cleaved into: Cell death protein 3 subunit p17; Cell death protein 3 subunit p15; Cell death protein 3 subunit p13]
[FADD MORT1 GIG3] FAS-associated death domain protein (FAS-associating death domain-containing protein) (Growth-inhibiting gene 3 protein) (Mediator of receptor induced toxicity) (Protein FADD)
[CASP7 MCH3] Caspase-7 (CASP-7) (EC 3.4.22.60) (Apoptotic protease Mch-3) (ICE-like apoptotic protease 3) (ICE-LAP3) (SREBP cleavage activity 2) (SCA-2) [Cleaved into: Caspase-7 subunit p20; Caspase-7 subunit p11]
[Fadd Mort1] FAS-associated death domain protein (FAS-associating death domain-containing protein) (Mediator of receptor induced toxicity) (Protein FADD)
[NLRC4 CARD12 CLAN CLAN1 IPAF UNQ6189/PRO20215] NLR family CARD domain-containing protein 4 (CARD, LRR, and NACHT-containing protein) (Clan protein) (Caspase recruitment domain-containing protein 12) (Ice protease-activating factor) (Ipaf)
[rep 1a-1b] Replicase polyprotein 1ab (ORF1ab polyprotein) [Cleaved into: Nsp1 (EC 3.4.22.-); Nsp1-alpha papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-alpha); Nsp1-beta papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-beta); Nsp2 cysteine proteinase (EC 3.4.19.12) (EC 3.4.22.-) (CP2) (CP); Non-structural protein 3 (Nsp3); Serine protease nsp4 (3CLSP) (EC 3.4.21.-) (3C-like serine proteinase) (Nsp4); Non-structural protein 5-6-7 (Nsp5-6-7); Non-structural protein 5 (Nsp5); Non-structural protein 6 (Nsp6); Non-structural protein 7-alpha (Nsp7-alpha); Non-structural protein 7-beta (Nsp7-beta); Non-structural protein 8 (Nsp8); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Nsp9); Helicase nsp10 (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Nsp10); Non-structural protein 11 (Nsp11); Non-structural protein 12 (Nsp12)]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[BCL10 CIPER CLAP] B-cell lymphoma/leukemia 10 (B-cell CLL/lymphoma 10) (Bcl-10) (CARD-containing molecule enhancing NF-kappa-B) (CARD-like apoptotic protein) (hCLAP) (CED-3/ICH-1 prodomain homologous E10-like regulator) (CIPER) (Cellular homolog of vCARMEN) (cCARMEN) (Cellular-E10) (c-E10) (Mammalian CARD-containing adapter molecule E10) (mE10)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]

Bibliography :