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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_HUMAN             Reviewed;         277 AA.
P42574; A8K5M2; D3DP53; Q96AN1; Q96KP2;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
11-OCT-2005, sequence version 2.
03-JUL-2019, entry version 221.
RecName: Full=Caspase-3;
Short=CASP-3;
EC=3.4.22.56;
AltName: Full=Apopain;
AltName: Full=Cysteine protease CPP32;
Short=CPP-32;
AltName: Full=Protein Yama;
AltName: Full=SREBP cleavage activity 1;
Short=SCA-1;
Contains:
RecName: Full=Caspase-3 subunit p17;
Contains:
RecName: Full=Caspase-3 subunit p12;
Flags: Precursor;
Name=CASP3; Synonyms=CPP32;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASP-190.
TISSUE=T-cell;
PubMed=7983002;
Fernandes-Alnemri T., Litwack G., Alnemri E.S.;
"CPP32, a novel human apoptotic protein with homology to
Caenorhabditis elegans cell death protein Ced-3 and mammalian
interleukin-1 beta-converting enzyme.";
J. Biol. Chem. 269:30761-30764(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7774019; DOI=10.1016/0092-8674(95)90541-3;
Tewari M., Quan L.T., O'Rourke K., Desnoyers S., Zeng Z.,
Beidler D.R., Poirier G.G., Salvesen G.S., Dixit V.M.;
"Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable
protease that cleaves the death substrate poly(ADP-ribose)
polymerase.";
Cell 81:801-809(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASP-190.
PubMed=15003516; DOI=10.1016/j.bbrc.2004.02.021;
Pelletier M., Cartron P.F., Delaval F., Meflah K., Vallette F.M.,
Oliver L.;
"Caspase 3 activation is controlled by a sequence located in the N-
terminus of its large subunit.";
Biochem. Biophys. Res. Commun. 316:93-99(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Tongue;
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).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[6]
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lymph;
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).
[8]
PROTEIN SEQUENCE OF 29-46 AND 176-193, FUNCTION, AND VARIANT ASP-190.
PubMed=7596430; DOI=10.1038/376037a0;
Nicholson D.W., Ali A., Thornberry N.A., Vaillancourt J.P., Ding C.K.,
Gallant M., Gareau Y., Griffin P.R., Labelle M., Lazebnik Y.A.,
Munday N.A., Raju S.M., Smulson M.E., Yamin T.-T., Li V.L.,
Miller D.K.;
"Identification and inhibition of the ICE/CED-3 protease necessary for
mammalian apoptosis.";
Nature 376:37-43(1995).
[9]
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).
[10]
CLEAVAGE OF HUNTINGTIN.
PubMed=8696339; DOI=10.1038/ng0896-442;
Goldberg Y.P., Nicholson D.W., Rasper D.M., Kalchman M.A., Koide H.B.,
Graham R.K., Bromm M., Kazemi-Esfarjani P., Thornberry N.A.,
Vaillancourt J.P., Hayden M.R.;
"Cleavage of huntingtin by apopain, a proapoptotic cysteine protease,
is modulated by the polyglutamine tract.";
Nat. Genet. 13:442-449(1996).
[11]
S-NITROSYLATION AT CYS-163.
PubMed=10213689; DOI=10.1126/science.284.5414.651;
Mannick J.B., Hausladen A., Liu L., Hess D.T., Zeng M., Miao Q.X.,
Kane L.S., Gow A.J., Stamler J.S.;
"Fas-induced caspase denitrosylation.";
Science 284:651-654(1999).
[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 MET-1, 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]
FUNCTION IN CELL ADHESION.
PubMed=21357690; DOI=10.1074/jbc.M110.195461;
Cabrera J.R., Bouzas-Rodriguez J., Tauszig-Delamasure S., Mehlen P.;
"RET modulates cell adhesion via its cleavage by caspase in
sympathetic neurons.";
J. Biol. Chem. 286:14628-14638(2011).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[18]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 28-277.
PubMed=8673606; DOI=10.1038/nsb0796-619;
Rotonda J., Nicholson D.W., Fazil K.M., Gallant M., Gareau Y.,
Labelle M., Peterson E.P., Rasper D.M., Ruel R., Vaillancourt J.P.,
Thornberry N.A., Becker J.W.;
"The three-dimensional structure of apopain/CPP32, a key mediator of
apoptosis.";
Nat. Struct. Biol. 3:619-625(1996).
