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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.
13-FEB-2019, entry version 96.
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;
Note=No experimental confirmation available. {ECO:0000305};
-!- 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|RuleBase:RU003971, ECO:0000255|SAAS:SAAS00535228}.
-!- 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. [Q9TZP5-2]
RefSeq; NP_001335546.1; NM_001348645.1. [Q9TZP5-1]
RefSeq; NP_001335547.1; NM_001348644.1.
UniGene; Cel.19615; -.
ProteinModelPortal; Q9TZP5; -.
STRING; 6239.Y73B6BL.7; -.
MEROPS; C14.014; -.
EnsemblMetazoa; Y73B6BL.7a; Y73B6BL.7a; WBGene00000820. [Q9TZP5-2]
EnsemblMetazoa; Y73B6BL.7b; Y73B6BL.7b; WBGene00000820. [Q9TZP5-1]
EnsemblMetazoa; Y73B6BL.7c; Y73B6BL.7c; WBGene00000820. [Q9TZP5-3]
GeneID; 177391; -.
KEGG; cel:CELE_Y73B6BL.7; -.
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.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00940000171812; -.
OrthoDB; 824788at2759; -.
Reactome; R-CEL-6809371; Formation of the cornified envelope.
PRO; PR:Q9TZP5; -.
Proteomes; UP000001940; Chromosome IV.
Bgee; WBGene00000820; Expressed in 4 organ(s), highest expression level in germ line (C elegans).
ExpressionAtlas; Q9TZP5; baseline and differential.
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:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IMP:UniProtKB.
GO; GO:0035375; F:zymogen binding; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; 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; Complete proteome; Cytoplasm;
Reference proteome.
PROPEP 1 8 Removed in mature form by cps-1 or ced-3.
{ECO:0000269|PubMed:9857046}.
/FTId=PRO_0000439221.
CHAIN 9 263 Putative inactive caspase B subunit p31.
{ECO:0000303|PubMed:9857046}.
/FTId=PRO_0000439222.
CHAIN 9 149 Putative inactive caspase B subunit p17.
{ECO:0000303|PubMed:9857046}.
/FTId=PRO_0000439223.
CHAIN 150 263 Putative inactive caspase subunit p14.
{ECO:0000303|PubMed:9857046}.
/FTId=PRO_0000439224.
VAR_SEQ 1 1 M -> MKIGWLLITICSGIITKCINAHSSPYQNANESAIDD
AYFLVLIIPAVSVAIVLVVVIFLCCPRQQIRSDNVIKLEEG
VNDVIEENVTHVVSLREAKVSGMMTDLTRFRQEIFTKHLTF
NSNPESIDAATKNVQNVKQSLDTWRDRIKERLDEIDRLCTE
EGDSLTPEQYSALREMRRQLADEYDTVLRTVEGIHTRLNIL
SALLIEFSSVTSSMQSWMTDRARLAGDIRHKSGDPMRVDEA
RFEAKSLMDEVVREESRLKTIGASVLKIEQEISAMRDDVRA
SRSTDDVGISMDEVYEKRRRVEVDYMQLLRQCQDLISLQIR
LHAMNDEHAEQARRAEGWLQMLKNDVAGVAKDPRFKKDEDL
IERDEELNRMAAGGSGGPTSRQLAMREKIEQREREEEEWRR
KAKEKFEEEAAKNRARERKWAEEHGFNRPIRTRSQKYAEQD
RIRYARKKAALEQSNEQSNESTDDAVESDSDDVPAPQSPPT
PSPADPGPTTSSSSLTQDPASNATGFSDVPAPQAPPTPSPA
DPGPTTSSSSLTQDPASNATGFSGSSPPNSFEETRM (in
isoform a). {ECO:0000305}.
/FTId=VSP_058807.
VAR_SEQ 1 1 M -> MMTDLTRFRQEIFTKHLTFNSNPESIDAATKNVQNV
KQSLDTWRDRIKERLDEIDRLCTEEGDSLTPEQYSALREMR
RQLADEYDTVLRTVEGIHTRLNILSALLIEFSSVTSSMQSW
MTDRARLAGDIRHKSGDPMRVDEARFEAKSLMDEVVREESR
LKTIGASVLKIEQEISAMRDDVRASRSTDDVGISMDEVYEK
RRRVEVDYMQLLRQCQDLISLQIRLHAMNDEHAEQARRAEG
WLQMLKNDVAGVAKDPRFKKDEDLIERDEELNRMAAGGSGG
PTSRQLAMREKIEQREREEEEWRRKAKEKFEEEAAKNRARE
RKWAEEHGFNRPIRTRSQKYAEQDRIRYARKKAALEQSNEQ
SNESTDDAVESDSDDVPAPQSPPTPSPADPGPTTSSSSLTQ
DPASNATGFSDVPAPQAPPTPSPADPGPTTSSSSLTQDPAS
NATGFSGSSPPNSFEETRM (in isoform c).
{ECO:0000305}.
/FTId=VSP_059611.
MUTAGEN 8 8 D->A: Loss of propeptide cleavage.
{ECO:0000269|PubMed:9857046}.
MUTAGEN 131 132 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.
{ECO:0000269|PubMed:19575016}.
MUTAGEN 134 134 C->E: Reduction in the interaction with
ced-3 small subunit p13.
{ECO:0000269|PubMed:19575016}.
MUTAGEN 186 186 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.
{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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Pathways :
WP1493: Carbon assimilation C4 pathway
WP1581: Histidine metabolism
WP1624: Bacterial secretion system
WP1673: Naphthalene and anthracene degradation
WP1689: Porphyrin and chlorophyll metabolism
WP1692: Protein export
WP1700: Selenoamino acid metabolism
WP1709: Thiamine metabolism
WP1714: Tyrosine metabolism
WP1965: VEGF-receptor Signal Transduction
WP2359: Parkin-Ubiquitin Proteasomal System pathway
WP88: Toll Like Receptor signaling
WP1566: Citrate cycle (TCA cycle)
WP1614: 1- and 2-Methylnaphthalene degradation
WP1626: Benzoate degradation via CoA ligation
WP1634: Butanoate metabolism
WP1644: DNA replication
WP1655: Geraniol degradation
WP1663: Homologous recombination
WP1671: Methane metabolism
WP1672: Mismatch repair
WP1680: Oxidative phosphorylation
WP1693: Purine metabolism
WP1694: Pyrimidine metabolism
WP1711: Trinitrotoluene degradation

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]
[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]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 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]
[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]
[Drice ICE CG7788] Caspase (EC 3.4.22.-) (drICE) [Cleaved into: Caspase subunit p21; Caspase subunit p12]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[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]
[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]
[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]
[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]
[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]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 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]
[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]
[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]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]

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