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Caspase-1 (CASP-1) (EC 3.4.22.36) (Interleukin-1 beta convertase) (IL-1BC) (Interleukin-1 beta-converting enzyme) (ICE) (IL-1 beta-converting enzyme) (p45) [Cleaved into: Caspase-1 subunit p20; Caspase-1 subunit p10]

 CASP1_HUMAN             Reviewed;         404 AA.
P29466; B5MDZ1; Q53EY6; Q6DMQ1; Q6GSS3; Q6PI75; Q9UCN3;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
03-JUL-2019, entry version 215.
RecName: Full=Caspase-1;
Short=CASP-1;
EC=3.4.22.36;
AltName: Full=Interleukin-1 beta convertase;
Short=IL-1BC;
AltName: Full=Interleukin-1 beta-converting enzyme;
Short=ICE;
Short=IL-1 beta-converting enzyme;
AltName: Full=p45;
Contains:
RecName: Full=Caspase-1 subunit p20;
Contains:
RecName: Full=Caspase-1 subunit p10;
Flags: Precursor;
Name=CASP1; Synonyms=IL1BC, IL1BCE;
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 ALPHA), PARTIAL PROTEIN SEQUENCE,
ACTIVE SITE, AND FUNCTION.
PubMed=1574116; DOI=10.1038/356768a0;
Thornberry N.A., Bull H.G., Calaycay J.R., Chapman K.T., Howard A.D.,
Kostura M.J., Miller D.K., Molineaux S.M., Weidner J.R., Aunins J.,
Elliston K.O., Ayala J.M., Casano F.J., Chin J., Ding G.J.-F.,
Egger L.A., Gaffney E.P., Limjuco G., Palyha O.C., Raju M.,
Rolando A.M., Salley J.P., Yamin T.-T., Lee T.D., Shively J.E.,
McCross M., Mumford R.A., Schmidt J.A., Tocci M.J.;
"A novel heterodimeric cysteine protease is required for interleukin-1
beta processing in monocytes.";
Nature 356:768-774(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), AND PROTEIN SEQUENCE OF
120-142.
PubMed=1373520; DOI=10.1126/science.1373520;
Cerretti D.P., Kozlosky C.J., Mosley B., Nelson N., van Ness K.,
Greenstreet T.A., March C.J., Kronheim S.R., Druck T.,
Cannizzaro L.A., Huebner K., Black R.A.;
"Molecular cloning of the interleukin-1 beta converting enzyme.";
Science 256:97-100(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA; DELTA; EPSILON AND GAMMA),
ALTERNATIVE SPLICING, AND FUNCTION.
PubMed=7876192; DOI=10.1074/jbc.270.9.4312;
Alnemri E.S., Fernandes-Alnemri T., Litwack G.;
"Cloning and expression of four novel isoforms of human interleukin-1
beta converting enzyme with different apoptotic activities.";
J. Biol. Chem. 270:4312-4317(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 4-404 (ISOFORM BETA).
TISSUE=Testis;
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 32-404 (ISOFORM ALPHA), FUNCTION,
MUTAGENESIS OF CYS-285, ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
PubMed=15498465; DOI=10.1016/j.ygeno.2004.06.005;
Feng Q., Li P., Leung P.C.K., Auersperg N.;
"Caspase-1 zeta, a new splice variant of caspase-1 gene.";
Genomics 84:587-591(2004).
[8]
PROTEIN SEQUENCE OF 120-142.
PubMed=1321594; DOI=10.1016/0003-9861(92)90629-B;
Kronheim S.R., Mumma A., Greenstreet T., Glackin P.J., Van Ness K.,
March C.J., Black R.A.;
"Purification of interleukin-1 beta converting enzyme, the protease
that cleaves the interleukin-1 beta precursor.";
Arch. Biochem. Biophys. 296:698-703(1992).
[9]
INTERACTION WITH CARD18.
PubMed=11051551; DOI=10.1016/S0092-8674(00)00108-2;
Humke E.W., Shriver S.K., Starovasnik M.A., Fairbrother W.J.,
Dixit V.M.;
"ICEBERG: a novel inhibitor of interleukin-1beta generation.";
Cell 103:99-111(2000).
[10]
COMPONENT OF THE INFLAMMASOME.