[19]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 35-173 AND 185-277.
PubMed=9045680; DOI=10.1074/jbc.272.10.6539;
Mittl P.R.E., di Marco S., Krebs J.F., Bai X., Karanewsky D.S.,
Priestle J.P., Tomaselli K.J., Gruetter M.G.;
"Structure of recombinant human CPP32 in complex with the tetrapeptide
acetyl-Asp-Val-Ala-Asp fluoromethyl ketone.";
J. Biol. Chem. 272:6539-6547(1997).
[20]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
PubMed=10821855; DOI=10.1074/jbc.275.21.16007;
Lee D., Long S.A., Adams J.L., Chan G., Vaidya K.S., Francis T.A.,
Kikly K., Winkler J.D., Sung C.-M., Debouck C., Richardson S.,
Levy M.A., DeWolf W.E. Jr., Keller P.M., Tomaszek T., Head M.S.,
Ryan M.D., Haltiwanger R.C., Liang P.-H., Janson C.A., McDevitt P.J.,
Johanson K., Concha N.O., Chan W., Abdel-Meguid S.S., Badger A.M.,
Lark M.W., Nadeau D.P., Suva L.J., Gowen M., Nuttall M.E.;
"Potent and selective nonpeptide inhibitors of caspases 3 and 7
inhibit apoptosis and maintain cell functionality.";
J. Biol. Chem. 275:16007-16014(2000).
-!- FUNCTION: Involved in the activation cascade of caspases
responsible for apoptosis execution. At the onset of apoptosis it
proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a
'216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory
element binding proteins (SREBPs) between the basic helix-loop-
helix leucine zipper domain and the membrane attachment domain.
Cleaves and activates caspase-6, -7 and -9. Involved in the
cleavage of huntingtin. Triggers cell adhesion in sympathetic
neurons through RET cleavage. {ECO:0000269|PubMed:21357690,
ECO:0000269|PubMed:7596430}.
-!- CATALYTIC ACTIVITY:
Reaction=Strict requirement for an Asp residue at positions P1 and
P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-
Asp-|- with a hydrophobic amino-acid residue at P2 and a
hydrophilic amino-acid residue at P3, although Val or Ala are
also accepted at this position.; EC=3.4.22.56;
-!- ACTIVITY REGULATION: Inhibited by isatin sulfonamides.
-!- SUBUNIT: Heterotetramer that consists of two anti-parallel
arranged heterodimers, each one formed by a 17 kDa (p17) and a 12
kDa (p12) subunit. Interacts with BIRC6/bruce.
{ECO:0000269|PubMed:15200957}.
-!- INTERACTION:
O43823:AKAP8; NbExp=5; IntAct=EBI-524064, EBI-1237481;
Q9Y243:AKT3; NbExp=2; IntAct=EBI-524064, EBI-296115;
P55212:CASP6; NbExp=2; IntAct=EBI-524064, EBI-718729;
P55211:CASP9; NbExp=2; IntAct=EBI-524064, EBI-516799;
Q00987:MDM2; NbExp=2; IntAct=EBI-524064, EBI-389668;
P09874:PARP1; NbExp=2; IntAct=EBI-524064, EBI-355676;
P10599:TXN; NbExp=6; IntAct=EBI-524064, EBI-594644;
Q9BYP7:WNK3; NbExp=2; IntAct=EBI-524064, EBI-1182602;
P98170:XIAP; NbExp=3; IntAct=EBI-524064, EBI-517127;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: Highly expressed in lung, spleen, heart, liver
and kidney. Moderate levels in brain and skeletal muscle, and low
in testis. Also found in many cell lines, highest expression in
cells of the immune system.
-!- PTM: Cleavage by granzyme B, caspase-6, caspase-8 and caspase-10
generates the two active subunits. Additional processing of the
propeptides is likely due to the autocatalytic activity of the
activated protease. Active heterodimers between the small subunit
of caspase-7 protease and the large subunit of caspase-3 also
occur and vice versa.
