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P42574 (CASP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 170. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Caspase-3

Short name=CASP-3
EC=3.4.22.56
Alternative name(s):
Apopain
Cysteine protease CPP32
Short name=CPP-32
Protein Yama
SREBP cleavage activity 1
Short name=SCA-1

Cleaved into the following 2 chains:

  1. Caspase-3 subunit p17
  2. Caspase-3 subunit p12
Gene names
Name:CASP3
Synonyms:CPP32
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length277 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.8 Ref.15

Catalytic activity

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.

Enzyme regulation

Inhibited by isatin sulfonamides.

Subunit structure

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. Ref.12

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.

Post-translational modification

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.

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.

Sequence similarities

Belongs to the peptidase C14A family.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   Molecular functionHydrolase
Protease
Thiol protease
   PTMAcetylation
Phosphoprotein
S-nitrosylation
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processB cell homeostasis

Inferred from electronic annotation. Source: Ensembl

T cell homeostasis

Inferred from electronic annotation. Source: Ensembl

activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c

Traceable author statement. Source: Reactome

apoptotic DNA fragmentation

Traceable author statement. Source: Reactome

apoptotic process

Traceable author statement. Source: Reactome

apoptotic signaling pathway

Traceable author statement PubMed 10521396. Source: BHF-UCL

cell fate commitment

Inferred from electronic annotation. Source: Ensembl

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

cellular response to DNA damage stimulus

Inferred from electronic annotation. Source: Ensembl

erythrocyte differentiation

Inferred from direct assay PubMed 17167422. Source: UniProtKB

execution phase of apoptosis

Inferred from direct assay PubMed 8689682. Source: UniProtKB

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

extrinsic apoptotic signaling pathway via death domain receptors

Inferred from electronic annotation. Source: Ensembl

glial cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

heart development

Inferred from electronic annotation. Source: Ensembl

hippo signaling

Traceable author statement. Source: Reactome

intrinsic apoptotic signaling pathway

Traceable author statement. Source: Reactome

intrinsic apoptotic signaling pathway in response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

keratinocyte differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of B cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of activated T cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from genetic interaction PubMed 9353287. Source: MGI

negative regulation of cyclin-dependent protein serine/threonine kinase activity

Inferred from electronic annotation. Source: Ensembl

neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

platelet formation

Traceable author statement PubMed 18309324. Source: UniProtKB

positive regulation of apoptotic process

Traceable author statement. Source: Reactome

positive regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

proteolysis

Inferred from direct assay PubMed 12888622. Source: UniProtKB

regulation of apoptotic process

Traceable author statement. Source: Reactome

regulation of cysteine-type endopeptidase activity involved in apoptotic process

Traceable author statement. Source: Reactome

release of cytochrome c from mitochondria

Inferred from electronic annotation. Source: Ensembl

response to UV

Inferred from electronic annotation. Source: Ensembl

response to tumor necrosis factor

Traceable author statement PubMed 10521396. Source: BHF-UCL

response to wounding

Inferred from electronic annotation. Source: Ensembl

sensory perception of sound

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Inferred from direct assay PubMed 17167422. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 17167422. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionaspartic-type endopeptidase activity

Inferred from experiment. Source: Reactome

cyclin-dependent protein serine/threonine kinase inhibitor activity

Inferred from electronic annotation. Source: Ensembl

cysteine-type endopeptidase activity

Inferred from direct assay PubMed 19240112PubMed 21726810. Source: UniProtKB

cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype PubMed 10921886. Source: UniProtKB

cysteine-type endopeptidase activity involved in execution phase of apoptosis

Inferred from mutant phenotype PubMed 17559062. Source: UniProtKB

peptidase activity

Inferred from direct assay PubMed 17167422. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

WNK3Q9BYP72EBI-524064,EBI-1182602

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 99
PRO_0000004569
Propeptide10 – 2819
PRO_0000004570
Chain29 – 175147Caspase-3 subunit p17
PRO_0000004571
Chain176 – 277102Caspase-3 subunit p12
PRO_0000004572