PubMed=15030775; DOI=10.1016/S1074-7613(04)00046-9;
Agostini L., Martinon F., Burns K., McDermott M.F., Hawkins P.N.,
Tschopp J.;
"NALP3 forms an IL-1beta-processing inflammasome with increased
activity in Muckle-Wells autoinflammatory disorder.";
Immunity 20:319-325(2004).
[11]
INTERACTION WITH CARD17.
PubMed=15383541; DOI=10.1074/jbc.M407891200;
Lamkanfi M., Denecker G., Kalai M., D'hondt K., Meeus A., Declercq W.,
Saelens X., Vandenabeele P.;
"INCA, a novel human caspase recruitment domain protein that inhibits
interleukin-1beta generation.";
J. Biol. Chem. 279:51729-51738(2004).
[12]
INTERACTION WITH MEFV.
PubMed=16785446; DOI=10.1073/pnas.0602081103;
Chae J.J., Wood G., Masters S.L., Richard K., Park G., Smith B.J.,
Kastner D.L.;
"The B30.2 domain of pyrin, the familial Mediterranean fever protein,
interacts directly with caspase-1 to modulate IL-1beta production.";
Proc. Natl. Acad. Sci. U.S.A. 103:9982-9987(2006).
[13]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-285.
PubMed=20197547; DOI=10.1182/blood-2009-10-243444;
Weigert A., Cremer S., Schmidt M.V., von Knethen A., Angioni C.,
Geisslinger G., Bruene B.;
"Cleavage of sphingosine kinase 2 by caspase-1 provokes its release
from apoptotic cells.";
Blood 115:3531-3540(2010).
[14]
INDUCTION BY M.TUBERCULOSIS.
TISSUE=Macrophage;
PubMed=20148899; DOI=10.1111/j.1462-5822.2010.01450.x;
Mishra B.B., Moura-Alves P., Sonawane A., Hacohen N., Griffiths G.,
Moita L.F., Anes E.;
"Mycobacterium tuberculosis protein ESAT-6 is a potent activator of
the NLRP3/ASC inflammasome.";
Cell. Microbiol. 12:1046-1063(2010).
[15]
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).
[16]
FUNCTION.
PubMed=28314590; DOI=10.1016/j.immuni.2017.02.011;
Wang Y., Ning X., Gao P., Wu S., Sha M., Lv M., Zhou X., Gao J.,
Fang R., Meng G., Su X., Jiang Z.;
"Inflammasome activation triggers caspase-1-mediated cleavage of cGAS
to regulate responses to DNA virus infection.";
Immunity 46:393-404(2017).
[17]
INTERACTION WITH SERPINB1.
PubMed=30692621; DOI=10.1038/s41590-018-0303-z;
Choi Y.J., Kim S., Choi Y., Nielsen T.B., Yan J., Lu A., Ruan J.,
Lee H.R., Wu H., Spellberg B., Jung J.U.;
"SERPINB1-mediated checkpoint of inflammatory caspase activation.";
Nat. Immunol. 20:276-287(2019).
[18]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND SUBUNIT.
PubMed=8044845; DOI=10.1016/0092-8674(94)90303-4;
Walker N.P.C., Talanian R.V., Brady K.D., Dang L.C., Bump N.J.,
Ferenz C.R., Franklin S., Ghayur T., Hackett M.C., Hammill L.D.,
Herzog L., Hugunin M., Houy W., Mankovich J.A., McGuiness L.,
Orlewicz E., Paskind M., Pratt C.A., Reis P., Summani A.,
Terranova M., Welch J.P., Xiong L., Moeller A., Tracey D.E., Kamen R.,
Wong W.W.;
"Crystal structure of the cysteine protease interleukin-1 beta-
converting enzyme: a (p20/p10)2 homodimer.";
Cell 78:343-352(1994).
[19]
X-RAY CRYSTALLOGRAPHY (2.73 ANGSTROMS).
PubMed=9190289; DOI=10.1016/S1074-5521(97)90258-1;
Rano T.A., Timkey T., Peterson E.P., Rotonda J., Nicholson D.W.,
Becker J.W., Chapman K.T., Thornberry N.A.;
"A combinatorial approach for determining protease specificities:
application to interleukin-1beta converting enzyme (ICE).";
Chem. Biol. 4:149-155(1997).
