ID CASP3_HUMAN Reviewed; 277 AA.
AC P42574; A8K5M2; D3DP53; Q96AN1; Q96KP2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 2.
DT 01-MAY-2013, entry version 159.
DE RecName: Full=Caspase-3;
DE Short=CASP-3;
DE EC=3.4.22.56;
DE AltName: Full=Apopain;
DE AltName: Full=Cysteine protease CPP32;
DE Short=CPP-32;
DE AltName: Full=Protein Yama;
DE AltName: Full=SREBP cleavage activity 1;
DE Short=SCA-1;
DE Contains:
DE RecName: Full=Caspase-3 subunit p17;
DE Contains:
DE RecName: Full=Caspase-3 subunit p12;
DE Flags: Precursor;
GN Name=CASP3; Synonyms=CPP32;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASP-190.
RC TISSUE=T-cell;
RX PubMed=7983002;
RA Fernandes-Alnemri T., Litwack G., Alnemri E.S.;
RT "CPP32, a novel human apoptotic protein with homology to
RT Caenorhabditis elegans cell death protein Ced-3 and mammalian
RT interleukin-1 beta-converting enzyme.";
RL J. Biol. Chem. 269:30761-30764(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7774019; DOI=10.1016/0092-8674(95)90541-3;
RA Tewari M., Quan L.T., O'Rourke K., Desnoyers S., Zeng Z.,
RA Beidler D.R., Poirier G.G., Salvesen G.S., Dixit V.M.;
RT "Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable
RT protease that cleaves the death substrate poly(ADP-ribose)
RT polymerase.";
RL Cell 81:801-809(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASP-190.
RX PubMed=15003516; DOI=10.1016/j.bbrc.2004.02.021;
RA Pelletier M., Cartron P.F., Delaval F., Meflah K., Vallette F.M.,
RA Oliver L.;
RT "Caspase 3 activation is controlled by a sequence located in the N-
RT terminus of its large subunit.";
RL Biochem. Biophys. Res. Commun. 316:93-99(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 29-46 AND 175-193, FUNCTION, AND VARIANT ASP-190.
RX PubMed=7596430; DOI=10.1038/376037a0;
RA Nicholson D.W., Ali A., Thornberry N.A., Vaillancourt J.P., Ding C.K.,
RA Gallant M., Gareau Y., Griffin P.R., Labelle M., Lazebnik Y.A.,
RA Munday N.A., Raju S.M., Smulson M.E., Yamin T.-T., Li V.L.,
RA Miller D.K.;
RT "Identification and inhibition of the ICE/CED-3 protease necessary for
RT mammalian apoptosis.";
RL Nature 376:37-43(1995).
RN [9]
RP PROTEOLYTIC PROCESSING.
RX PubMed=8755496; DOI=10.1073/pnas.93.15.7464;
RA Fernandes-Alnemri T., Armstrong R.C., Krebs J.F., Srinivasula S.M.,
RA Wang L., Bullrich F., Fritz L.C., Trapani J.A., Tomaselli K.J.,
RA Litwack G., Alnemri E.S.;
RT "In vitro activation of CPP32 and Mch3 by Mch4, a novel human
RT apoptotic cysteine protease containing two FADD-like domains.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:7464-7469(1996).
RN [10]
RP CLEAVAGE OF HUNTINGTIN.
RX PubMed=8696339; DOI=10.1038/ng0896-442;
RA Goldberg Y.P., Nicholson D.W., Rasper D.M., Kalchman M.A., Koide H.B.,
RA Graham R.K., Bromm M., Kazemi-Esfarjani P., Thornberry N.A.,
RA Vaillancourt J.P., Hayden M.R.;
RT "Cleavage of huntingtin by apopain, a proapoptotic cysteine protease,
RT is modulated by the polyglutamine tract.";
RL Nat. Genet. 13:442-449(1996).
RN [11]
RP S-NITROSYLATION.
RX PubMed=10213689; DOI=10.1126/science.284.5414.651;
RA Mannick J.B., Hausladen A., Liu L., Hess D.T., Zeng M., Miao Q.X.,
RA Kane L.S., Gow A.J., Stamler J.S.;
RT "Fas-induced caspase denitrosylation.";
RL Science 284:651-654(1999).
RN [12]
RP INTERACTION WITH BIRC6/BRUCE.
RX PubMed=15200957; DOI=10.1016/j.molcel.2004.05.018;
RA Bartke T., Pohl C., Pyrowolakis G., Jentsch S.;
RT "Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3
RT ubiquitin ligase.";
RL Mol. Cell 14:801-811(2004).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP FUNCTION IN CELL ADHESION.
RX PubMed=21357690; DOI=10.1074/jbc.M110.195461;
RA Cabrera J.R., Bouzas-Rodriguez J., Tauszig-Delamasure S., Mehlen P.;
RT "RET modulates cell adhesion via its cleavage by caspase in
RT sympathetic neurons.";
RL J. Biol. Chem. 286:14628-14638(2011).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 28-277.
RX PubMed=8673606; DOI=10.1038/nsb0796-619;
RA Rotonda J., Nicholson D.W., Fazil K.M., Gallant M., Gareau Y.,
RA Labelle M., Peterson E.P., Rasper D.M., Ruel R., Vaillancourt J.P.,
RA Thornberry N.A., Becker J.W.;
RT "The three-dimensional structure of apopain/CPP32, a key mediator of
RT apoptosis.";
RL Nat. Struct. Biol. 3:619-625(1996).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 35-173 AND 185-277.
RX PubMed=9045680; DOI=10.1074/jbc.272.10.6539;
RA Mittl P.R.E., di Marco S., Krebs J.F., Bai X., Karanewsky D.S.,
RA Priestle J.P., Tomaselli K.J., Gruetter M.G.;
RT "Structure of recombinant human CPP32 in complex with the tetrapeptide
RT acetyl-Asp-Val-Ala-Asp fluoromethyl ketone.";
RL J. Biol. Chem. 272:6539-6547(1997).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=10821855; DOI=10.1074/jbc.275.21.16007;
RA Lee D., Long S.A., Adams J.L., Chan G., Vaidya K.S., Francis T.A.,
RA Kikly K., Winkler J.D., Sung C.-M., Debouck C., Richardson S.,
RA Levy M.A., DeWolf W.E. Jr., Keller P.M., Tomaszek T., Head M.S.,
RA Ryan M.D., Haltiwanger R.C., Liang P.-H., Janson C.A., McDevitt P.J.,
RA Johanson K., Concha N.O., Chan W., Abdel-Meguid S.S., Badger A.M.,
RA Lark M.W., Nadeau D.P., Suva L.J., Gowen M., Nuttall M.E.;
RT "Potent and selective nonpeptide inhibitors of caspases 3 and 7
RT inhibit apoptosis and maintain cell functionality.";
RL J. Biol. Chem. 275:16007-16014(2000).
CC -!- FUNCTION: Involved in the activation cascade of caspases
CC responsible for apoptosis execution. At the onset of apoptosis it
CC proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a
CC '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory
CC element binding proteins (SREBPs) between the basic helix-loop-
CC helix leucine zipper domain and the membrane attachment domain.
CC Cleaves and activates caspase-6, -7 and -9. Involved in the
CC cleavage of huntingtin. Triggers cell adhesion in sympathetic
CC neurons through RET cleavage.
CC -!- CATALYTIC ACTIVITY: Strict requirement for an Asp residue at
CC positions P1 and P4. It has a preferred cleavage sequence of Asp-
CC Xaa-Xaa-Asp-|- with a hydrophobic amino-acid residue at P2 and a
CC hydrophilic amino-acid residue at P3, although Val or Ala are also
CC accepted at this position.
CC -!- ENZYME REGULATION: Inhibited by isatin sulfonamides.
CC -!- SUBUNIT: Heterotetramer that consists of two anti-parallel
CC arranged heterodimers, each one formed by a 17 kDa (p17) and a 12
CC kDa (p12) subunit. Interacts with BIRC6/bruce.
CC -!- INTERACTION:
CC Q9BYP7:WNK3; NbExp=2; IntAct=EBI-524064, EBI-1182602;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Highly expressed in lung, spleen, heart, liver
CC and kidney. Moderate levels in brain and skeletal muscle, and low
CC in testis. Also found in many cell lines, highest expression in
CC cells of the immune system.
CC -!- PTM: Cleavage by granzyme B, caspase-6, caspase-8 and caspase-10
CC generates the two active subunits. Additional processing of the
CC propeptides is likely due to the autocatalytic activity of the
CC activated protease. Active heterodimers between the small subunit
CC of caspase-7 protease and the large subunit of caspase-3 also
CC occur and vice versa.