Sites

Active site1211 By similarity
Active site1631 By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.13 Ref.16
Modified residue111N6-acetyllysine By similarity
Modified residue261Phosphoserine By similarity
Modified residue1631S-nitrosocysteine; in inhibited form Ref.11

Natural variations

Natural variant221H → R.
Corresponds to variant rs35578277 [ dbSNP | Ensembl ].
VAR_048616
Natural variant1901E → D. Ref.1 Ref.3 Ref.8
Corresponds to variant rs1049210 [ dbSNP | Ensembl ].
VAR_001401

Experimental info

Sequence conflict31 – 366ISLDNS → MSWDTG in CAC88866. Ref.3

Secondary structure

................................................ 277
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P42574 [UniParc].

Last modified October 11, 2005. Version 2.
Checksum: 2F35CD3BCF7FF64A

FASTA27731,608
        10         20         30         40         50         60 
MENTENSVDS KSIKNLEPKI IHGSESMDSG ISLDNSYKMD YPEMGLCIII NNKNFHKSTG 

        70         80         90        100        110        120 
MTSRSGTDVD AANLRETFRN LKYEVRNKND LTREEIVELM RDVSKEDHSK RSSFVCVLLS 

       130        140        150        160        170        180 
HGEEGIIFGT NGPVDLKKIT NFFRGDRCRS LTGKPKLFII QACRGTELDC GIETDSGVDD 

       190        200        210        220        230        240 
DMACHKIPVE ADFLYAYSTA PGYYSWRNSK DGSWFIQSLC AMLKQYADKL EFMHILTRVN 