[20]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
PubMed=9987822; DOI=10.1248/cpb.47.11;
Okamoto Y., Anan H., Nakai E., Morihira K., Yonetoku Y., Kurihara H.,
Sakashita H., Terai Y., Takeuchi M., Shibanuma T., Isomura Y.;
"Peptide based interleukin-1 beta converting enzyme (ICE) inhibitors:
synthesis, structure activity relationships and crystallographic study
of the ICE-inhibitor complex.";
Chem. Pharm. Bull. 47:11-21(1999).
[21]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 120-404 OF MUTANT ALA-285.
PubMed=15296730; DOI=10.1016/j.str.2004.05.010;
Romanowski M.J., Scheer J.M., O'Brien T., McDowell R.S.;
"Crystal structures of a ligand-free and malonate-bound human caspase-
1: implications for the mechanism of substrate binding.";
Structure 12:1361-1371(2004).
-!- FUNCTION: Thiol protease that cleaves IL-1 beta between an Asp and
an Ala, releasing the mature cytokine which is involved in a
variety of inflammatory processes. Important for defense against
pathogens. Cleaves and activates sterol regulatory element binding
proteins (SREBPs). Can also promote apoptosis. Upon inflammasome
activation, during DNA virus infection but not RNA virus
challenge, controls antiviral immunity through the cleavage of
CGAS, rendering it inactive (PubMed:28314590). In apoptotic cells,
cleaves SPHK2 which is released from cells and remains
enzymatically active extracellularly (PubMed:20197547).
{ECO:0000269|PubMed:15498465, ECO:0000269|PubMed:1574116,
ECO:0000269|PubMed:20197547, ECO:0000269|PubMed:28314590,
ECO:0000269|PubMed:7876192}.
-!- CATALYTIC ACTIVITY:
Reaction=Strict requirement for an Asp residue at position P1 and
has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|-.;
EC=3.4.22.36;
-!- ACTIVITY REGULATION: Specifically inhibited by the cowpox virus
Crma protein.
-!- SUBUNIT: Heterotetramer that consists of two anti-parallel
arranged heterodimers, each one formed by a 20 kDa (p20) and a 10
kDa (p10) subunit. The p20 subunit can also form a heterodimer
with the epsilon isoform which then has an inhibitory effect. May
be a component of the inflammasome, a protein complex which also
includes PYCARD, CARD8 and NALP2 and whose function would be the
activation of proinflammatory caspases. Both the p10 and p20
subunits interact with MEFV. Interacts with CARD17/INCA and
CARD18. Interacts with SERPINB1; this interaction regulates CASP1
activity. {ECO:0000269|PubMed:11051551,
ECO:0000269|PubMed:15383541, ECO:0000269|PubMed:16785446,
ECO:0000269|PubMed:30692621, ECO:0000269|PubMed:8044845,
ECO:0000269|PubMed:9987822}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-516667, EBI-516667;
Q5XLA6:CARD17; NbExp=3; IntAct=EBI-516667, EBI-16203934;
P57730:CARD18; NbExp=3; IntAct=EBI-516667, EBI-16203975;
P09038:FGF2; NbExp=2; IntAct=EBI-516667, EBI-977447;
P01583:IL1A; NbExp=3; IntAct=EBI-516667, EBI-1749782;
O15553:MEFV; NbExp=2; IntAct=EBI-516667, EBI-7644532;
O15553-2:MEFV; NbExp=3; IntAct=EBI-516667, EBI-15588296;
Q9NPP4:NLRC4; NbExp=4; IntAct=EBI-516667, EBI-1222527;
Q9C000:NLRP1; NbExp=3; IntAct=EBI-516667, EBI-1220518;
Q9HC29:NOD2; NbExp=4; IntAct=EBI-516667, EBI-7445625;
Q9ULZ3:PYCARD; NbExp=9; IntAct=EBI-516667, EBI-751215;
P58753-2:TIRAP; NbExp=5; IntAct=EBI-516667, EBI-528654;
Q08AM6:VAC14; NbExp=3; IntAct=EBI-516667, EBI-2107455;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20197547}.