-!- PTM: S-nitrosylated on its catalytic site cysteine in unstimulated
human cell lines and denitrosylated upon activation of the Fas
apoptotic pathway, associated with an increase in intracellular
caspase activity. Fas therefore activates caspase-3 not only by
inducing the cleavage of the caspase zymogen to its active
subunits, but also by stimulating the denitrosylation of its
active site thiol. {ECO:0000269|PubMed:10213689}.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/casp3/";
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EMBL; U13737; AAA65015.1; -; mRNA.
EMBL; U13738; AAB60355.1; -; mRNA.
EMBL; U26943; AAA74929.1; -; mRNA.
EMBL; AJ413269; CAC88866.1; -; mRNA.
EMBL; AK291337; BAF84026.1; -; mRNA.
EMBL; AY219866; AAO25654.1; -; Genomic_DNA.
EMBL; CH471056; EAX04673.1; -; Genomic_DNA.
EMBL; CH471056; EAX04674.1; -; Genomic_DNA.
EMBL; CH471056; EAX04675.1; -; Genomic_DNA.
EMBL; BC016926; AAH16926.1; -; mRNA.
CCDS; CCDS3836.1; -.
PIR; A55315; A55315.
RefSeq; NP_004337.2; NM_004346.3.
RefSeq; NP_116786.1; NM_032991.2.
RefSeq; XP_011530603.1; XM_011532301.1.
PDB; 1CP3; X-ray; 2.30 A; A/B=1-277.
PDB; 1GFW; X-ray; 2.80 A; A=29-175, B=181-277.
PDB; 1I3O; X-ray; 2.70 A; A/C=1-175, B/D=176-277.
PDB; 1NME; X-ray; 1.60 A; A=29-174, B=186-277.
PDB; 1NMQ; X-ray; 2.40 A; A/B=29-277.
PDB; 1NMS; X-ray; 1.70 A; A/B=29-277.
PDB; 1PAU; X-ray; 2.50 A; A=29-175, B=176-277.
PDB; 1QX3; X-ray; 1.90 A; A=29-277.
PDB; 1RE1; X-ray; 2.50 A; A=29-175, B=176-277.
PDB; 1RHJ; X-ray; 2.20 A; A/C=29-175, B/D=176-277.
PDB; 1RHK; X-ray; 2.50 A; A=29-175, B=176-277.
PDB; 1RHM; X-ray; 2.50 A; A/C=29-175, B/D=176-277.
PDB; 1RHQ; X-ray; 3.00 A; A/D=29-175, B/E=176-277.
PDB; 1RHR; X-ray; 3.00 A; A=29-175, B=176-277.
PDB; 1RHU; X-ray; 2.51 A; A=29-175, B=176-277.
PDB; 2C1E; X-ray; 1.77 A; A=29-175, B=176-277.
PDB; 2C2K; X-ray; 1.87 A; A=29-175, B=176-277.
PDB; 2C2M; X-ray; 1.94 A; A=29-175, B=176-277.
PDB; 2C2O; X-ray; 2.45 A; A=29-175, B=176-277.
PDB; 2CDR; X-ray; 1.70 A; A=29-175, B=176-277.
PDB; 2CJX; X-ray; 1.70 A; A=29-175, B=176-277.
PDB; 2CJY; X-ray; 1.67 A; A=29-175, B=176-277.
PDB; 2CNK; X-ray; 1.75 A; A=29-175, B=176-277.
PDB; 2CNL; X-ray; 1.67 A; A=29-175, B=176-277.
PDB; 2CNN; X-ray; 1.70 A; A=29-175, B=176-277.
PDB; 2CNO; X-ray; 1.95 A; A=29-175, B=176-277.
PDB; 2DKO; X-ray; 1.06 A; A=29-174, B=175-277.
PDB; 2H5I; X-ray; 1.69 A; A=29-174, B=184-277.
PDB; 2H5J; X-ray; 2.00 A; A/C=29-174, B/D=184-277.
PDB; 2H65; X-ray; 2.30 A; A/C=29-174, B/D=184-277.
PDB; 2J30; X-ray; 1.40 A; A=29-277.
PDB; 2J31; X-ray; 1.50 A; A=29-277.
PDB; 2J32; X-ray; 1.30 A; A=29-277.
PDB; 2J33; X-ray; 2.00 A; A=29-277.