       250        260        270 
RKVATEFESF SFDATFHAKK QIPCIVSMLT KELYFYH 

« Hide

References

« Hide 'large scale' references
[1]"CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 beta-converting enzyme."
Fernandes-Alnemri T., Litwack G., Alnemri E.S.
J. Biol. Chem. 269:30761-30764(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASP-190.
Tissue: T-cell.
[2]"Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase."
Tewari M., Quan L.T., O'Rourke K., Desnoyers S., Zeng Z., Beidler D.R., Poirier G.G., Salvesen G.S., Dixit V.M.
Cell 81:801-809(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Caspase 3 activation is controlled by a sequence located in the N-terminus of its large subunit."
Pelletier M., Cartron P.F., Delaval F., Meflah K., Vallette F.M., Oliver L.
Biochem. Biophys. Res. Commun. 316:93-99(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASP-190.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Tongue.
[5]NIEHS SNPs program
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lymph.
[8]"Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis."
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.
Nature 376:37-43(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 29-46 AND 175-193, FUNCTION, VARIANT ASP-190.
[9]"In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains."
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.
Proc. Natl. Acad. Sci. U.S.A. 93:7464-7469(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING.
[10]"Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract."
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.
Nat. Genet. 13:442-449(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE OF HUNTINGTIN.
[11]"Fas-induced caspase denitrosylation."
Mannick J.B., Hausladen A., Liu L., Hess D.T., Zeng M., Miao Q.X., Kane L.S., Gow A.J., Stamler J.S.
Science 284:651-654(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: S-NITROSYLATION AT CYS-163.
[12]"Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3 ubiquitin ligase."
Bartke T., Pohl C., Pyrowolakis G., Jentsch S.
Mol. Cell 14:801-811(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BIRC6/BRUCE.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"RET modulates cell adhesion via its cleavage by caspase in sympathetic neurons."
Cabrera J.R., Bouzas-Rodriguez J., Tauszig-Delamasure S., Mehlen P.
J. Biol. Chem. 286:14628-14638(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL ADHESION.
[16]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis."
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.
Nat. Struct. Biol. 3:619-625(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 28-277.
[18]"Structure of recombinant human CPP32 in complex with the tetrapeptide acetyl-Asp-Val-Ala-Asp fluoromethyl ketone."
Mittl P.R.E., di Marco S., Krebs J.F., Bai X., Karanewsky D.S., Priestle J.P., Tomaselli K.J., Gruetter M.G.
J. Biol. Chem. 272:6539-6547(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 35-173 AND 185-277.
[19]"Potent and selective nonpeptide inhibitors of caspases 3 and 7 inhibit apoptosis and maintain cell functionality."
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. expand/collapse author list , 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.
J. Biol. Chem. 275:16007-16014(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U13737 mRNA. Translation: AAA65015.1.
U13738 mRNA. Translation: AAB60355.1.
U26943 mRNA. Translation: AAA74929.1.
AJ413269 mRNA. Translation: CAC88866.1.
AK291337 mRNA. Translation: BAF84026.1.
AY219866 Genomic DNA. Translation: AAO25654.1.
CH471056 Genomic DNA. Translation: EAX04673.1.
CH471056 Genomic DNA. Translation: EAX04674.1.
CH471056 Genomic DNA. Translation: EAX04675.1.
BC016926 mRNA. Translation: AAH16926.1.
PIRA55315.
RefSeqNP_004337.2. NM_004346.3.
NP_116786.1. NM_032991.2.
UniGeneHs.141125.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CP3X-ray2.30A/B1-277[»]
1GFWX-ray2.80A29-175[»]
B181-277[»]
1I3OX-ray2.70A/C1-175[»]
B/D176-277[»]
1NMEX-ray1.60A29-174[»]
B186-277[»]
1NMQX-ray2.40A/B29-277[»]
1NMSX-ray1.70A/B29-277[»]
1PAUX-ray2.50A29-175[»]
B176-277[»]
1QX3X-ray1.90A29-277[»]
1RE1X-ray2.50A29-175[»]
B176-277[»]
1RHJX-ray2.20A/C29-175[»]
B/D176-277[»]
1RHKX-ray2.50A29-175[»]
B176-277[»]
1RHMX-ray2.50A/C29-175[»]
B/D176-277[»]
1RHQX-ray3.00A/D29-175[»]
B/E176-277[»]
1RHRX-ray3.00A29-175[»]
B176-277[»]
1RHUX-ray2.51A29-175[»]
B176-277[»]
2C1EX-ray1.77A29-175[»]
B176-277[»]
2C2KX-ray1.87A29-175[»]
B176-277[»]
2C2MX-ray1.94A29-175[»]
B176-277[»]
2C2OX-ray2.45A29-175[»]
B176-277[»]
2CDRX-ray1.70A29-175[»]
B176-277[»]
2CJXX-ray1.70A29-175[»]
B176-277[»]
2CJYX-ray1.67A29-175[»]
B176-277[»]
2CNKX-ray1.75A29-175[»]
B176-277[»]
2CNLX-ray1.67A29-175[»]
B176-277[»]
2CNNX-ray1.70A29-175[»]
B176-277[»]
2CNOX-ray1.95A29-175[»]
B176-277[»]
2DKOX-ray1.06A29-174[»]
B176-277[»]
2H5IX-ray1.69A29-174[»]
B184-277[»]
2H5JX-ray2.00A/C29-174[»]
B/D184-277[»]
2H65X-ray2.30A/C29-174[»]
B/D184-277[»]
2J30X-ray1.40A29-277[»]
2J31X-ray1.50A29-277[»]
2J32X-ray1.30A29-277[»]
2J33X-ray2.00A29-277[»]
2XYGX-ray1.54A29-174[»]
B185-277[»]
2XYHX-ray1.89A29-174[»]
B185-277[»]
2XYPX-ray1.86A29-174[»]
B185-277[»]
2XZDX-ray2.10A/C29-175[»]
B/D176-277[»]
2XZTX-ray2.70A/C29-175[»]
B/D176-277[»]
2Y0BX-ray2.10A/C29-175[»]
B/D176-277[»]
3DEHX-ray2.50A/B/C/D29-277[»]
3DEIX-ray2.80A/B/C/D29-277[»]
3DEJX-ray2.60A/B/C/D29-277[»]
3DEKX-ray2.40A/B/C/D29-277[»]
3EDQX-ray1.61A/C29-175[»]
B/D176-277[»]
3GJQX-ray2.60A/C29-175[»]
B/D176-277[»]
3GJRX-ray2.20A/C29-175[»]
B/D176-277[»]
3GJSX-ray1.90A/C29-175[»]
B/D176-277[»]
3GJTX-ray2.20A/C29-175[»]
B/D176-277[»]
3H0EX-ray2.00A/B29-277[»]
3ITNX-ray1.63A29-277[»]
3KJFX-ray2.00A29-175[»]
B176-277[»]
3PCXX-ray1.50A29-277[»]
3PD0X-ray2.00A29-277[»]
3PD1X-ray1.62A29-277[»]
4DCJX-ray1.70A/D29-175[»]
B/E176-277[»]
4DCOX-ray1.70A/D29-175[»]
B/E176-277[»]
4DCPX-ray1.70A/D29-175[»]
B/E176-277[»]
4EHAX-ray1.70A/C1-277[»]
4EHDX-ray1.58A1-277[»]
4EHFX-ray1.66A1-277[»]
4EHHX-ray1.78A1-277[»]
4EHKX-ray1.67A/C1-277[»]
4EHLX-ray1.80A/C1-277[»]
4EHNX-ray1.69A1-277[»]
4JJEX-ray1.48A29-277[»]
4JQYX-ray2.50A/B34-277[»]
4JQZX-ray2.89A/B34-277[»]
4JR0X-ray1.80A/B34-277[»]
ProteinModelPortalP42574.
SMRP42574. Positions 29-277.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107286. 74 interactions.
DIPDIP-268N.
IntActP42574. 21 interactions.
MINTMINT-147180.
STRING9606.ENSP00000311032.