Cell membrane {ECO:0000269|PubMed:20197547}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Additional isoforms seem to exist.;
Name=Alpha;
IsoId=P29466-1; Sequence=Displayed;
Name=Beta;
IsoId=P29466-2; Sequence=VSP_000798;
Name=Gamma;
IsoId=P29466-3; Sequence=VSP_000799;
Name=Delta;
IsoId=P29466-4; Sequence=VSP_000799, VSP_000800;
Note=Apoptosis inactive.;
Name=Epsilon;
IsoId=P29466-5; Sequence=VSP_000797;
Note=Apoptosis inactive.;
-!- TISSUE SPECIFICITY: Expressed in larger amounts in spleen and
lung. Detected in liver, heart, small intestine, colon, thymus,
prostate, skeletal muscle, peripheral blood leukocytes, kidney and
testis. No expression in the brain. {ECO:0000269|PubMed:15498465}.
-!- INDUCTION: Transcription and translation induced by M.tuberculosis
and a number of different M.tuberculosis components; EsxA is the
most potent activator tested (at protein level) (PubMed:20148899).
{ECO:0000269|PubMed:20148899}.
-!- PTM: The two subunits are derived from the precursor sequence by
an autocatalytic mechanism.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAT72297.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT72297.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CASP1ID145ch11q22.html";
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EMBL; X65019; CAA46153.1; -; mRNA.
EMBL; M87507; AAA66942.1; -; mRNA.
EMBL; U13697; AAC50107.1; -; mRNA.
EMBL; U13698; AAC50108.1; -; mRNA.
EMBL; U13699; AAC50109.1; -; mRNA.
EMBL; U13700; AAC50110.1; -; mRNA.
EMBL; AK223503; BAD97223.1; -; mRNA.
EMBL; AP001153; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC041689; AAH41689.1; -; mRNA.
EMBL; BC062327; AAH62327.1; -; mRNA.
EMBL; AY660536; AAT72297.1; ALT_SEQ; mRNA.
CCDS; CCDS53704.1; -. [P29466-3]
CCDS; CCDS8329.1; -. [P29466-2]
CCDS; CCDS8330.1; -. [P29466-1]
CCDS; CCDS8331.1; -. [P29466-4]
CCDS; CCDS8332.1; -. [P29466-5]
PIR; A54263; A42677.
PIR; A56084; A56084.
PIR; B56084; B56084.
PIR; C56084; C56084.
PIR; D56084; D56084.
RefSeq; NP_001214.1; NM_001223.4. [P29466-2]
RefSeq; NP_001244047.1; NM_001257118.2. [P29466-1]
RefSeq; NP_001244048.1; NM_001257119.2. [P29466-2]
RefSeq; NP_150634.1; NM_033292.3. [P29466-1]
RefSeq; NP_150635.1; NM_033293.3. [P29466-3]
RefSeq; NP_150636.1; NM_033294.3. [P29466-4]
RefSeq; NP_150637.1; NM_033295.3. [P29466-5]
PDB; 1BMQ; X-ray; 2.50 A; A=131-297, B=317-404.
PDB; 1IBC; X-ray; 2.73 A; A=104-297, B=317-404.
PDB; 1ICE; X-ray; 2.60 A; A=131-297, B=317-404.
PDB; 1RWK; X-ray; 2.30 A; A=120-297, B=317-404.
PDB; 1RWM; X-ray; 2.70 A; A=120-297, B=317-404.
PDB; 1RWN; X-ray; 2.00 A; A=120-297, B=317-404.
PDB; 1RWO; X-ray; 2.10 A; A=120-297, B=317-404.
PDB; 1RWP; X-ray; 2.20 A; A=120-297, B=317-404.
PDB; 1RWV; X-ray; 2.10 A; A=120-297, B=317-404.
PDB; 1RWW; X-ray; 2.80 A; A=120-297, B=317-404.
PDB; 1RWX; X-ray; 1.85 A; A=120-297, B=317-404.
PDB; 1SC1; X-ray; 2.60 A; A=120-297, B=317-404.
PDB; 1SC3; X-ray; 1.80 A; A=120-297, B=317-404.
PDB; 1SC4; X-ray; 2.10 A; A=120-297, B=317-404.
PDB; 2FQQ; X-ray; 3.30 A; A=120-297, B=317-404.
PDB; 2H48; X-ray; 2.20 A; A=120-297, B=317-404.
PDB; 2H4W; X-ray; 2.00 A; A=120-297, B=317-404.