PDB; 2XYG; X-ray; 1.54 A; A=29-174, B=185-277.
PDB; 2XYH; X-ray; 1.89 A; A=29-174, B=185-277.
PDB; 2XYP; X-ray; 1.86 A; A=29-174, B=185-277.
PDB; 2XZD; X-ray; 2.10 A; A/C=27-175, B/D=176-277.
PDB; 2XZT; X-ray; 2.70 A; A/C=29-175, B/D=176-277.
PDB; 2Y0B; X-ray; 2.10 A; A/C=29-175, B/D=176-277.
PDB; 3DEH; X-ray; 2.50 A; A/B/C/D=29-277.
PDB; 3DEI; X-ray; 2.80 A; A/B/C/D=29-277.
PDB; 3DEJ; X-ray; 2.60 A; A/B/C/D=29-277.
PDB; 3DEK; X-ray; 2.40 A; A/B/C/D=29-277.
PDB; 3EDQ; X-ray; 1.61 A; A/C=29-175, B/D=176-277.
PDB; 3GJQ; X-ray; 2.60 A; A/C=29-175, B/D=176-277.
PDB; 3GJR; X-ray; 2.20 A; A/C=29-175, B/D=176-277.
PDB; 3GJS; X-ray; 1.90 A; A/C=29-175, B/D=176-277.
PDB; 3GJT; X-ray; 2.20 A; A/C=29-175, B/D=176-277.
PDB; 3H0E; X-ray; 2.00 A; A/B=29-277.
PDB; 3ITN; X-ray; 1.63 A; A=29-277.
PDB; 3KJF; X-ray; 2.00 A; A=29-175, B=176-277.
PDB; 3PCX; X-ray; 1.50 A; A=29-277.
PDB; 3PD0; X-ray; 2.00 A; A=29-277.
PDB; 3PD1; X-ray; 1.62 A; A=29-277.
PDB; 4DCJ; X-ray; 1.70 A; A/D=29-175, B/E=176-277.
PDB; 4DCO; X-ray; 1.70 A; A/D=29-175, B/E=176-277.
PDB; 4DCP; X-ray; 1.70 A; A/D=29-175, B/E=176-277.
PDB; 4EHA; X-ray; 1.70 A; A/C=1-277.
PDB; 4EHD; X-ray; 1.58 A; A=1-277.
PDB; 4EHF; X-ray; 1.66 A; A=1-277.
PDB; 4EHH; X-ray; 1.78 A; A=1-277.
PDB; 4EHK; X-ray; 1.67 A; A/C=1-277.
PDB; 4EHL; X-ray; 1.80 A; A/C=1-277.
PDB; 4EHN; X-ray; 1.69 A; A=1-277.
PDB; 4JJE; X-ray; 1.48 A; A=29-277.
PDB; 4JQY; X-ray; 2.50 A; A/B=34-277.
PDB; 4JQZ; X-ray; 2.89 A; A/B=34-277.
PDB; 4JR0; X-ray; 1.80 A; A/B=34-277.
PDB; 4PRY; X-ray; 1.70 A; A=1-277.
PDB; 4PS0; X-ray; 1.63 A; A/B=1-277.
PDB; 4QTX; X-ray; 1.97 A; A=1-277.
PDB; 4QTY; X-ray; 1.60 A; A=29-277.
PDB; 4QU0; X-ray; 1.95 A; A=1-277.
PDB; 4QU5; X-ray; 1.91 A; A=1-277.
PDB; 4QU8; X-ray; 1.72 A; A=1-277.
PDB; 4QU9; X-ray; 1.56 A; A=1-277.
PDB; 4QUA; X-ray; 1.89 A; A=1-277.
PDB; 4QUB; X-ray; 1.69 A; A=1-277.
PDB; 4QUD; X-ray; 2.00 A; A/B=1-277.
PDB; 4QUE; X-ray; 1.84 A; A/C=1-277.
PDB; 4QUG; X-ray; 1.92 A; A/C=1-277.
PDB; 4QUH; X-ray; 1.76 A; A/C=1-277.
PDB; 4QUI; X-ray; 1.76 A; A/B=1-277.
PDB; 4QUJ; X-ray; 1.50 A; A=1-277.
PDB; 4QUL; X-ray; 1.90 A; A/C=1-277.