CC -!- PTM: S-nitrosylated on its catalytic site cysteine in unstimulated
CC human cell lines and denitrosylated upon activation of the Fas
CC apoptotic pathway, associated with an increase in intracellular
CC caspase activity. Fas therefore activates caspase-3 not only by
CC inducing the cleavage of the caspase zymogen to its active
CC subunits, but also by stimulating the denitrosylation of its
CC active site thiol.
CC -!- SIMILARITY: Belongs to the peptidase C14A family.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/casp3/";
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DR EMBL; U13737; AAA65015.1; -; mRNA.
DR EMBL; U13738; AAB60355.1; -; mRNA.
DR EMBL; U26943; AAA74929.1; -; mRNA.
DR EMBL; AJ413269; CAC88866.1; -; mRNA.
DR EMBL; AK291337; BAF84026.1; -; mRNA.
DR EMBL; AY219866; AAO25654.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04673.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04674.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04675.1; -; Genomic_DNA.
DR EMBL; BC016926; AAH16926.1; -; mRNA.
DR IPI; IPI00292140; -.
DR PIR; A55315; A55315.
DR RefSeq; NP_004337.2; NM_004346.3.
DR RefSeq; NP_116786.1; NM_032991.2.
DR UniGene; Hs.141125; -.
DR PDB; 1CP3; X-ray; 2.30 A; A/B=1-277.
DR PDB; 1GFW; X-ray; 2.80 A; A=29-175, B=181-277.
DR PDB; 1I3O; X-ray; 2.70 A; A/C=1-175, B/D=176-277.
DR PDB; 1NME; X-ray; 1.60 A; A=29-174, B=186-277.
DR PDB; 1NMQ; X-ray; 2.40 A; A/B=29-277.
DR PDB; 1NMS; X-ray; 1.70 A; A/B=29-277.
DR PDB; 1PAU; X-ray; 2.50 A; A=29-175, B=176-277.
DR PDB; 1QX3; X-ray; 1.90 A; A=29-277.
DR PDB; 1RE1; X-ray; 2.50 A; A=29-175, B=176-277.
DR PDB; 1RHJ; X-ray; 2.20 A; A/C=29-175, B/D=176-277.
DR PDB; 1RHK; X-ray; 2.50 A; A=29-175, B=176-277.
DR PDB; 1RHM; X-ray; 2.50 A; A/C=29-175, B/D=176-277.
DR PDB; 1RHQ; X-ray; 3.00 A; A/D=29-175, B/E=176-277.
DR PDB; 1RHR; X-ray; 3.00 A; A=29-175, B=176-277.
DR PDB; 1RHU; X-ray; 2.51 A; A=29-175, B=176-277.
DR PDB; 2C1E; X-ray; 1.77 A; A=29-175, B=176-277.
DR PDB; 2C2K; X-ray; 1.87 A; A=29-175, B=176-277.
DR PDB; 2C2M; X-ray; 1.94 A; A=29-175, B=176-277.
DR PDB; 2C2O; X-ray; 2.45 A; A=29-175, B=176-277.
DR PDB; 2CDR; X-ray; 1.70 A; A=29-175, B=176-277.
DR PDB; 2CJX; X-ray; 1.70 A; A=29-175, B=176-277.
DR PDB; 2CJY; X-ray; 1.67 A; A=29-175, B=176-277.
DR PDB; 2CNK; X-ray; 1.75 A; A=29-175, B=176-277.
DR PDB; 2CNL; X-ray; 1.67 A; A=29-175, B=176-277.
DR PDB; 2CNN; X-ray; 1.70 A; A=29-175, B=176-277.
DR PDB; 2CNO; X-ray; 1.95 A; A=29-175, B=176-277.
DR PDB; 2DKO; X-ray; 1.06 A; A=29-174, B=176-277.
DR PDB; 2H5I; X-ray; 1.69 A; A=29-174, B=184-277.
DR PDB; 2H5J; X-ray; 2.00 A; A/C=29-174, B/D=184-277.
DR PDB; 2H65; X-ray; 2.30 A; A/C=29-174, B/D=184-277.
DR PDB; 2J30; X-ray; 1.40 A; A=29-277.
DR PDB; 2J31; X-ray; 1.50 A; A=29-277.
DR PDB; 2J32; X-ray; 1.30 A; A=29-277.
DR PDB; 2J33; X-ray; 2.00 A; A=29-277.
DR PDB; 2XYG; X-ray; 1.54 A; A=29-174, B=185-277.
DR PDB; 2XYH; X-ray; 1.89 A; A=29-174, B=185-277.