PDB; 2H4Y; X-ray; 1.90 A; A=120-297, B=317-404.
PDB; 2H51; X-ray; 2.10 A; A=120-297, B=317-404.
PDB; 2H54; X-ray; 1.80 A; A=120-297, B=317-404.
PDB; 2HBQ; X-ray; 1.80 A; A=120-297, B=317-404.
PDB; 2HBR; X-ray; 2.20 A; A=120-297, B=317-404.
PDB; 2HBY; X-ray; 2.10 A; A=120-297, B=317-404.
PDB; 2HBZ; X-ray; 1.90 A; A=120-297, B=317-404.
PDB; 3D6F; X-ray; 1.90 A; A=120-297, B=317-404.
PDB; 3D6H; X-ray; 2.00 A; A=120-297, B=317-404.
PDB; 3D6M; X-ray; 1.80 A; A=120-297, B=317-404.
PDB; 3E4C; X-ray; 2.05 A; A/B=104-404.
PDB; 3NS7; X-ray; 2.60 A; A=136-297, B=317-404.
PDB; 5FNA; EM; 4.80 A; A/B/C/D/E/F/G/H=2-86.
PDB; 5MMV; X-ray; 2.15 A; A=120-297, B=317-404.
PDB; 5MTK; X-ray; 2.53 A; A=120-297, B=317-404.
PDB; 6BZ9; X-ray; 1.80 A; A=120-297, B=317-404.
PDB; 6F6R; X-ray; 1.80 A; A=118-297, B=317-404.
PDBsum; 1BMQ; -.
PDBsum; 1IBC; -.
PDBsum; 1ICE; -.
PDBsum; 1RWK; -.
PDBsum; 1RWM; -.
PDBsum; 1RWN; -.
PDBsum; 1RWO; -.
PDBsum; 1RWP; -.
PDBsum; 1RWV; -.
PDBsum; 1RWW; -.
PDBsum; 1RWX; -.
PDBsum; 1SC1; -.
PDBsum; 1SC3; -.
PDBsum; 1SC4; -.
PDBsum; 2FQQ; -.
PDBsum; 2H48; -.
PDBsum; 2H4W; -.
PDBsum; 2H4Y; -.
PDBsum; 2H51; -.
PDBsum; 2H54; -.
PDBsum; 2HBQ; -.
PDBsum; 2HBR; -.
PDBsum; 2HBY; -.
PDBsum; 2HBZ; -.
PDBsum; 3D6F; -.
PDBsum; 3D6H; -.
PDBsum; 3D6M; -.
PDBsum; 3E4C; -.
PDBsum; 3NS7; -.
PDBsum; 5FNA; -.
PDBsum; 5MMV; -.
PDBsum; 5MTK; -.
PDBsum; 6BZ9; -.
PDBsum; 6F6R; -.
SMR; P29466; -.
BioGrid; 107284; 44.
CORUM; P29466; -.
DIP; DIP-175N; -.
IntAct; P29466; 18.
MINT; P29466; -.
STRING; 9606.ENSP00000433138; -.
BindingDB; P29466; -.
ChEMBL; CHEMBL4801; -.
DrugBank; DB07744; 3-[2-(2-BENZYLOXYCARBONYLAMINO-3-METHYL-BUTYRYLAMINO)-PROPIONYLAMINO]-4-OXO-PENTANOIC ACID.
DrugBank; DB07916; 3-{6-[(8-HYDROXY-QUINOLINE-2-CARBONYL)-AMINO]-2-THIOPHEN-2-YL-HEXANOYLAMINO}-4-OXO-BUTYRI ACID.
DrugBank; DB05408; IDN-6556.
DrugBank; DB05301; LAX-101.
DrugBank; DB01017; Minocycline.
DrugBank; DB04875; Pralnacasan.
DrugBank; DB05507; VX-765.
GuidetoPHARMACOLOGY; 1617; -.
iPTMnet; P29466; -.
PhosphoSitePlus; P29466; -.
BioMuta; CASP1; -.
DMDM; 266321; -.
EPD; P29466; -.
jPOST; P29466; -.
MaxQB; P29466; -.
PaxDb; P29466; -.
PeptideAtlas; P29466; -.
PRIDE; P29466; -.
ProteomicsDB; 54571; -.