PDB; 5I9B; X-ray; 1.80 A; A=1-277.
PDB; 5I9T; X-ray; 1.95 A; A/C=1-277.
PDB; 5IAB; X-ray; 1.79 A; A/C=1-277.
PDB; 5IAE; X-ray; 1.55 A; A/C=1-277.
PDB; 5IAG; X-ray; 1.98 A; A=1-277.
PDB; 5IAJ; X-ray; 1.58 A; A=1-277.
PDB; 5IAK; X-ray; 1.82 A; A=1-277.
PDB; 5IAN; X-ray; 2.70 A; A=1-277.
PDB; 5IAR; X-ray; 1.76 A; A=1-277.
PDB; 5IAS; X-ray; 1.54 A; A=1-277.
PDB; 5IBC; X-ray; 1.66 A; A=1-277.
PDB; 5IBP; X-ray; 1.38 A; A=1-277.
PDB; 5IBR; X-ray; 1.74 A; A/C=1-277.
PDB; 5IC4; X-ray; 2.65 A; A/C/E/G=1-175, B/D/F/H=176-276.
PDBsum; 1CP3; -.
PDBsum; 1GFW; -.
PDBsum; 1I3O; -.
PDBsum; 1NME; -.
PDBsum; 1NMQ; -.
PDBsum; 1NMS; -.
PDBsum; 1PAU; -.
PDBsum; 1QX3; -.
PDBsum; 1RE1; -.
PDBsum; 1RHJ; -.
PDBsum; 1RHK; -.
PDBsum; 1RHM; -.
PDBsum; 1RHQ; -.
PDBsum; 1RHR; -.
PDBsum; 1RHU; -.
PDBsum; 2C1E; -.
PDBsum; 2C2K; -.
PDBsum; 2C2M; -.
PDBsum; 2C2O; -.
PDBsum; 2CDR; -.
PDBsum; 2CJX; -.
PDBsum; 2CJY; -.
PDBsum; 2CNK; -.
PDBsum; 2CNL; -.
PDBsum; 2CNN; -.
PDBsum; 2CNO; -.
PDBsum; 2DKO; -.
PDBsum; 2H5I; -.
PDBsum; 2H5J; -.
PDBsum; 2H65; -.
PDBsum; 2J30; -.
PDBsum; 2J31; -.
PDBsum; 2J32; -.
PDBsum; 2J33; -.
PDBsum; 2XYG; -.
PDBsum; 2XYH; -.
PDBsum; 2XYP; -.
PDBsum; 2XZD; -.
PDBsum; 2XZT; -.
PDBsum; 2Y0B; -.
PDBsum; 3DEH; -.
PDBsum; 3DEI; -.
PDBsum; 3DEJ; -.
PDBsum; 3DEK; -.
PDBsum; 3EDQ; -.
PDBsum; 3GJQ; -.
PDBsum; 3GJR; -.
PDBsum; 3GJS; -.
PDBsum; 3GJT; -.
PDBsum; 3H0E; -.
PDBsum; 3ITN; -.
PDBsum; 3KJF; -.
PDBsum; 3PCX; -.
PDBsum; 3PD0; -.
PDBsum; 3PD1; -.
PDBsum; 4DCJ; -.
PDBsum; 4DCO; -.
PDBsum; 4DCP; -.
PDBsum; 4EHA; -.
PDBsum; 4EHD; -.
PDBsum; 4EHF; -.
PDBsum; 4EHH; -.
PDBsum; 4EHK; -.
PDBsum; 4EHL; -.
PDBsum; 4EHN; -.
PDBsum; 4JJE; -.
PDBsum; 4JQY; -.
PDBsum; 4JQZ; -.
PDBsum; 4JR0; -.
PDBsum; 4PRY; -.
PDBsum; 4PS0; -.
PDBsum; 4QTX; -.
PDBsum; 4QTY; -.
PDBsum; 4QU0; -.
PDBsum; 4QU5; -.
PDBsum; 4QU8; -.
PDBsum; 4QU9; -.
PDBsum; 4QUA; -.
PDBsum; 4QUB; -.
PDBsum; 4QUD; -.
PDBsum; 4QUE; -.
PDBsum; 4QUG; -.
PDBsum; 4QUH; -.