Chemistry

BindingDBP42574.
ChEMBLCHEMBL2334.
DrugBankDB01065. Melatonin.
DB01017. Minocycline.
DB00641. Simvastatin.
GuidetoPHARMACOLOGY1619.

Protein family/group databases

MEROPSC14.003.

PTM databases

PhosphoSiteP42574.

Polymorphism databases

DMDM77416852.

2D gel databases

OGPP42574.

Proteomic databases

PaxDbP42574.
PeptideAtlasP42574.
PRIDEP42574.

Protocols and materials databases

DNASU836.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308394; ENSP00000311032; ENSG00000164305.
ENST00000523916; ENSP00000428929; ENSG00000164305.
GeneID836.
KEGGhsa:836.
UCSCuc003iwh.3. human.

Organism-specific databases

CTD836.
GeneCardsGC04M185548.
HGNCHGNC:1504. CASP3.
HPACAB000091.
CAB008381.
HPA002643.
MIM600636. gene.
neXtProtNX_P42574.
PharmGKBPA26087.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG279444.
HOGENOMHOG000231878.
HOVERGENHBG050802.
InParanoidP42574.
KOK02187.
OMASSFVCVL.
OrthoDBEOG7TTQ7K.
PhylomeDBP42574.
TreeFamTF102023.

Enzyme and pathway databases

BRENDA3.4.22.56. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.
REACT_578. Apoptosis.
SABIO-RKP42574.

Gene expression databases

ArrayExpressP42574.
BgeeP42574.
CleanExHS_CASP3.
GenevestigatorP42574.

Family and domain databases

InterProIPR011600. Pept_C14_caspase.
IPR001309. Pept_C14_ICE_p20.
IPR016129. Pept_C14_ICE_p20_AS.
IPR002138. Pept_C14_p10.
IPR015917. Pept_C14A_p45_core.
[Graphical view]
PfamPF00656. Peptidase_C14. 1 hit.
[Graphical view]
PRINTSPR00376. IL1BCENZYME.
SMARTSM00115. CASc. 1 hit.
[Graphical view]
PROSITEPS01122. CASPASE_CYS. 1 hit.
PS01121. CASPASE_HIS. 1 hit.
PS50207. CASPASE_P10. 1 hit.
PS50208. CASPASE_P20. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP42574.
GeneWikiCaspase_3.
GenomeRNAi836.
NextBio3478.
PMAP-CutDBP42574.
PROP42574.
SOURCESearch...

Entry information

Entry nameCASP3_HUMAN
AccessionPrimary (citable) accession number: P42574
Secondary accession number(s): A8K5M2 expand/collapse secondary AC list , D3DP53, Q96AN1, Q96KP2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 11, 2005
Last modified: April 16, 2014
This is version 170 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM