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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]

 CASP7_HUMAN             Reviewed;         303 AA.
P55210; B4DQU7; B5BU45; D3DRB8; Q13364; Q53YD5; Q5SVL0; Q5SVL3;
Q96BA0;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
13-FEB-2019, entry version 201.
RecName: Full=Caspase-7;
Short=CASP-7;
EC=3.4.22.60;
AltName: Full=Apoptotic protease Mch-3;
AltName: Full=CMH-1;
AltName: Full=ICE-like apoptotic protease 3;
Short=ICE-LAP3;
Contains:
RecName: Full=Caspase-7 subunit p20;
Contains:
RecName: Full=Caspase-7 subunit p11;
Flags: Precursor;
Name=CASP7; Synonyms=MCH3;
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 ALPHA AND BETA).
TISSUE=T-cell;
PubMed=8521391;
Fernandes-Alnemri T., Takahashi A., Armstrong R.C., Krebs J.,
Fritz L.C., Tomaselli K.J., Wang L., Yu Z., Croce C.M., Salveson G.,
Earnshaw W.C., Litwack G., Alnemri E.S.;
"Mch3, a novel human apoptotic cysteine protease highly related to
CPP32.";
Cancer Res. 55:6045-6052(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
PubMed=8576161; DOI=10.1074/jbc.271.3.1621;
Duan H., Chinnaiyan A.M., Hudson P.L., Wing J.P., He W.-W.,
Dixit V.M.;
"ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans
cell death protein Ced-3 is activated during Fas- and tumor necrosis
factor-induced apoptosis.";
J. Biol. Chem. 271:1621-1625(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
TISSUE=Spleen;
PubMed=8567622; DOI=10.1074/jbc.271.4.1825;
Lippke J.A., Gu Y., Sarnecki C., Caron P.R., Su M.S.-S.;
"Identification and characterization of CPP32/Mch2 homolog 1, a novel
cysteine protease similar to CPP32.";
J. Biol. Chem. 271:1825-1828(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND ALPHA').
TISSUE=Fetal lung, and Fetal spleen;
PubMed=9070923; DOI=10.1006/geno.1996.4548;
Juan T.S.-C., McNiece I.K., Argento J.M., Jenkins N.A., Gilbert D.J.,
Copeland N.G., Fletcher F.A.;
"Identification and mapping of Casp7, a cysteine protease resembling
CPP32 beta, interleukin-1 beta converting enzyme, and CED-3.";
Genomics 40:86-93(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), AND VARIANT
GLU-4.
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA').
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[9]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), AND VARIANT
GLU-4.
TISSUE=Skin;
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).
[11]
PROTEOLYTIC PROCESSING.
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).
[12]
INTERACTION WITH BIRC6/BRUCE.
PubMed=15200957; DOI=10.1016/j.molcel.2004.05.018;
Bartke T., Pohl C., Pyrowolakis G., Jentsch S.;
"Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3
ubiquitin ligase.";
Mol. Cell 14:801-811(2004).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
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).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 51-303, AND SUBUNIT.
PubMed=11701129; DOI=10.1016/S0092-8674(01)00544-X;
Chai J., Wu Q., Shiozaki E., Srinivasula S.M., Alnemri E.S., Shi Y.;
"Crystal structure of a procaspase-7 zymogen: mechanisms of activation
and substrate binding.";
Cell 107:399-407(2001).
-!- FUNCTION: Involved in the activation cascade of caspases
responsible for apoptosis execution. Cleaves and activates sterol
regulatory element binding proteins (SREBPs). Proteolytically
cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-
217' bond. Overexpression promotes programmed cell death.
-!- CATALYTIC ACTIVITY:
Reaction=Strict requirement for an Asp residue at position P1 and
has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-.;
EC=3.4.22.60;
-!- ACTIVITY REGULATION: Inhibited by isatin sulfonamides.
-!- SUBUNIT: Heterotetramer that consists of two anti-parallel
arranged heterodimers, each one formed by a 20 kDa (p20) and a 11
kDa (p11) subunit. Interacts with BIRC6/bruce.
{ECO:0000269|PubMed:11701129, ECO:0000269|PubMed:15200957}.
