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Putative inactive caspase B [Cleaved into: Putative inactive caspase B subunit p31; Putative inactive caspase B subunit p17; Putative inactive caspase subunit p14]

 CSP2_CAEEL              Reviewed;         263 AA.
Q9TZP5; A0A1N7SZF9; G5ECY5;
15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
07-APR-2021, entry version 106.
RecName: Full=Putative inactive caspase B {ECO:0000305};
Contains:
RecName: Full=Putative inactive caspase B subunit p31 {ECO:0000305|PubMed:9857046};
Contains:
RecName: Full=Putative inactive caspase B subunit p17 {ECO:0000305|PubMed:9857046};
Contains:
RecName: Full=Putative inactive caspase subunit p14 {ECO:0000305|PubMed:9857046};
Flags: Precursor;
Name=csp-2 {ECO:0000303|PubMed:9857046, ECO:0000312|WormBase:Y73B6BL.7b};
ORFNames=Y73B6BL.7 {ECO:0000312|WormBase:Y73B6BL.7b};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
Caenorhabditis.
NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
[1] {ECO:0000312|EMBL:AAC98296.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, LACK OF CATALYTIC
ACTIVITY, PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF ASP-8.
STRAIN=Bristol N2 {ECO:0000312|EMBL:AAC98296.1};
PubMed=9857046; DOI=10.1074/jbc.273.52.35109;
Shaham S.;
"Identification of multiple Caenorhabditis elegans caspases and their
potential roles in proteolytic cascades.";
J. Biol. Chem. 273:35109-35117(1998).
[2] {ECO:0000312|Proteomes:UP000001940}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for investigating
biology.";
Science 282:2012-2018(1998).
[3] {ECO:0000305}
FUNCTION (ISOFORMS A AND B), INTERACTION WITH CED-3, SUBCELLULAR LOCATION,
TISSUE SPECIFICITY, AND MUTAGENESIS OF 131-TRP--LEU-132; CYS-134 AND
PHE-186.
PubMed=19575016; DOI=10.1038/cdd.2009.88;
Geng X., Zhou Q.H., Kage-Nakadai E., Shi Y., Yan N., Mitani S., Xue D.;
"Caenorhabditis elegans caspase homolog CSP-2 inhibits CED-3 autoactivation
and apoptosis in germ cells.";
Cell Death Differ. 16:1385-1394(2009).
[4] {ECO:0000305}
DISRUPTION PHENOTYPE.
PubMed=23505386; DOI=10.1371/journal.pgen.1003341;
Denning D.P., Hatch V., Horvitz H.R.;
"Both the caspase CSP-1 and a caspase-independent pathway promote
programmed cell death in parallel to the canonical pathway for apoptosis in
Caenorhabditis elegans.";
PLoS Genet. 9:E1003341-E1003341(2013).
-!- FUNCTION: [Isoform b]: Putative inactive caspase (PubMed:9857046). In
the germline, binds caspase ced-3 zymogen and prevents ced-3
autoactivation. Does not affect the caspase activity of mature ced-3
and ced-4-mediated mature ced-3 activation (PubMed:19575016).
Negatively regulates germline apoptosis by inhibiting autocleavage of
caspase ced-3 (PubMed:19575016). Involved in fertility
(PubMed:19575016). {ECO:0000269|PubMed:19575016,
ECO:0000269|PubMed:9857046}.
-!- FUNCTION: [Isoform a]: Putative inactive caspase (PubMed:9857046).
Dispensable for the inhibition of germline apoptosis (PubMed:19575016).
{ECO:0000269|PubMed:19575016, ECO:0000303|PubMed:9857046}.
-!- SUBUNIT: Interacts with ced-3 (via large subunit p17 or small subunit
p13); the interaction inhibits ced-3 autoactivation.
{ECO:0000269|PubMed:19575016}.
-!- SUBCELLULAR LOCATION: [Isoform b]: Cytoplasm
{ECO:0000269|PubMed:19575016}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=b {ECO:0000312|WormBase:Y73B6BL.7b};
IsoId=Q9TZP5-1; Sequence=Displayed;
Name=a {ECO:0000312|WormBase:Y73B6BL.7a};
IsoId=Q9TZP5-2; Sequence=VSP_058807;
Name=c {ECO:0000312|WormBase:Y73B6BL.7c};
IsoId=Q9TZP5-3; Sequence=VSP_059611;
-!- TISSUE SPECIFICITY: Specifically expressed in the hermaphrodite
germline. {ECO:0000269|PubMed:19575016}.
