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Database: UniProt
Entry: P42574
LinkDB: P42574
Original site: P42574 
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   09-JUL-2014, entry version 173.
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 AT CYS-163.
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   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [14]
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   [15]
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   [16]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.M111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
RA   Meinnel T., Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [17]
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   [18]
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   [19]
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   CCDS; CCDS3836.1; -.
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=175-277.
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=27-175, 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   PDB; 4JJE; X-ray; 1.48 A; A=29-277.
DR   PDB; 4JQY; X-ray; 2.50 A; A/B=34-277.
DR   PDB; 4JQZ; X-ray; 2.89 A; A/B=34-277.
DR   PDB; 4JR0; X-ray; 1.80 A; A/B=34-277.
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   PDBsum; 4JJE; -.
DR   PDBsum; 4JQY; -.
DR   PDBsum; 4JQZ; -.
DR   PDBsum; 4JR0; -.
DR   ProteinModelPortal; P42574; -.
DR   SMR; P42574; 29-277.
DR   BioGrid; 107286; 74.
DR   DIP; DIP-268N; -.
DR   IntAct; P42574; 21.
DR   MINT; MINT-147180; -.
DR   STRING; 9606.ENSP00000311032; -.
DR   BindingDB; P42574; -.
DR   ChEMBL; CHEMBL2334; -.
DR   DrugBank; DB01065; Melatonin.
DR   DrugBank; DB01017; Minocycline.
DR   DrugBank; DB00641; Simvastatin.
DR   GuidetoPHARMACOLOGY; 1619; -.
DR   MEROPS; C14.003; -.
DR   PhosphoSite; P42574; -.
DR   DMDM; 77416852; -.
DR   OGP; P42574; -.
DR   MaxQB; 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; EOG7TTQ7K; -.
DR   PhylomeDB; P42574; -.
DR   TreeFam; TF102023; -.
DR   BRENDA; 3.4.22.56; 2681.
DR   Reactome; REACT_111102; Signal Transduction.
DR   Reactome; REACT_118779; Extracellular matrix organization.
DR   Reactome; REACT_578; Apoptosis.
DR   SABIO-RK; P42574; -.
DR   EvolutionaryTrace; P42574; -.
DR   GeneWiki; Caspase_3; -.
DR   GenomeRNAi; 836; -.
DR   NextBio; 3478; -.
DR   PMAP-CutDB; P42574; -.
DR   PRO; PR:P42574; -.
DR   ArrayExpress; P42574; -.
DR   Bgee; P42574; -.
DR   CleanEx; HS_CASP3; -.
DR   Genevestigator; P42574; -.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; EXP:Reactome.
DR   GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; IEA:Ensembl.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
DR   GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IMP:UniProtKB.
DR   GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI: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:0006915; P:apoptotic process; TAS:Reactome.
DR   GO; GO:0097190; P:apoptotic signaling pathway; TAS:BHF-UCL.
DR   GO; GO:0001782; P:B cell homeostasis; IEA:Ensembl.
DR   GO; GO:0045165; P:cell fate commitment; IEA:Ensembl.
DR   GO; GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; TAS:Reactome.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:Ensembl.
DR   GO; GO:0030218; P:erythrocyte differentiation; IDA:UniProtKB.
DR   GO; GO:0097194; P:execution phase of apoptosis; IDA:UniProtKB.
DR   GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
DR   GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
DR   GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR   GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR   GO; GO:0034349; P:glial cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   GO; GO:0035329; P:hippo signaling; TAS:Reactome.
DR   GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:Reactome.
DR   GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IEA:Ensembl.
DR   GO; GO:0030216; P:keratinocyte differentiation; IBA:RefGenome.
DR   GO; GO:0046007; P:negative regulation of activated T cell proliferation; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IGI:MGI.
DR   GO; GO:0030889; P:negative regulation of B cell proliferation; IEA:Ensembl.
DR   GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:Ensembl.
DR   GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0030182; P:neuron differentiation; IBA:RefGenome.
DR   GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0030220; P:platelet formation; TAS:UniProtKB.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome.
DR   GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR   GO; GO:0042981; P:regulation of apoptotic process; TAS:Reactome.
DR   GO; GO:0043281; P:regulation of cysteine-type endopeptidase activity involved in apoptotic process; TAS:Reactome.
DR   GO; GO:0001836; P:release of cytochrome c from mitochondria; IEA:Ensembl.
DR   GO; GO:0034612; P:response to tumor necrosis factor; TAS:BHF-UCL.
DR   GO; GO:0009411; P:response to UV; IEA:Ensembl.
DR   GO; GO:0009611; P:response to wounding; IEA:Ensembl.
DR   GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR   GO; GO:0043029; P:T cell homeostasis; IEA:Ensembl.
DR   Gene3D; 3.40.50.1460; -; 1.
DR   InterPro; IPR029030; Caspase-like_dom.
DR   InterPro; IPR015470; Caspase_3.
DR   InterPro; IPR011600; Pept_C14_caspase.
DR   InterPro; IPR001309; Pept_C14_ICE_p20.
DR   InterPro; IPR016129; Pept_C14_ICE_p20_AS.
DR   InterPro; IPR002138; Pept_C14_p10.
DR   InterPro; IPR015917; Pept_C14A_p45_core.
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; Acetylation; 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       1      1       N-acetylmethionine.
FT   MOD_RES      11     11       N6-acetyllysine (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    105
FT   HELIX       108    110
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      165    167
FT   STRAND      178    181
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   HELIX       254    256
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
//
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