-!- INTERACTION:
Q13490:BIRC2; NbExp=2; IntAct=EBI-523958, EBI-514538;
Q9GZT8:NIF3L1; NbExp=4; IntAct=EBI-523958, EBI-740897;
Q13177:PAK2; NbExp=6; IntAct=EBI-523958, EBI-1045887;
P21673:SAT1; NbExp=5; IntAct=EBI-523958, EBI-711613;
P17405:SMPD1; NbExp=6; IntAct=EBI-523958, EBI-7095800;
P98170:XIAP; NbExp=2; IntAct=EBI-523958, EBI-517127;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=Alpha;
IsoId=P55210-1; Sequence=Displayed;
Name=Beta;
IsoId=P55210-2; Sequence=VSP_000807;
Note=Lacks enzymatic activity.;
Name=Alpha'; Synonyms=Beta;
IsoId=P55210-3; Sequence=VSP_000806;
Note=What we call isoform Alpha' is also known as Beta.
{ECO:0000305|PubMed:9070923};
Name=4;
IsoId=P55210-4; Sequence=VSP_045325;
-!- TISSUE SPECIFICITY: Highly expressed in lung, skeletal muscle,
liver, kidney, spleen and heart, and moderately in testis. No
expression in the brain.
-!- PTM: Cleavages by granzyme B or caspase-10 generate the two active
subunits. Propeptide domains can also be cleaved efficiently by
caspase-3. Active heterodimers between the small subunit of
caspase-7 and the large subunit of caspase-3, and vice versa, also
occur. {ECO:0000269|PubMed:8755496}.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
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EMBL; U37448; AAC50303.1; -; mRNA.
EMBL; U37449; AAC50304.1; -; mRNA.
EMBL; U39613; AAC50346.1; -; mRNA.
EMBL; U40281; AAC50352.1; -; mRNA.
EMBL; U67319; AAC51152.1; -; mRNA.
EMBL; U67320; AAC51153.1; -; mRNA.
EMBL; U67206; AAF21460.1; -; mRNA.
EMBL; BT006683; AAP35329.1; -; mRNA.
EMBL; AB451281; BAG70095.1; -; mRNA.
EMBL; AB451413; BAG70227.1; -; mRNA.
EMBL; AK298964; BAG61059.1; -; mRNA.
EMBL; AL592546; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL627395; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471066; EAW49494.1; -; Genomic_DNA.
EMBL; CH471066; EAW49495.1; -; Genomic_DNA.
EMBL; CH471066; EAW49498.1; -; Genomic_DNA.
EMBL; CH471066; EAW49496.1; -; Genomic_DNA.
EMBL; CH471066; EAW49497.1; -; Genomic_DNA.
EMBL; BC015799; AAH15799.1; -; mRNA.
CCDS; CCDS58096.1; -. [P55210-4]
CCDS; CCDS7580.1; -. [P55210-3]
CCDS; CCDS7581.1; -. [P55210-1]
CCDS; CCDS7582.1; -. [P55210-2]
RefSeq; NP_001218.1; NM_001227.4. [P55210-1]
RefSeq; NP_001253985.1; NM_001267056.1. [P55210-1]
RefSeq; NP_001253986.1; NM_001267057.1.
RefSeq; NP_001253987.1; NM_001267058.1. [P55210-4]
RefSeq; NP_001307840.1; NM_001320911.1.
RefSeq; NP_203124.1; NM_033338.5. [P55210-3]
RefSeq; NP_203125.1; NM_033339.4. [P55210-1]
RefSeq; NP_203126.1; NM_033340.3. [P55210-2]
UniGene; Hs.9216; -.
PDB; 1F1J; X-ray; 2.35 A; A/B=2-303.
PDB; 1GQF; X-ray; 2.90 A; A/B=47-303.
PDB; 1I4O; X-ray; 2.40 A; A/B=24-303.
PDB; 1I51; X-ray; 2.45 A; A/C=51-198, B/D=199-303.
PDB; 1K86; X-ray; 2.60 A; A/B=51-303.
PDB; 1K88; X-ray; 2.70 A; A/B=51-303.
PDB; 1KMC; X-ray; 2.90 A; A/B=1-303.
PDB; 1MIA; Model; -; A=57-193, B=211-303.
