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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)

 CAR16_HUMAN             Reviewed;         197 AA.
Q5EG05; Q96RJ9;
02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
15-MAR-2005, sequence version 1.
08-MAY-2019, entry version 110.
RecName: Full=Caspase recruitment domain-containing protein 16;
AltName: Full=Caspase recruitment domain-only protein 1;
Short=CARD-only protein 1;
AltName: Full=Caspase-1 inhibitor COP;
AltName: Full=Pseudo interleukin-1 beta converting enzyme;
Short=Pseudo-ICE;
Short=Pseudo-IL1B-converting enzyme;
Name=CARD16; Synonyms=COP, COP1;
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), FUNCTION, TISSUE SPECIFICITY,
AND INTERACTION WITH CASP1 AND RIPK2.
PubMed=11536016; DOI=10.1038/sj.cdd.4400881;
Druilhe A., Srinivasula S.M., Razmara M., Ahmad M., Alnemri E.S.;
"Regulation of IL-1beta generation by Pseudo-ICE and ICEBERG, two
dominant negative caspase recruitment domain proteins.";
Cell Death Differ. 8:649-657(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Wang P.Z., Wang F., Wang X., Wu J.;
"Novel splicing variants of some human genes.";
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Spleen;
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).
[4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
[6]
FUNCTION, TISSUE SPECIFICITY, SUBUNIT, AND INTERACTION WITH CASP1 AND
RIPK2.
PubMed=11432859; DOI=10.1074/jbc.M101415200;
Lee S.H., Stehlik C., Reed J.C.;
"Cop, a caspase recruitment domain-containing protein and inhibitor of
caspase-1 activation processing.";
J. Biol. Chem. 276:34495-34500(2001).
[7]
INTERACTION WITH CARD8.
PubMed=11821383; DOI=10.1074/jbc.M107811200;
Razmara M., Srinivasula S.M., Wang L., Poyet J.-L., Geddes B.J.,
DiStefano P.S., Bertin J., Alnemri E.S.;
"CARD-8 protein, a new CARD family member that regulates caspase-1
activation and apoptosis.";
J. Biol. Chem. 277:13952-13958(2002).
[8]
INDUCTION.
PubMed=16354923; DOI=10.1523/JNEUROSCI.4181-05.2005;
Wang X., Wang H., Figueroa B.E., Zhang W.-H., Huo C., Guan Y.,
Zhang Y., Bruey J.-M., Reed J.C., Friedlander R.M.;
"Dysregulation of receptor interacting protein-2 and caspase
recruitment domain only protein mediates aberrant caspase-1 activation
in Huntington's disease.";
J. Neurosci. 25:11645-11654(2005).
[9]
FUNCTION, AND INTERACTION WITH CASP4.
PubMed=16920334; DOI=10.1016/j.bbadis.2006.06.015;
Wang X., Narayanan M., Bruey J.-M., Rigamonti D., Cattaneo E.,
Reed J.C., Friedlander R.M.;
"Protective role of Cop in Rip2/caspase-1/caspase-4-mediated HeLa cell
death.";
Biochim. Biophys. Acta 1762:742-754(2006).
[10]
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).
-!- FUNCTION: Caspase inhibitor. Acts as a regulator of procaspase-
1/CASP1 activation implicated in the regulation of the proteolytic
maturation of pro-interleukin-1 beta (IL1B) and its release during
inflammation. Inhibits the release of IL1B in response to LPS in
monocytes. Also induces NF-kappa-B activation during the pro-
inflammatory cytokine response. Also able to inhibit CASP1-
mediated neuronal cell death, TNF-alpha, hypoxia-, UV-, and
staurosporine-mediated cell death but not ER stress-mediated cell
death. Acts by preventing activation of caspases CASP1 and CASP4,
possibly by preventing the interaction between CASP1 and RIPK2.
{ECO:0000269|PubMed:11432859, ECO:0000269|PubMed:11536016,
ECO:0000269|PubMed:16920334}.
-!- SUBUNIT: Homooligomer. Interacts with CASP1, CASP4, CARD8 and
RIPK2. {ECO:0000269|PubMed:11432859, ECO:0000269|PubMed:11536016,
ECO:0000269|PubMed:11821383, ECO:0000269|PubMed:16920334}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q5EG05-1; Sequence=Displayed;
Name=2;
IsoId=Q5EG05-2; Sequence=VSP_035216;
-!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in
placenta, spleen, lymph node and bone marrow. Weakly or not
expressed in thymus. {ECO:0000269|PubMed:11432859,
ECO:0000269|PubMed:11536016}.
-!- INDUCTION: Down-regulated in patients suffering of Huntington
disease. {ECO:0000269|PubMed:16354923}.
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; AF367017; AAK71682.1; -; mRNA.
EMBL; AY885669; AAW78563.1; -; mRNA.
EMBL; AK311902; BAG34843.1; -; mRNA.
EMBL; CH471065; EAW67062.1; -; Genomic_DNA.
EMBL; BC117478; AAI17479.1; -; mRNA.
EMBL; BC117480; AAI17481.1; -; mRNA.
CCDS; CCDS31661.1; -. [Q5EG05-1]
CCDS; CCDS41705.1; -. [Q5EG05-2]
RefSeq; NP_001017534.1; NM_001017534.1. [Q5EG05-1]
RefSeq; NP_443121.1; NM_052889.2. [Q5EG05-2]
SMR; Q5EG05; -.
BioGrid; 125339; 3.
IntAct; Q5EG05; 1.
MINT; Q5EG05; -.
STRING; 9606.ENSP00000364858; -.
iPTMnet; Q5EG05; -.
PhosphoSitePlus; Q5EG05; -.
BioMuta; CARD16; -.
DMDM; 74722547; -.
jPOST; Q5EG05; -.
MaxQB; Q5EG05; -.
PaxDb; Q5EG05; -.
PeptideAtlas; Q5EG05; -.
PRIDE; Q5EG05; -.
ProteomicsDB; 62773; -.
ProteomicsDB; 62774; -. [Q5EG05-2]
Ensembl; ENST00000375704; ENSP00000364856; ENSG00000204397. [Q5EG05-2]
Ensembl; ENST00000375706; ENSP00000364858; ENSG00000204397. [Q5EG05-1]
Ensembl; ENST00000525374; ENSP00000433700; ENSG00000204397. [Q5EG05-2]
GeneID; 114769; -.
KEGG; hsa:114769; -.
UCSC; uc001pio.2; human. [Q5EG05-1]
CTD; 114769; -.
DisGeNET; 114769; -.
GeneCards; CARD16; -.
HGNC; HGNC:33701; CARD16.
HPA; HPA053981; -.
HPA; HPA062805; -.
MIM; 615680; gene.
neXtProt; NX_Q5EG05; -.
OpenTargets; ENSG00000204397; -.
PharmGKB; PA164717628; -.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00940000159114; -.
HOGENOM; HOG000111300; -.
InParanoid; Q5EG05; -.
KO; K12806; -.
OMA; CITDICE; -.
OrthoDB; 1327703at2759; -.
PhylomeDB; Q5EG05; -.
TreeFam; TF330675; -.
ChiTaRS; CARD16; human.
GeneWiki; COP1; -.
GenomeRNAi; 114769; -.
PRO; PR:Q5EG05; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000204397; Expressed in 171 organ(s), highest expression level in leukocyte.
ExpressionAtlas; Q5EG05; baseline and differential.
Genevisible; Q5EG05; HS.
GO; GO:0097179; C:protease inhibitor complex; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:0050700; F:CARD domain binding; IPI:UniProtKB.
GO; GO:0089720; F:caspase binding; IPI:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
GO; GO:0071456; P:cellular response to hypoxia; IDA:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
GO; GO:0071494; P:cellular response to UV-C; IDA:UniProtKB.
GO; GO:0097340; P:inhibition of cysteine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0050713; P:negative regulation of interleukin-1 beta secretion; IDA:UniProtKB.
GO; GO:0031665; P:negative regulation of lipopolysaccharide-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0032091; P:negative regulation of protein binding; IDA:UniProtKB.
GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
InterPro; IPR001315; CARD.
InterPro; IPR011029; DEATH-like_dom_sf.