-!- PTM: Cleavage by csp-1 isoform b or ced-3 removes the propeptide and
generates subunit p31 in vitro. An additional cleavage at Asp-149
generates the 2 subunits p17 and p14 but this cleavage appears to be
less efficient. {ECO:0000269|PubMed:9857046}.
-!- DISRUPTION PHENOTYPE: Survival of touch neurons and several pharyngeal
cells is not affected during development. In a ced-3 n2427 or ced-3
n2427 and cps-3 n4872 mutant background, no extra pharyngeal cells
caused by impaired apoptosis are produced. In a csp-3 n4872, csp-1
n4967 and ced-3 n3692 mutant background, pharyngeal cells, that are
normally fated to die, survive and 16 percent of animals have still 1
or more cell corpses that are morphologically apoptotic and are
internalized by engulfing cells. In addition, apoptosis of the male
linker cell occurs normally. {ECO:0000269|PubMed:23505386}.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000255,
ECO:0000255|RuleBase:RU003971}.
-!- CAUTION: Although the active site residues Cys and His are conserved,
appears to lack catalytic activity in vitro. This is probably due to
the active site pentapeptide VCCRG being highly divergent from the
canonical active site pentapeptide QAC[RQG]G present in catalytically
active caspases. {ECO:0000303|PubMed:9857046}.
---------------------------------------------------------------------------
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EMBL; AF088288; AAC98295.1; -; mRNA.
EMBL; AF088289; AAC98296.1; -; mRNA.
EMBL; BX284604; CCD74157.1; -; Genomic_DNA.
EMBL; BX284604; SIT60436.1; -; Genomic_DNA.
EMBL; BX284604; SIT60437.1; -; Genomic_DNA.
PIR; T43638; T43638.
RefSeq; NP_001023575.1; NM_001028404.2.
RefSeq; NP_001335546.1; NM_001348645.1.
RefSeq; NP_001335547.1; NM_001348644.1.
STRING; 6239.Y73B6BL.7; -.
MEROPS; C14.014; -.
EnsemblMetazoa; Y73B6BL.7a.1; Y73B6BL.7a.1; WBGene00000820. [Q9TZP5-2]
EnsemblMetazoa; Y73B6BL.7b.1; Y73B6BL.7b.1; WBGene00000820. [Q9TZP5-1]
EnsemblMetazoa; Y73B6BL.7c.1; Y73B6BL.7c.1; WBGene00000820. [Q9TZP5-3]
GeneID; 177391; -.
UCSC; Y73B6BL.7; c. elegans. [Q9TZP5-1]
CTD; 177391; -.
WormBase; Y73B6BL.7a; CE28270; WBGene00000820; csp-2. [Q9TZP5-2]
WormBase; Y73B6BL.7b; CE51898; WBGene00000820; csp-2. [Q9TZP5-1]
WormBase; Y73B6BL.7c; CE51881; WBGene00000820; csp-2. [Q9TZP5-3]
eggNOG; KOG0516; Eukaryota.
eggNOG; KOG3573; Eukaryota.
GeneTree; ENSGT00970000196149; -.
HOGENOM; CLU_342972_0_0_1; -.
OrthoDB; 824788at2759; -.
Reactome; R-CEL-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-CEL-198323; AKT phosphorylates targets in the cytosol.
Reactome; R-CEL-264870; Caspase-mediated cleavage of cytoskeletal proteins.
Reactome; R-CEL-448706; Interleukin-1 processing.
Reactome; R-CEL-5357905; Regulation of TNFR1 signaling.
Reactome; R-CEL-5660668; CLEC7A/inflammasome pathway.
Reactome; R-CEL-75153; Apoptotic execution phase.
PRO; PR:Q9TZP5; -.
Proteomes; UP000001940; Chromosome IV.
Bgee; WBGene00000820; Expressed in germ line (C elegans) and 4 other tissues.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0097179; C:protease inhibitor complex; IMP:UniProtKB.