ProteomicsDB; 54572; -. [P29466-2]
ProteomicsDB; 54573; -. [P29466-3]
ProteomicsDB; 54574; -. [P29466-4]
ProteomicsDB; 54575; -. [P29466-5]
DNASU; 834; -.
Ensembl; ENST00000353247; ENSP00000344132; ENSG00000137752. [P29466-5]
Ensembl; ENST00000436863; ENSP00000410076; ENSG00000137752. [P29466-1]
Ensembl; ENST00000446369; ENSP00000403260; ENSG00000137752. [P29466-4]
Ensembl; ENST00000525825; ENSP00000434779; ENSG00000137752. [P29466-2]
Ensembl; ENST00000526568; ENSP00000434250; ENSG00000137752. [P29466-3]
Ensembl; ENST00000531166; ENSP00000434303; ENSG00000137752. [P29466-5]
Ensembl; ENST00000533400; ENSP00000433138; ENSG00000137752. [P29466-1]
Ensembl; ENST00000534497; ENSP00000436875; ENSG00000137752. [P29466-4]
GeneID; 834; -.
KEGG; hsa:834; -.
UCSC; uc001pig.5; human. [P29466-1]
CTD; 834; -.
DisGeNET; 834; -.
GeneCards; CASP1; -.
HGNC; HGNC:1499; CASP1.
HPA; CAB002685; -.
HPA; HPA003056; -.
MIM; 147678; gene.
neXtProt; NX_P29466; -.
OpenTargets; ENSG00000137752; -.
PharmGKB; PA26083; -.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00940000159114; -.
InParanoid; P29466; -.
KO; K01370; -.
OMA; EYAWSCD; -.
OrthoDB; 1610446at2759; -.
PhylomeDB; P29466; -.
TreeFam; TF102023; -.
BRENDA; 3.4.22.36; 2681.
Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
Reactome; R-HSA-448706; Interleukin-1 processing.
Reactome; R-HSA-6803207; TP53 Regulates Transcription of Caspase Activators and Caspases.
Reactome; R-HSA-844456; The NLRP3 inflammasome.
Reactome; R-HSA-844615; The AIM2 inflammasome.
Reactome; R-HSA-844623; The IPAF inflammasome.
Reactome; R-HSA-9008059; Interleukin-37 signaling.
SABIO-RK; P29466; -.
SignaLink; P29466; -.
SIGNOR; P29466; -.
ChiTaRS; CASP1; human.
EvolutionaryTrace; P29466; -.
GeneWiki; Caspase_1; -.
GenomeRNAi; 834; -.
PMAP-CutDB; P29466; -.
PRO; PR:P29466; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000137752; Expressed in 204 organ(s), highest expression level in leukocyte.
ExpressionAtlas; P29466; baseline and differential.
Genevisible; P29466; HS.
GO; GO:0097169; C:AIM2 inflammasome complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0072557; C:IPAF inflammasome complex; ISS:UniProtKB.
GO; GO:0072558; C:NLRP1 inflammasome complex; IDA:UniProtKB.
GO; GO:0072559; C:NLRP3 inflammasome complex; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0097179; C:protease inhibitor complex; IMP:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:0050700; F:CARD domain binding; IPI:UniProtKB.
GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; TAS:ProtInc.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0097199; F:cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IBA:GO_Central.
GO; GO:0004175; F:endopeptidase activity; IDA:ParkinsonsUK-UCL.
GO; GO:0042802; F:identical protein binding; IMP:UniProtKB.
GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; IBA:GO_Central.
GO; GO:0071345; P:cellular response to cytokine stimulus; TAS:Reactome.
GO; GO:0071346; P:cellular response to interferon-gamma; IMP:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:UniProtKB.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
GO; GO:0071310; P:cellular response to organic substance; IDA:MGI.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0097194; P:execution phase of apoptosis; IBA:GO_Central.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
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:0050718; P:positive regulation of interleukin-1 beta secretion; IDA:UniProtKB.
GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0016540; P:protein autoprocessing; IDA:UniProtKB.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; TAS:Reactome.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd00032; CASc; 1.
InterPro; IPR001315; CARD.
InterPro; IPR029030; Caspase-like_dom_sf.
InterPro; IPR033139; Caspase_cys_AS.