PDBsum; 4QUI; -.
PDBsum; 4QUJ; -.
PDBsum; 4QUL; -.
PDBsum; 5I9B; -.
PDBsum; 5I9T; -.
PDBsum; 5IAB; -.
PDBsum; 5IAE; -.
PDBsum; 5IAG; -.
PDBsum; 5IAJ; -.
PDBsum; 5IAK; -.
PDBsum; 5IAN; -.
PDBsum; 5IAR; -.
PDBsum; 5IAS; -.
PDBsum; 5IBC; -.
PDBsum; 5IBP; -.
PDBsum; 5IBR; -.
PDBsum; 5IC4; -.
SMR; P42574; -.
BioGrid; 107286; 103.
ComplexPortal; CPX-970; Caspase-3 complex.
DIP; DIP-268N; -.
ELM; P42574; -.
IntAct; P42574; 55.
MINT; P42574; -.
STRING; 9606.ENSP00000311032; -.
BindingDB; P42574; -.
ChEMBL; CHEMBL2334; -.
DrugBank; DB06862; 2-HYDROXY-5-(2-MERCAPTO-ETHYLSULFAMOYL)-BENZOIC ACID.
DrugBank; DB08251; 4-[5-(2-CARBOXY-1-FORMYL-ETHYLCARBAMOYL)-PYRIDIN-3-YL]-BENZOIC ACID.
DrugBank; DB03124; 5-[4-(1-Carboxymethyl-2-Oxo-Propylcarbamoyl)-Benzylsulfamoyl]-2-Hydroxy-Benzoic Acid.
DrugBank; DB08229; [N-(3-DIBENZYLCARBAMOYL-OXIRANECARBONYL)-HYDRAZINO]-ACETIC ACID.
DrugBank; DB05408; IDN-6556.
DrugBank; DB07696; methyl (3S)-3-[(tert-butoxycarbonyl)amino]-4-oxopentanoate.
DrugBank; DB01017; Minocycline.
GuidetoPHARMACOLOGY; 1619; -.
MEROPS; C14.003; -.
iPTMnet; P42574; -.
PhosphoSitePlus; P42574; -.
BioMuta; CASP3; -.
DMDM; 77416852; -.
OGP; P42574; -.
EPD; P42574; -.
jPOST; P42574; -.
MaxQB; P42574; -.
PaxDb; P42574; -.
PeptideAtlas; P42574; -.
PRIDE; P42574; -.
ProteomicsDB; 55518; -.
DNASU; 836; -.
Ensembl; ENST00000308394; ENSP00000311032; ENSG00000164305.
Ensembl; ENST00000523916; ENSP00000428929; ENSG00000164305.
GeneID; 836; -.
KEGG; hsa:836; -.
UCSC; uc003iwh.3; human.
CTD; 836; -.
DisGeNET; 836; -.
GeneCards; CASP3; -.
HGNC; HGNC:1504; CASP3.
HPA; CAB000091; -.
HPA; CAB008381; -.
HPA; HPA002643; -.
MIM; 600636; gene.
neXtProt; NX_P42574; -.
OpenTargets; ENSG00000164305; -.
PharmGKB; PA26087; -.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00940000153232; -.
HOGENOM; HOG000231878; -.
InParanoid; P42574; -.
KO; K02187; -.
OMA; YSWRNSR; -.
OrthoDB; 984395at2759; -.
PhylomeDB; P42574; -.
TreeFam; TF102023; -.
BRENDA; 3.4.22.56; 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-140342; Apoptosis induced DNA fragmentation.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
Reactome; R-HSA-2028269; Signaling by Hippo.
Reactome; R-HSA-205025; NADE modulates death signalling.
Reactome; R-HSA-211736; Stimulation of the cell death response by PAK-2p34.
Reactome; R-HSA-264870; Caspase-mediated cleavage of cytoskeletal proteins.
Reactome; R-HSA-351906; Apoptotic cleavage of cell adhesion proteins.
Reactome; R-HSA-418889; Caspase activation via Dependence Receptors in the absence of ligand.
Reactome; R-HSA-449836; Other interleukin signaling.
SABIO-RK; P42574; -.
SIGNOR; P42574; -.
ChiTaRS; CASP3; human.
EvolutionaryTrace; P42574; -.