GO; GO:0089720; F:caspase binding; IPI: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:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IBA:GO_Central.
GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IMP:UniProtKB.
GO; GO:0035375; F:zymogen binding; IDA: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:0097194; P:execution phase of apoptosis; IBA:GO_Central.
GO; GO:1990001; P:inhibition of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IGI:UniProtKB.
GO; GO:1904747; P:positive regulation of apoptotic process involved in development; IGI:UniProtKB.
GO; GO:0090727; P:positive regulation of brood size; IMP:UniProtKB.
GO; GO:1905516; P:positive regulation of fertilization; IGI:UniProtKB.
CDD; cd00032; CASc; 1.
InterPro; IPR029030; Caspase-like_dom_sf.
InterPro; IPR016129; Caspase_his_AS.
InterPro; IPR002398; Pept_C14.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
PANTHER; PTHR10454; PTHR10454; 1.
PRINTS; PR00376; IL1BCENZYME.
SMART; SM00115; CASc; 1.
SUPFAM; SSF52129; SSF52129; 1.
PROSITE; PS01121; CASPASE_HIS; 1.
PROSITE; PS50207; CASPASE_P10; 1.
PROSITE; PS50208; CASPASE_P20; 1.
1: Evidence at protein level;
Alternative splicing; Cytoplasm; Reference proteome.
PROPEP 1..8
/note="Removed in mature form by cps-1 or ced-3"
/evidence="ECO:0000269|PubMed:9857046"
/id="PRO_0000439221"
CHAIN 9..263
/note="Putative inactive caspase B subunit p31"
/evidence="ECO:0000303|PubMed:9857046"
/id="PRO_0000439222"
CHAIN 9..149
/note="Putative inactive caspase B subunit p17"
/evidence="ECO:0000303|PubMed:9857046"
/id="PRO_0000439223"
CHAIN 150..263
/note="Putative inactive caspase subunit p14"
/evidence="ECO:0000303|PubMed:9857046"
/id="PRO_0000439224"
VAR_SEQ 1
/note="M -> MKIGWLLITICSGIITKCINAHSSPYQNANESAIDDAYFLVLIIPAV
SVAIVLVVVIFLCCPRQQIRSDNVIKLEEGVNDVIEENVTHVVSLREAKVSGMMTDLTR
FRQEIFTKHLTFNSNPESIDAATKNVQNVKQSLDTWRDRIKERLDEIDRLCTEEGDSLT
PEQYSALREMRRQLADEYDTVLRTVEGIHTRLNILSALLIEFSSVTSSMQSWMTDRARL
AGDIRHKSGDPMRVDEARFEAKSLMDEVVREESRLKTIGASVLKIEQEISAMRDDVRAS
RSTDDVGISMDEVYEKRRRVEVDYMQLLRQCQDLISLQIRLHAMNDEHAEQARRAEGWL
QMLKNDVAGVAKDPRFKKDEDLIERDEELNRMAAGGSGGPTSRQLAMREKIEQREREEE
EWRRKAKEKFEEEAAKNRARERKWAEEHGFNRPIRTRSQKYAEQDRIRYARKKAALEQS
NEQSNESTDDAVESDSDDVPAPQSPPTPSPADPGPTTSSSSLTQDPASNATGFSDVPAP
QAPPTPSPADPGPTTSSSSLTQDPASNATGFSGSSPPNSFEETRM (in isoform
a)"
/evidence="ECO:0000305"
/id="VSP_058807"
VAR_SEQ 1
/note="M -> MMTDLTRFRQEIFTKHLTFNSNPESIDAATKNVQNVKQSLDTWRDRI
KERLDEIDRLCTEEGDSLTPEQYSALREMRRQLADEYDTVLRTVEGIHTRLNILSALLI
EFSSVTSSMQSWMTDRARLAGDIRHKSGDPMRVDEARFEAKSLMDEVVREESRLKTIGA
SVLKIEQEISAMRDDVRASRSTDDVGISMDEVYEKRRRVEVDYMQLLRQCQDLISLQIR
LHAMNDEHAEQARRAEGWLQMLKNDVAGVAKDPRFKKDEDLIERDEELNRMAAGGSGGP
TSRQLAMREKIEQREREEEEWRRKAKEKFEEEAAKNRARERKWAEEHGFNRPIRTRSQK
YAEQDRIRYARKKAALEQSNEQSNESTDDAVESDSDDVPAPQSPPTPSPADPGPTTSSS
SLTQDPASNATGFSDVPAPQAPPTPSPADPGPTTSSSSLTQDPASNATGFSGSSPPNSF
EETRM (in isoform c)"
/evidence="ECO:0000305"
/id="VSP_059611"
MUTAGEN 8
/note="D->A: Loss of propeptide cleavage."