Pfam; PF00619; CARD; 1.
SMART; SM00114; CARD; 1.
SUPFAM; SSF47986; SSF47986; 1.
PROSITE; PS50209; CARD; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Polymorphism;
Protease inhibitor; Reference proteome; Thiol protease inhibitor.
CHAIN 1 197 Caspase recruitment domain-containing
protein 16.
/FTId=PRO_0000349180.
DOMAIN 1 91 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
VAR_SEQ 92 197 ALQAVQDNPAMPTCSSPEGRIKLCFLEDAQRIWKQKLQRCH
VQNTIIKWSERYTSGSFEMQWLFLRTNFIERFWRNILLLPL
HKGSLYPRIPGLGKELQTGTHKLS -> GPIPGN (in
isoform 2). {ECO:0000303|PubMed:11536016,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_035216.
VARIANT 33 33 R -> S (in dbSNP:rs35966314).
/FTId=VAR_046279.
VARIANT 37 37 Q -> K (in dbSNP:rs1042744).
/FTId=VAR_046280.
VARIANT 56 56 A -> D (in dbSNP:rs34534919).
/FTId=VAR_046281.
VARIANT 167 167 N -> I (in dbSNP:rs542571).
/FTId=VAR_046282.
SEQUENCE 197 AA; 22625 MW; 5DCAC6A9B2FAE82F CRC64;
MADKVLKEKR KLFIHSMGEG TINGLLDELL QTRVLNQEEM EKVKRENATV MDKTRALIDS
VIPKGAQACQ ICITYICEED SYLAETLGLS AALQAVQDNP AMPTCSSPEG RIKLCFLEDA
QRIWKQKLQR CHVQNTIIKW SERYTSGSFE MQWLFLRTNF IERFWRNILL LPLHKGSLYP
RIPGLGKELQ TGTHKLS


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Pathways :
WP1493: Carbon assimilation C4 pathway
WP1689: Porphyrin and chlorophyll metabolism
WP1566: Citrate cycle (TCA cycle)
WP210: Cytoplasmic Ribosomal Proteins
WP2218: sGC
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation

Related Genes :
[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)
[NLRP1 CARD7 DEFCAP KIAA0926 NAC NALP1] NACHT, LRR and PYD domains-containing protein 1 (Caspase recruitment domain-containing protein 7) (Death effector filament-forming ced-4-like apoptosis protein) (Nucleotide-binding domain and caspase recruitment domain)
[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]
[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)
[Nlrc4 Card12 Ipaf] NLR family CARD domain-containing protein 4 (Caspase recruitment domain-containing protein 12) (Ice protease-activating factor) (Ipaf)
[PYCARD ASC CARD5 TMS1] Apoptosis-associated speck-like protein containing a CARD (hASC) (Caspase recruitment domain-containing protein 5) (PYD and CARD domain-containing protein) (Target of methylation-induced silencing 1)
[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]
[NOD2 CARD15 IBD1] Nucleotide-binding oligomerization domain-containing protein 2 (Caspase recruitment domain-containing protein 15) (Inflammatory bowel disease protein 1)
[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)
[CARD11 CARMA1] Caspase recruitment domain-containing protein 11 (CARD-containing MAGUK protein 1) (Carma 1)
[CARD9] Caspase recruitment domain-containing protein 9 (hCARD9)
[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]
[CARD14 CARMA2] Caspase recruitment domain-containing protein 14 (CARD-containing MAGUK protein 2) (Carma 2)
[Card11] Caspase recruitment domain-containing protein 11
[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 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]
[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]
[Il1b] Interleukin-1 beta (IL-1 beta)
[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) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[CARD10 CARMA3] Caspase recruitment domain-containing protein 10 (CARD-containing MAGUK protein 3) (Carma 3)
[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]
[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]
[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]
[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]
[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]
[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]
[IL1B M91_19273] Multifunctional fusion protein [Includes: Interleukin-1; Interleukin-1 beta]
[IL1B IL1F2] Interleukin-1 beta (IL-1 beta) (Catabolin)
[IL1B] Interleukin-1 beta (IL-1 beta)

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