PDB; 1SHJ; X-ray; 2.80 A; A/B=50-303.
PDB; 1SHL; X-ray; 3.00 A; A/B=57-303.
PDB; 2QL5; X-ray; 2.34 A; A/C=24-196, B/D=207-303.
PDB; 2QL7; X-ray; 2.40 A; A/C=24-196, B/D=207-303.
PDB; 2QL9; X-ray; 2.14 A; A/C=24-196, B/D=207-303.
PDB; 2QLB; X-ray; 2.25 A; A/C=24-196, B/D=207-303.
PDB; 2QLF; X-ray; 2.80 A; A/C=24-196, B/D=207-303.
PDB; 2QLJ; X-ray; 2.60 A; A/C=24-196, B/D=207-303.
PDB; 3EDR; X-ray; 2.45 A; A/C=24-196, B/D=207-303.
PDB; 3H1P; X-ray; 2.61 A; A/B=50-303.
PDB; 3IBC; X-ray; 2.75 A; A/C=24-196, B/D=207-303.
PDB; 3IBF; X-ray; 2.50 A; A/C=24-196, B/D=207-303.
PDB; 3R5K; X-ray; 2.86 A; A/B=1-303.
PDB; 4FDL; X-ray; 2.80 A; A/B=2-303.
PDB; 4FEA; X-ray; 3.79 A; A/B=57-303.
PDB; 4HQ0; X-ray; 3.00 A; A/B=47-303.
PDB; 4HQR; X-ray; 3.00 A; A/B=47-303.
PDB; 4JB8; X-ray; 1.70 A; A=24-198, B=207-303.
PDB; 4JJ8; X-ray; 2.94 A; A/B=57-303.
PDB; 4JR1; X-ray; 2.15 A; A/B=57-303.
PDB; 4JR2; X-ray; 1.65 A; A/B=57-303.
PDB; 4LSZ; X-ray; 2.26 A; A/C=24-198, B/D=207-303.
PDB; 4ZVO; X-ray; 2.85 A; A/C=1-198, B/D=199-303.
PDB; 4ZVP; X-ray; 2.50 A; A/C=1-198, B/D=199-303.
PDB; 4ZVQ; X-ray; 2.50 A; A/C=1-198, B/D=199-303.
PDB; 4ZVR; X-ray; 2.30 A; A/C=1-198, B/D=199-303.
PDB; 4ZVS; X-ray; 2.50 A; A/C=1-198, B/D=199-303.
PDB; 4ZVT; X-ray; 2.85 A; A/C=1-198, B/D=199-303.
PDB; 4ZVU; X-ray; 2.60 A; A/C=1-198, B/D=199-303.
PDB; 5IC6; X-ray; 2.70 A; A/C=1-198, B/D=199-303.
PDB; 5K20; X-ray; 2.20 A; A/C=1-198, B/D=199-303.
PDB; 5V6U; X-ray; 2.80 A; A/B=1-303.
PDB; 5V6Z; X-ray; 2.60 A; A/B=1-303.
PDBsum; 1F1J; -.
PDBsum; 1GQF; -.
PDBsum; 1I4O; -.
PDBsum; 1I51; -.
PDBsum; 1K86; -.
PDBsum; 1K88; -.
PDBsum; 1KMC; -.
PDBsum; 1MIA; -.
PDBsum; 1SHJ; -.
PDBsum; 1SHL; -.
PDBsum; 2QL5; -.
PDBsum; 2QL7; -.
PDBsum; 2QL9; -.
PDBsum; 2QLB; -.
PDBsum; 2QLF; -.
PDBsum; 2QLJ; -.
PDBsum; 3EDR; -.
PDBsum; 3H1P; -.
PDBsum; 3IBC; -.
PDBsum; 3IBF; -.
PDBsum; 3R5K; -.
PDBsum; 4FDL; -.
PDBsum; 4FEA; -.
PDBsum; 4HQ0; -.
PDBsum; 4HQR; -.
PDBsum; 4JB8; -.
PDBsum; 4JJ8; -.
PDBsum; 4JR1; -.
PDBsum; 4JR2; -.
PDBsum; 4LSZ; -.
PDBsum; 4ZVO; -.
PDBsum; 4ZVP; -.