DR PDB; 2XYP; X-ray; 1.86 A; A=29-174, B=185-277.
DR PDB; 2XZD; X-ray; 2.10 A; A/C=29-175, B/D=176-277.
DR PDB; 2XZT; X-ray; 2.70 A; A/C=29-175, B/D=176-277.
DR PDB; 2Y0B; X-ray; 2.10 A; A/C=29-175, B/D=176-277.
DR PDB; 3DEH; X-ray; 2.50 A; A/B/C/D=29-277.
DR PDB; 3DEI; X-ray; 2.80 A; A/B/C/D=29-277.
DR PDB; 3DEJ; X-ray; 2.60 A; A/B/C/D=29-277.
DR PDB; 3DEK; X-ray; 2.40 A; A/B/C/D=29-277.
DR PDB; 3EDQ; X-ray; 1.61 A; A/C=29-175, B/D=176-277.
DR PDB; 3GJQ; X-ray; 2.60 A; A/C=29-175, B/D=176-277.
DR PDB; 3GJR; X-ray; 2.20 A; A/C=29-175, B/D=176-277.
DR PDB; 3GJS; X-ray; 1.90 A; A/C=29-175, B/D=176-277.
DR PDB; 3GJT; X-ray; 2.20 A; A/C=29-175, B/D=176-277.
DR PDB; 3H0E; X-ray; 2.00 A; A/B=29-277.
DR PDB; 3ITN; X-ray; 1.63 A; A=29-277.
DR PDB; 3KJF; X-ray; 2.00 A; A=29-175, B=176-277.
DR PDB; 3PCX; X-ray; 1.50 A; A=29-277.
DR PDB; 3PD0; X-ray; 2.00 A; A=29-277.
DR PDB; 3PD1; X-ray; 1.62 A; A=29-277.
DR PDB; 4DCJ; X-ray; 1.70 A; A/D=29-175, B/E=176-277.
DR PDB; 4DCO; X-ray; 1.70 A; A/D=29-175, B/E=176-277.
DR PDB; 4DCP; X-ray; 1.70 A; A/D=29-175, B/E=176-277.
DR PDB; 4EHA; X-ray; 1.70 A; A/C=1-277.
DR PDB; 4EHD; X-ray; 1.58 A; A=1-277.
DR PDB; 4EHF; X-ray; 1.66 A; A=1-277.
DR PDB; 4EHH; X-ray; 1.78 A; A=1-277.
DR PDB; 4EHK; X-ray; 1.67 A; A/C=1-277.
DR PDB; 4EHL; X-ray; 1.80 A; A/C=1-277.
DR PDB; 4EHN; X-ray; 1.69 A; A=1-277.
DR PDBsum; 1CP3; -.
DR PDBsum; 1GFW; -.
DR PDBsum; 1I3O; -.
DR PDBsum; 1NME; -.
DR PDBsum; 1NMQ; -.
DR PDBsum; 1NMS; -.
DR PDBsum; 1PAU; -.
DR PDBsum; 1QX3; -.
DR PDBsum; 1RE1; -.
DR PDBsum; 1RHJ; -.
DR PDBsum; 1RHK; -.
DR PDBsum; 1RHM; -.
DR PDBsum; 1RHQ; -.
DR PDBsum; 1RHR; -.
DR PDBsum; 1RHU; -.
DR PDBsum; 2C1E; -.
DR PDBsum; 2C2K; -.
DR PDBsum; 2C2M; -.
DR PDBsum; 2C2O; -.
DR PDBsum; 2CDR; -.
DR PDBsum; 2CJX; -.
DR PDBsum; 2CJY; -.
DR PDBsum; 2CNK; -.
DR PDBsum; 2CNL; -.
DR PDBsum; 2CNN; -.
DR PDBsum; 2CNO; -.
DR PDBsum; 2DKO; -.
DR PDBsum; 2H5I; -.
DR PDBsum; 2H5J; -.
DR PDBsum; 2H65; -.
DR PDBsum; 2J30; -.
DR PDBsum; 2J31; -.
DR PDBsum; 2J32; -.
DR PDBsum; 2J33; -.
DR PDBsum; 2XYG; -.
DR PDBsum; 2XYH; -.
DR PDBsum; 2XYP; -.
DR PDBsum; 2XZD; -.
DR PDBsum; 2XZT; -.
DR PDBsum; 2Y0B; -.
DR PDBsum; 3DEH; -.
DR PDBsum; 3DEI; -.
DR PDBsum; 3DEJ; -.
DR PDBsum; 3DEK; -.
DR PDBsum; 3EDQ; -.
DR PDBsum; 3GJQ; -.
DR PDBsum; 3GJR; -.
DR PDBsum; 3GJS; -.
DR PDBsum; 3GJT; -.
DR PDBsum; 3H0E; -.
DR PDBsum; 3ITN; -.
DR PDBsum; 3KJF; -.
DR PDBsum; 3PCX; -.
DR PDBsum; 3PD0; -.
DR PDBsum; 3PD1; -.
DR PDBsum; 4DCJ; -.
DR PDBsum; 4DCO; -.
DR PDBsum; 4DCP; -.
DR PDBsum; 4EHA; -.
DR PDBsum; 4EHD; -.
DR PDBsum; 4EHF; -.
DR PDBsum; 4EHH; -.
DR PDBsum; 4EHK; -.
DR PDBsum; 4EHL; -.
DR PDBsum; 4EHN; -.
DR ProteinModelPortal; P42574; -.
DR DIP; DIP-268N; -.
DR IntAct; P42574; 12.
DR MINT; MINT-147180; -.
DR STRING; 9606.ENSP00000311032; -.
DR MEROPS; C14.003; -.
DR PhosphoSite; P42574; -.
DR DMDM; 77416852; -.
DR OGP; P42574; -.
DR PaxDb; P42574; -.
DR PeptideAtlas; P42574; -.
DR PRIDE; P42574; -.
DR DNASU; 836; -.
DR Ensembl; ENST00000308394; ENSP00000311032; ENSG00000164305.
DR Ensembl; ENST00000523916; ENSP00000428929; ENSG00000164305.
DR GeneID; 836; -.
DR KEGG; hsa:836; -.
DR UCSC; uc003iwh.3; human.
DR CTD; 836; -.
DR GeneCards; GC04M185548; -.
DR HGNC; HGNC:1504; CASP3.
DR HPA; CAB000091; -.
DR HPA; CAB008381; -.
DR HPA; HPA002643; -.
DR MIM; 600636; gene.
DR neXtProt; NX_P42574; -.
DR PharmGKB; PA26087; -.
DR eggNOG; NOG279444; -.
DR HOGENOM; HOG000231878; -.
DR HOVERGEN; HBG050802; -.
DR InParanoid; P42574; -.
DR KO; K02187; -.
DR OMA; SSFVCVL; -.
DR OrthoDB; EOG4CZBGR; -.
DR PhylomeDB; P42574; -.
DR BRENDA; 3.4.22.56; 2681.
DR Pathway_Interaction_DB; a6b1_a6b4_integrin_pathway; a6b1 and a6b4 Integrin signaling.
DR Pathway_Interaction_DB; nfat_tfpathway; Calcineurin-regulated NFAT-dependent transcription in lymphocytes.
DR Pathway_Interaction_DB; caspase_pathway; Caspase cascade in apoptosis.
DR Pathway_Interaction_DB; faspathway; FAS signaling pathway (CD95).
DR Pathway_Interaction_DB; hivnefpathway; HIV-1 Nef: Negative effector of Fas and TNF-alpha.
DR Pathway_Interaction_DB; lysophospholipid_pathway; LPA receptor mediated events.
DR Pathway_Interaction_DB; p75ntrpathway; p75(NTR)-mediated signaling.
DR Pathway_Interaction_DB; nfat_3pathway; Role of Calcineurin-dependent NFAT signaling in lymphocytes.
DR Pathway_Interaction_DB; syndecan_2_pathway; Syndecan-2-mediated signaling events.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_578; Apoptosis.
DR BindingDB; P42574; -.
DR ChEMBL; CHEMBL2334; -.
DR DrugBank; DB01065; Melatonin.
DR DrugBank; DB01017; Minocycline.
DR DrugBank; DB00641; Simvastatin.
DR EvolutionaryTrace; P42574; -.
DR GenomeRNAi; 836; -.
DR NextBio; 3478; -.
DR PMAP-CutDB; P42574; -.
DR ArrayExpress; P42574; -.
DR Bgee; P42574; -.
DR CleanEx; HS_CASP3; -.
DR Genevestigator; P42574; -.
DR GermOnline; ENSG00000164305; Homo sapiens.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:Compara.
DR GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; IEA:Compara.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0008635; P:activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c; TAS:Reactome.
DR GO; GO:0006309; P:apoptotic DNA fragmentation; TAS:Reactome.