GeneWiki; Caspase_3; -.
GenomeRNAi; 836; -.
PMAP-CutDB; P42574; -.
PRO; PR:P42574; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000164305; Expressed in 194 organ(s), highest expression level in jejunal mucosa.
ExpressionAtlas; P42574; baseline and differential.
Genevisible; P42574; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0031264; C:death-inducing signaling complex; IEA:Ensembl.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:Ensembl.
GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; IEA:Ensembl.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0097199; F:cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IMP:UniProtKB.
GO; GO:0005123; F:death receptor binding; IEA:Ensembl.
GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
GO; GO:0016005; F:phospholipase A2 activator activity; IEA:Ensembl.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
GO; GO:0061713; P:anterior neural tube closure; IEA:Ensembl.
GO; GO:0006309; P:apoptotic DNA fragmentation; TAS:Reactome.
GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
GO; GO:0097190; P:apoptotic signaling pathway; TAS:BHF-UCL.
GO; GO:0007413; P:axonal fasciculation; IEA:Ensembl.
GO; GO:0001782; P:B cell homeostasis; IEA:Ensembl.
GO; GO:0045165; P:cell fate commitment; IEA:Ensembl.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:Ensembl.
GO; GO:0072734; P:cellular response to staurosporine; IMP:CAFA.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0030218; P:erythrocyte differentiation; IDA:UniProtKB.
GO; GO:0097194; P:execution phase of apoptosis; IDA:UniProtKB.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; TAS:Reactome.
GO; GO:0034349; P:glial cell apoptotic process; IEA:Ensembl.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0035329; P:hippo signaling; TAS:Reactome.
GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
GO; GO:0008627; P:intrinsic apoptotic signaling pathway in response to osmotic stress; IEA:Ensembl.
GO; GO:0030216; P:keratinocyte differentiation; IBA:GO_Central.
GO; GO:0007611; P:learning or memory; IEA:Ensembl.
GO; GO:0071887; P:leukocyte apoptotic process; IEA:Ensembl.
GO; GO:0001554; P:luteolysis; IEA:Ensembl.
GO; GO:0046007; P:negative regulation of activated T cell proliferation; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IGI:MGI.
GO; GO:0030889; P:negative regulation of B cell proliferation; IEA:Ensembl.
GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; IDA:MGI.
GO; GO:0030220; P:platelet formation; TAS:UniProtKB.
GO; GO:1902004; P:positive regulation of amyloid-beta formation; IDA:UniProtKB.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0016485; P:protein processing; IEA:Ensembl.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0016241; P:regulation of macroautophagy; TAS:ParkinsonsUK-UCL.
GO; GO:0031647; P:regulation of protein stability; IDA:UniProtKB.
GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
GO; GO:0032025; P:response to cobalt ion; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
GO; GO:0009749; P:response to glucose; IEA:Ensembl.
GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
GO; GO:0034612; P:response to tumor necrosis factor; TAS:BHF-UCL.
GO; GO:0009411; P:response to UV; IEA:Ensembl.
GO; GO:0010165; P:response to X-ray; IEA:Ensembl.
GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
GO; GO:0051146; P:striated muscle cell differentiation; IEA:Ensembl.
GO; GO:0043029; P:T cell homeostasis; IEA:Ensembl.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
CDD; cd00032; CASc; 1.
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.
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; Apoptosis; Complete proteome; Cytoplasm;
Direct protein sequencing; Hydrolase; Phosphoprotein; Polymorphism;
Protease; Reference proteome; S-nitrosylation; Thiol protease;
Zymogen.
PROPEP 1 9
/FTId=PRO_0000004569.
PROPEP 10 28 {ECO:0000269|PubMed:7596430}.
/FTId=PRO_0000004570.
CHAIN 29 175 Caspase-3 subunit p17.
/FTId=PRO_0000004571.
CHAIN 176 277 Caspase-3 subunit p12.
/FTId=PRO_0000004572.
ACT_SITE 121 121 {ECO:0000250}.
ACT_SITE 163 163 {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
MOD_RES 11 11 N6-acetyllysine.
{ECO:0000250|UniProtKB:P70677}.
MOD_RES 26 26 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 163 163 S-nitrosocysteine; in inhibited form.