PDBsum; 4ZVQ; -.
PDBsum; 4ZVR; -.
PDBsum; 4ZVS; -.
PDBsum; 4ZVT; -.
PDBsum; 4ZVU; -.
PDBsum; 5IC6; -.
PDBsum; 5K20; -.
PDBsum; 5V6U; -.
PDBsum; 5V6Z; -.
ProteinModelPortal; P55210; -.
SMR; P55210; -.
BioGrid; 107290; 47.
ComplexPortal; CPX-2862; Caspase-7 complex.
DIP; DIP-29973N; -.
ELM; P55210; -.
IntAct; P55210; 18.
MINT; P55210; -.
STRING; 9606.ENSP00000358327; -.
BindingDB; P55210; -.
ChEMBL; CHEMBL3468; -.
DrugBank; DB03384; Fica.
DrugBank; DB05408; IDN-6556.
GuidetoPHARMACOLOGY; 1623; -.
MEROPS; C14.004; -.
iPTMnet; P55210; -.
PhosphoSitePlus; P55210; -.
BioMuta; CASP7; -.
DMDM; 1730092; -.
EPD; P55210; -.
jPOST; P55210; -.
MaxQB; P55210; -.
PaxDb; P55210; -.
PeptideAtlas; P55210; -.
PRIDE; P55210; -.
ProteomicsDB; 56811; -.
ProteomicsDB; 56812; -. [P55210-2]
ProteomicsDB; 56813; -. [P55210-3]
DNASU; 840; -.
Ensembl; ENST00000345633; ENSP00000298701; ENSG00000165806. [P55210-1]
Ensembl; ENST00000369315; ENSP00000358321; ENSG00000165806. [P55210-1]
Ensembl; ENST00000369318; ENSP00000358324; ENSG00000165806. [P55210-1]
Ensembl; ENST00000369331; ENSP00000358337; ENSG00000165806. [P55210-2]
Ensembl; ENST00000452490; ENSP00000398107; ENSG00000165806. [P55210-4]
Ensembl; ENST00000614447; ENSP00000478285; ENSG00000165806. [P55210-2]
Ensembl; ENST00000621345; ENSP00000480584; ENSG00000165806. [P55210-1]
Ensembl; ENST00000621607; ENSP00000478999; ENSG00000165806. [P55210-3]
GeneID; 840; -.
KEGG; hsa:840; -.
UCSC; uc001lam.5; human. [P55210-1]
CTD; 840; -.
DisGeNET; 840; -.
EuPathDB; HostDB:ENSG00000165806.19; -.
GeneCards; CASP7; -.
HGNC; HGNC:1508; CASP7.
HPA; CAB025563; -.
MIM; 601761; gene.
neXtProt; NX_P55210; -.
OpenTargets; ENSG00000165806; -.
PharmGKB; PA26091; -.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00940000153232; -.
HOVERGEN; HBG050802; -.
InParanoid; P55210; -.
KO; K04397; -.
OrthoDB; 984395at2759; -.
PhylomeDB; P55210; -.
TreeFam; TF102023; -.
BRENDA; 3.4.22.60; 2681.
Reactome; R-HSA-111459; Activation of caspases through apoptosome-mediated cleavage.
Reactome; R-HSA-111463; SMAC (DIABLO) binds to IAPs.
Reactome; R-HSA-111464; SMAC(DIABLO)-mediated dissociation of IAP:caspase complexes.
Reactome; R-HSA-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-HSA-111469; SMAC, XIAP-regulated apoptotic response.
Reactome; R-HSA-264870; Caspase-mediated cleavage of cytoskeletal proteins.
SIGNOR; P55210; -.
ChiTaRS; CASP7; human.
EvolutionaryTrace; P55210; -.
GeneWiki; Caspase_7; -.
GenomeRNAi; 840; -.
PMAP-CutDB; P55210; -.
PRO; PR:P55210; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000165806; Expressed in 211 organ(s), highest expression level in colonic mucosa.
ExpressionAtlas; P55210; baseline and differential.
Genevisible; P55210; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; TAS:Reactome.
GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IMP:CAFA.
GO; GO:0008234; F:cysteine-type peptidase activity; TAS:ProtInc.
GO; GO:0008233; F:peptidase activity; IDA:BHF-UCL.
GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
GO; GO:0072734; P:cellular response to staurosporine; IMP:CAFA.
GO; GO:0097194; P:execution phase of apoptosis; TAS:Reactome.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
CDD; cd00032; CASc; 1.
InterPro; IPR015471; Casp3/7.
InterPro; IPR029030; Caspase-like_dom_sf.
InterPro; IPR033139; Caspase_cys_AS.
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.
PANTHER; PTHR10454:SF31; PTHR10454:SF31; 1.
PRINTS; PR00376; IL1BCENZYME.
SMART; SM00115; CASc; 1.
SUPFAM; SSF52129; SSF52129; 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; Acetylation; Alternative splicing; Apoptosis;
Complete proteome; Cytoplasm; Hydrolase; Phosphoprotein; Polymorphism;
Protease; Reference proteome; Thiol protease; Zymogen.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
PROPEP 2 23 N-terminally processed.
/FTId=PRO_0000004616.
CHAIN 24 198 Caspase-7 subunit p20.
/FTId=PRO_0000004617.
PROPEP 199 206
/FTId=PRO_0000004618.
CHAIN 207 303 Caspase-7 subunit p11.
/FTId=PRO_0000004619.
ACT_SITE 144 144 {ECO:0000250}.
ACT_SITE 186 186
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
MOD_RES 37 37 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 36 MADDQGCIEEQGVEDSANEDSVDAKPDRSSFVPSLF -> M
QRGLFSDGDT (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045325.
VAR_SEQ 1 1 M -> MDCVGWPPGRKWHLEKNTSCGGSSGICASYVTQM
(in isoform Alpha').
{ECO:0000303|PubMed:19054851,
ECO:0000303|PubMed:8521391,
ECO:0000303|PubMed:9070923}.
/FTId=VSP_000806.
VAR_SEQ 149 303 VIYGKDGVTPIKDLTAHFRGDRCKTLLEKPKLFFIQACRGT
ELDDGIQADSGPINDTDANPRYKIPVEADFLFAYSTVPGYY
SWRSPGRGSWFVQALCSILEEHGKDLEIMQILTRVNDRVAR
HFESQSDDPHFHEKKQIPCVVSMLTKELYFSQ -> MESCS
VTQAGVQRRDLGRLQPPPPRLAEGPSLMMASRPTRGPSMTQ
MLILDTRSQWKLTSSSPIPRFQAITRGGAQEEAPGLCKPSA
PSWRSTEKTWKSCRSSPG (in isoform Beta).
{ECO:0000303|PubMed:8521391}.
/FTId=VSP_000807.
VARIANT 4 4 D -> E (in dbSNP:rs11555408).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.5}.
/FTId=VAR_048617.
VARIANT 255 255 D -> E (in dbSNP:rs2227310).
/FTId=VAR_048618.
MUTAGEN 186 186 C->A: No apoptotic activity.
CONFLICT 194 194 G -> A (in Ref. 2; AAC50346).
{ECO:0000305}.
HELIX 56 58 {ECO:0000244|PDB:4JB8}.
STRAND 64 66 {ECO:0000244|PDB:4JR2}.
STRAND 68 74 {ECO:0000244|PDB:4JR2}.
HELIX 80 82 {ECO:0000244|PDB:4JR2}.
HELIX 90 104 {ECO:0000244|PDB:4JR2}.
STRAND 106 113 {ECO:0000244|PDB:4JR2}.
HELIX 116 127 {ECO:0000244|PDB:4JR2}.
HELIX 131 133 {ECO:0000244|PDB:1F1J}.
STRAND 137 143 {ECO:0000244|PDB:4JR2}.
STRAND 149 152 {ECO:0000244|PDB:4JR2}.
STRAND 155 158 {ECO:0000244|PDB:4JR2}.
HELIX 159 163 {ECO:0000244|PDB:4JR2}.
HELIX 164 166 {ECO:0000244|PDB:4JR2}.
TURN 168 170 {ECO:0000244|PDB:4JR2}.
HELIX 172 174 {ECO:0000244|PDB:4JR2}.
STRAND 179 185 {ECO:0000244|PDB:4JR2}.