InterPro; IPR016129; Caspase_his_AS.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR002398; Pept_C14.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
PANTHER; PTHR10454; PTHR10454; 1.
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; Alternative splicing; Apoptosis; Cell membrane;
Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase;
Membrane; Phosphoprotein; Polymorphism; Protease; Reference proteome;
Thiol protease; Zymogen.
PROPEP 1 119
/FTId=PRO_0000004521.
CHAIN 120 297 Caspase-1 subunit p20.
/FTId=PRO_0000004522.
PROPEP 298 316
/FTId=PRO_0000004523.
CHAIN 317 404 Caspase-1 subunit p10.
/FTId=PRO_0000004524.
DOMAIN 1 91 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
ACT_SITE 237 237 {ECO:0000269|PubMed:1574116}.
ACT_SITE 285 285 {ECO:0000269|PubMed:1574116}.
MOD_RES 302 302 Phosphoserine.
{ECO:0000250|UniProtKB:P29452}.
VAR_SEQ 20 335 Missing (in isoform Epsilon).
{ECO:0000303|PubMed:7876192}.
/FTId=VSP_000797.
VAR_SEQ 20 112 Missing (in isoform Gamma and isoform
Delta). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7876192}.
/FTId=VSP_000799.
VAR_SEQ 92 112 Missing (in isoform Beta).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7876192}.
/FTId=VSP_000798.
VAR_SEQ 288 335 Missing (in isoform Delta).
{ECO:0000303|PubMed:7876192}.
/FTId=VSP_000800.
VARIANT 15 15 R -> H (in dbSNP:rs1042743).
/FTId=VAR_048615.
MUTAGEN 285 285 C->A,S: Loss of activity. Loss of SPHK2
cleavage and release in apoptotic cells.
{ECO:0000269|PubMed:15498465,
ECO:0000269|PubMed:20197547}.
CONFLICT 319 319 K -> R (in Ref. 4; BAD97223).
{ECO:0000305}.
CONFLICT 402 402 P -> L (in Ref. 4; BAD97223).
{ECO:0000305}.
TURN 129 132 {ECO:0000244|PDB:6BZ9}.
HELIX 138 147 {ECO:0000244|PDB:6BZ9}.
HELIX 149 151 {ECO:0000244|PDB:6BZ9}.
TURN 158 160 {ECO:0000244|PDB:6BZ9}.
STRAND 164 169 {ECO:0000244|PDB:6BZ9}.
STRAND 174 176 {ECO:0000244|PDB:6BZ9}.
HELIX 182 195 {ECO:0000244|PDB:6BZ9}.
STRAND 199 205 {ECO:0000244|PDB:6BZ9}.
HELIX 208 219 {ECO:0000244|PDB:6BZ9}.
HELIX 222 226 {ECO:0000244|PDB:6BZ9}.
STRAND 230 236 {ECO:0000244|PDB:6BZ9}.
STRAND 242 244 {ECO:0000244|PDB:1SC3}.
STRAND 250 252 {ECO:0000244|PDB:6BZ9}.
STRAND 255 257 {ECO:0000244|PDB:1SC4}.
HELIX 258 265 {ECO:0000244|PDB:6BZ9}.
TURN 267 269 {ECO:0000244|PDB:6BZ9}.
HELIX 271 273 {ECO:0000244|PDB:6BZ9}.
STRAND 278 284 {ECO:0000244|PDB:6BZ9}.
STRAND 286 289 {ECO:0000244|PDB:6BZ9}.
STRAND 291 298 {ECO:0000244|PDB:3E4C}.
HELIX 316 319 {ECO:0000244|PDB:3E4C}.
STRAND 326 333 {ECO:0000244|PDB:6BZ9}.
STRAND 340 342 {ECO:0000244|PDB:6BZ9}.
TURN 343 345 {ECO:0000244|PDB:6BZ9}.
HELIX 348 360 {ECO:0000244|PDB:6BZ9}.
TURN 361 363 {ECO:0000244|PDB:6BZ9}.
HELIX 366 376 {ECO:0000244|PDB:6BZ9}.
STRAND 381 383 {ECO:0000244|PDB:6F6R}.
STRAND 388 391 {ECO:0000244|PDB:6BZ9}.
STRAND 395 397 {ECO:0000244|PDB:1RWM}.