DR GO; GO:0097190; P:apoptotic signaling pathway; TAS:BHF-UCL.
DR GO; GO:0001782; P:B cell homeostasis; IEA:Compara.
DR GO; GO:0045165; P:cell fate commitment; IEA:Compara.
DR GO; GO:0071310; P:cellular response to organic substance; IEA:Compara.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IEA:Compara.
DR GO; GO:0007507; P:heart development; IEA:Compara.
DR GO; GO:0035329; P:hippo signaling cascade; TAS:Reactome.
DR GO; GO:0006917; P:induction of apoptosis; TAS:ProtInc.
DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IEA:Compara.
DR GO; GO:0030216; P:keratinocyte differentiation; IEA:Compara.
DR GO; GO:0046007; P:negative regulation of activated T cell proliferation; IEA:Compara.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IGI:MGI.
DR GO; GO:0030889; P:negative regulation of B cell proliferation; IEA:Compara.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:Compara.
DR GO; GO:0048011; P:nerve growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Compara.
DR GO; GO:0030264; P:nuclear fragmentation involved in apoptotic nuclear change; IMP:HGNC.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Compara.
DR GO; GO:0016485; P:protein processing; IEA:Compara.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; IEA:Compara.
DR GO; GO:0006974; P:response to DNA damage stimulus; IEA:Compara.
DR GO; GO:0034612; P:response to tumor necrosis factor; TAS:BHF-UCL.
DR GO; GO:0009411; P:response to UV; IEA:Compara.
DR GO; GO:0009611; P:response to wounding; IEA:Compara.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Compara.
DR GO; GO:0043029; P:T cell homeostasis; IEA:Compara.
DR InterPro; IPR015470; Caspase_3.
DR InterPro; IPR011600; Pept_C14_cat.
DR InterPro; IPR001309; Pept_C14_ICE_p20.
DR InterPro; IPR016129; Pept_C14_ICE_p20_AS.
DR InterPro; IPR002138; Pept_C14_p10.
DR InterPro; IPR002398; Pept_C14_p45.
DR InterPro; IPR015917; Pept_C14_p45_core.
DR PANTHER; PTHR10454; PTHR10454; 1.
DR PANTHER; PTHR10454:SF30; PTHR10454:SF30; 1.
DR Pfam; PF00656; Peptidase_C14; 1.
DR PRINTS; PR00376; IL1BCENZYME.
DR SMART; SM00115; CASc; 1.
DR PROSITE; PS01122; CASPASE_CYS; 1.
DR PROSITE; PS01121; CASPASE_HIS; 1.
DR PROSITE; PS50207; CASPASE_P10; 1.
DR PROSITE; PS50208; CASPASE_P20; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Hydrolase; Phosphoprotein; Polymorphism;
KW Protease; Reference proteome; S-nitrosylation; Thiol protease;
KW Zymogen.
FT PROPEP 1 9
FT /FTId=PRO_0000004569.
FT PROPEP 10 28
FT /FTId=PRO_0000004570.
FT CHAIN 29 175 Caspase-3 subunit p17.
FT /FTId=PRO_0000004571.
FT CHAIN 176 277 Caspase-3 subunit p12.
FT /FTId=PRO_0000004572.
FT ACT_SITE 121 121 By similarity.
FT ACT_SITE 163 163 By similarity.
FT MOD_RES 26 26 Phosphoserine (By similarity).
FT MOD_RES 163 163 S-nitrosocysteine; in inhibited form.
FT VARIANT 22 22 H -> R (in dbSNP:rs35578277).
FT /FTId=VAR_048616.
FT VARIANT 190 190 E -> D (in dbSNP:rs1049210).
FT /FTId=VAR_001401.
FT CONFLICT 31 36 ISLDNS -> MSWDTG (in Ref. 3; CAC88866).
FT STRAND 41 51
FT HELIX 57 59
FT HELIX 67 80
FT STRAND 84 90
FT HELIX 93 104
FT STRAND 111 120
FT STRAND 126 129
FT STRAND 132 135
FT HELIX 136 141
FT TURN 145 147
FT HELIX 149 151
FT STRAND 156 162
FT STRAND 164 167
FT TURN 183 185
FT TURN 189 192
FT STRAND 193 199
FT STRAND 206 208
FT TURN 209 211
FT HELIX 214 226
FT TURN 227 229
FT HELIX 232 246
FT TURN 254 258
FT STRAND 264 267
FT STRAND 270 272
SQ 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
//