STRAND 188 190 {ECO:0000244|PDB:4JB8}.
TURN 209 211 {ECO:0000244|PDB:4JR1}.
TURN 215 218 {ECO:0000244|PDB:4JR2}.
STRAND 219 225 {ECO:0000244|PDB:4JR2}.
STRAND 227 229 {ECO:0000244|PDB:4HQ0}.
STRAND 232 234 {ECO:0000244|PDB:4JR2}.
TURN 235 237 {ECO:0000244|PDB:4JR2}.
HELIX 240 252 {ECO:0000244|PDB:4JR2}.
TURN 253 255 {ECO:0000244|PDB:4JR2}.
HELIX 258 272 {ECO:0000244|PDB:4JR2}.
TURN 276 278 {ECO:0000244|PDB:4ZVO}.
HELIX 280 282 {ECO:0000244|PDB:4JR2}.
STRAND 290 293 {ECO:0000244|PDB:4JR2}.
STRAND 296 298 {ECO:0000244|PDB:4JR2}.
SEQUENCE 303 AA; 34277 MW; CD373EE54A232CA4 CRC64;
MADDQGCIEE QGVEDSANED SVDAKPDRSS FVPSLFSKKK KNVTMRSIKT TRDRVPTYQY
NMNFEKLGKC IIINNKNFDK VTGMGVRNGT DKDAEALFKC FRSLGFDVIV YNDCSCAKMQ
DLLKKASEED HTNAACFACI LLSHGEENVI YGKDGVTPIK DLTAHFRGDR CKTLLEKPKL
FFIQACRGTE LDDGIQADSG PINDTDANPR YKIPVEADFL FAYSTVPGYY SWRSPGRGSW
FVQALCSILE EHGKDLEIMQ ILTRVNDRVA RHFESQSDDP HFHEKKQIPC VVSMLTKELY
FSQ


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Pathways :
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
WP1718: Vitamin B6 metabolism
WP1784: Apoptotic execution phase
WP2199: Seed Development
WP2231: Degradation of apoptotic cells
WP2272: Pathogenic Escherichia coli infection
WP2292: Chemokine signaling pathway
WP470: Proteasome Degradation
WP712: Estrogen signaling pathway

Related Genes :
[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]
[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]
[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]
[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]
[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]
[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]
[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]
[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]
[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) (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]
[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]
[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]
[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]
[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] 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]
[Drice ICE CG7788] Caspase (EC 3.4.22.-) (drICE) [Cleaved into: Caspase subunit p21; Caspase subunit p12]
[] Genome polyprotein [Cleaved into: N-terminal protease (N-pro) (EC 3.4.22.-) (Autoprotease p20); Capsid protein C; E(rns) glycoprotein (gp44/48); Envelope glycoprotein E1 (gp33); Envelope glycoprotein E2 (gp55); p7; Non-structural protein 2-3; Cysteine protease NS2 (EC 3.4.22.-) (Non-structural protein 2); Serine protease NS3 (EC 3.4.21.113) (EC 3.6.1.15) (EC 3.6.4.13) (Non-structural protein 3); Non-structural protein 4A (NS4A); Non-structural protein 4B (NS4B); Non-structural protein 5A (NS5A); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B)]
[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]
[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]
[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]
[csp-1 Y48E1B.13] Caspase A (EC 3.4.22.36) [Cleaved into: Caspase A subunit p16; Caspase A subunit p14]
[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]
[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] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[] Genome polyprotein [Cleaved into: N-terminal protease (N-pro) (EC 3.4.22.-) (Autoprotease p20); Capsid protein C; E(rns) glycoprotein (gp44/48); Envelope glycoprotein E1 (gp33); Envelope glycoprotein E2 (gp55); p7; Non-structural protein 2-3; Cysteine protease NS2 (EC 3.4.22.-) (Non-structural protein 2); Serine protease NS3 (EC 3.4.21.113) (EC 3.6.1.15) (EC 3.6.4.13) (Non-structural protein 3); Non-structural protein 4A (NS4A); Non-structural protein 4B (NS4B); Non-structural protein 5A (NS5A); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B)]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]

Bibliography :
[19617626] Calpain-1 cleaves and activates caspase-7.