/evidence="ECO:0000269|PubMed:9857046"
MUTAGEN 131..132
/note="WL->ER: Loss of interaction with ced-3 small subunit
p13. Increased germline apoptosis in a ced-6 n2095 mutant
background, loss of interaction with ced-3 and loss of ced-
3 autoactivation; when associated with D-186."
/evidence="ECO:0000269|PubMed:19575016"
MUTAGEN 134
/note="C->E: Reduction in the interaction with ced-3 small
subunit p13."
/evidence="ECO:0000269|PubMed:19575016"
MUTAGEN 186
/note="F->D: Severe reduction in the interaction with ced-3
large subunit p17. Increased germline apoptosis in a ced-6
n2095 mutant background, loss of interaction with ced-3 and
loss of ced-3 autoactivation; when associated with E-131
and R-132."
/evidence="ECO:0000269|PubMed:19575016"
SEQUENCE 263 AA; 30401 MW; FE94EC95B8B59FEE CRC64;
MMCEDASDGK KIDETRKYRN NRSSKCRAII INNVVFCGME KRIGSDKDKK KLSKLFERLG
YQSTSYDNLK SSEILETVRQ FTQSNHGDSL IITIMSHGDQ GLLYGVDGVP VQMLDIIDLM
CTASLAKKPK WLMCVCCRGD RIDRAVRCDG FIDNFFDRFP KFFQFMKSKF PSHQTSSSQA
DLLVSFSTSP GFLSFRDETK GTWYIQELYR VIIENAKDTH LADLLMETNR RVVEKYEADK
VVIVCKQAPE FWSRFTKQLF FDV


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Related Genes :
[csp-2 Y73B6BL.7] Putative inactive caspase B [Cleaved into: Putative inactive caspase B subunit p31; Putative inactive caspase B subunit p17; Putative inactive caspase subunit p14]
[csp-1 Y48E1B.13] Caspase A (EC 3.4.22.36) [Cleaved into: Caspase A subunit p16; Caspase A subunit p14]
[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]
[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]
[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]
[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) (LICE) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [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]
[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]
[CARD8 DACAR KIAA0955 NDPP1] Caspase recruitment domain-containing protein 8 (EC 3.4.-.-) (CARD-inhibitor of NF-kappa-B-activating ligand) (CARDINAL) (Tumor up-regulated CARD-containing antagonist of CASP9) (TUCAN) [Cleaved into: Caspase recruitment domain-containing protein 8, C-terminus (CARD8-CT); Caspase recruitment domain-containing protein 8, N-terminus (CARD8-NT)]
[Drice ICE CG7788] Caspase (EC 3.4.22.-) (drICE) [Cleaved into: Caspase subunit p21; Caspase subunit p12]
[caspb casp19a caspy2] Caspase b (EC 3.4.22.58) (Caspase 19a) [Cleaved into: Caspase b subunit p20; Caspase b subunit p10]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [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]
[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]
[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]
[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]
[Casp8] Caspase-8 (CASP-8) (EC 3.4.22.61) [Cleaved into: Caspase-8 subunit p18; Caspase-8 subunit p10]
[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]
[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]
[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 p10; Caspase-4 subunit p20]
[Casp8] Caspase-8 (CASP-8) (EC 3.4.22.61) [Cleaved into: Caspase-8 subunit p18; Caspase-8 subunit p10]
[caspa casp1 caspy] Caspase a (EC 3.4.22.36) [Cleaved into: Caspase a subunit p20; Caspase a subunit p10]
[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] Caspase-6 (CASP-6) (EC 3.4.22.59) (Apoptotic protease Mch-2) [Cleaved into: Caspase-6 subunit p18; Caspase-6 subunit p11]
[ced-3 CRE_10123] 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]

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