{ECO:0000269|PubMed:10213689}.
VARIANT 22 22 H -> R (in dbSNP:rs35578277).
/FTId=VAR_048616.
VARIANT 190 190 E -> D (in dbSNP:rs1049210).
{ECO:0000269|PubMed:15003516,
ECO:0000269|PubMed:7596430,
ECO:0000269|PubMed:7983002}.
/FTId=VAR_001401.
CONFLICT 31 36 ISLDNS -> MSWDTG (in Ref. 3; CAC88866).
{ECO:0000305}.
STRAND 41 51 {ECO:0000244|PDB:2DKO}.
HELIX 57 59 {ECO:0000244|PDB:2DKO}.
HELIX 67 80 {ECO:0000244|PDB:2DKO}.
STRAND 84 90 {ECO:0000244|PDB:2DKO}.
HELIX 93 105 {ECO:0000244|PDB:2DKO}.
HELIX 108 110 {ECO:0000244|PDB:1I3O}.
STRAND 111 120 {ECO:0000244|PDB:2DKO}.
STRAND 126 129 {ECO:0000244|PDB:2DKO}.
STRAND 132 135 {ECO:0000244|PDB:2DKO}.
HELIX 136 141 {ECO:0000244|PDB:2DKO}.
TURN 145 147 {ECO:0000244|PDB:2DKO}.
HELIX 149 151 {ECO:0000244|PDB:2DKO}.
STRAND 156 162 {ECO:0000244|PDB:2DKO}.
STRAND 165 167 {ECO:0000244|PDB:2DKO}.
STRAND 178 181 {ECO:0000244|PDB:2DKO}.
TURN 183 185 {ECO:0000244|PDB:1NMS}.
TURN 189 192 {ECO:0000244|PDB:2DKO}.
STRAND 193 199 {ECO:0000244|PDB:2DKO}.
STRAND 206 208 {ECO:0000244|PDB:2DKO}.
TURN 209 211 {ECO:0000244|PDB:2DKO}.
HELIX 214 226 {ECO:0000244|PDB:2DKO}.
TURN 227 229 {ECO:0000244|PDB:2DKO}.
HELIX 232 246 {ECO:0000244|PDB:2DKO}.
HELIX 254 256 {ECO:0000244|PDB:2DKO}.
STRAND 264 267 {ECO:0000244|PDB:2DKO}.
STRAND 270 272 {ECO:0000244|PDB:2DKO}.
SEQUENCE 277 AA; 31608 MW; 2F35CD3BCF7FF64A CRC64;
MENTENSVDS KSIKNLEPKI IHGSESMDSG ISLDNSYKMD YPEMGLCIII NNKNFHKSTG
MTSRSGTDVD AANLRETFRN LKYEVRNKND LTREEIVELM RDVSKEDHSK RSSFVCVLLS
HGEEGIIFGT NGPVDLKKIT NFFRGDRCRS LTGKPKLFII QACRGTELDC GIETDSGVDD
DMACHKIPVE ADFLYAYSTA PGYYSWRNSK DGSWFIQSLC AMLKQYADKL EFMHILTRVN
RKVATEFESF SFDATFHAKK QIPCIVSMLT KELYFYH


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WP1939: Unfolded Protein Response

Related Genes :
[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]
[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 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]
[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]
[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]
[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]
[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) (Apopain) (Cysteine protease CPP32) [Cleaved into: Caspase-3 subunit p17; Caspase-3 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]
[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]
[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]
[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]
[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 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]
[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] 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]
[Casp6] 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 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]
[Drice ICE CG7788] Caspase (EC 3.4.22.-) (drICE) [Cleaved into: Caspase subunit p21; Caspase subunit p12]
[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] Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (xCPP32) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[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]
[gag-pol] Gag-Pol polyprotein [Cleaved into: Matrix protein p19; p2A; p2B; p10; Capsid protein p27, alternate cleaved 1; Capsid protein p27, alternate cleaved 2; Spacer peptide (SP) (p3); Nucleocapsid protein p12; Protease p15 (EC 3.4.23.-); Reverse transcriptase, beta-subunit (RT-beta); Reverse transcriptase, alpha-subunit (RT-alpha) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-) (pp32); p4]
[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.-.-)]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]

Bibliography :
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