SEQUENCE 404 AA; 45159 MW; ABF33CF33CC71584 CRC64;
MADKVLKEKR KLFIRSMGEG TINGLLDELL QTRVLNKEEM EKVKRENATV MDKTRALIDS
VIPKGAQACQ ICITYICEED SYLAGTLGLS ADQTSGNYLN MQDSQGVLSS FPAPQAVQDN
PAMPTSSGSE GNVKLCSLEE AQRIWKQKSA EIYPIMDKSS RTRLALIICN EEFDSIPRRT
GAEVDITGMT MLLQNLGYSV DVKKNLTASD MTTELEAFAH RPEHKTSDST FLVFMSHGIR
EGICGKKHSE QVPDILQLNA IFNMLNTKNC PSLKDKPKVI IIQACRGDSP GVVWFKDSVG
VSGNLSLPTT EEFEDDAIKK AHIEKDFIAF CSSTPDNVSW RHPTMGSVFI GRLIEHMQEY
ACSCDVEEIF RKVRFSFEQP DGRAQMPTTE RVTLTRCFYL FPGH


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[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]
[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]
[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]
[CARD16 COP COP1] Caspase recruitment domain-containing protein 16 (Caspase recruitment domain-only protein 1) (CARD-only protein 1) (Caspase-1 inhibitor COP) (Pseudo interleukin-1 beta converting enzyme) (Pseudo-ICE) (Pseudo-IL1B-converting enzyme)
[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]
[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]
[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]
[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]
[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]
[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]
[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] 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]
[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]
[RIPK2 CARDIAK RICK RIP2 UNQ277/PRO314/PRO34092] Receptor-interacting serine/threonine-protein kinase 2 (EC 2.7.11.1) (CARD-containing interleukin-1 beta-converting enzyme-associated kinase) (CARD-containing IL-1 beta ICE-kinase) (RIP-like-interacting CLARP kinase) (Receptor-interacting protein 2) (RIP-2) (Tyrosine-protein kinase RIPK2) (EC 2.7.10.2)
[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]
[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 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]
[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]
[CASP13] Caspase-13 (CASP-13) (EC 3.4.22.-) (Evolutionary related interleukin-1-beta-converting enzyme) (ERICE) [Cleaved into: Caspase-13 subunit 1; Caspase-13 subunit 2]
[csp-1 Y48E1B.13] Caspase A (EC 3.4.22.36) [Cleaved into: Caspase A subunit p16; Caspase A subunit p14]
[Casp6] Caspase-6 (CASP-6) (EC 3.4.22.59) (Apoptotic protease Mch-2) [Cleaved into: Caspase-6 subunit p18; Caspase-6 subunit p11]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[Il1b] Interleukin-1 beta (IL-1 beta)
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[AMC4 AMC7 MCP2D At1g79340 YUP8H12R.4] Metacaspase-4 (AtMC4) (EC 3.4.22.-) (Metacaspase 2d) (AtMCP2d) (Metacaspase-7) [Cleaved into: Metacaspase-4 subunit p20; Metacaspase-4 subunit p10]
[Drice ICE CG7788] Caspase (EC 3.4.22.-) (drICE) [Cleaved into: Caspase subunit p21; Caspase subunit p12]
[IL33 C9orf26 IL1F11 NFHEV] Interleukin-33 (IL-33) (Interleukin-1 family member 11) (IL-1F11) (Nuclear factor from high endothelial venules) (NF-HEV) [Cleaved into: Interleukin-33 (95-270); Interleukin-33 (99-270); Interleukin-33 (109-270)]
[IL37 FIL1Z IL1F7 IL1H4 IL1RP1] Interleukin-37 (FIL1 zeta) (IL-1X) (Interleukin-1 family member 7) (IL-1F7) (Interleukin-1 homolog 4) (IL-1H) (IL-1H4) (Interleukin-1 zeta) (IL-1 zeta) (Interleukin-1-related protein) (IL-1RP1) (Interleukin-23) (IL-37)
[IL12RB1 IL12R IL12RB] Interleukin-12 receptor subunit beta-1 (IL-12 receptor subunit beta-1) (IL-12R subunit beta-1) (IL-12R-beta-1) (IL-12RB1) (IL-12 receptor beta component) (CD antigen CD212)

Bibliography :