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P42574

- CASP3_HUMAN

UniProt

P42574 - CASP3_HUMAN

Protein

Caspase-3

Gene

CASP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 175 (01 Oct 2014)
      Sequence version 2 (11 Oct 2005)
      Previous versions | rss
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    Functioni

    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.2 Publications

    Catalytic activityi

    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 regulationi

    Inhibited by isatin sulfonamides.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei121 – 1211By similarity
    Active sitei163 – 1631By similarity

    GO - Molecular functioni

    1. aspartic-type endopeptidase activity Source: Reactome
    2. cyclin-dependent protein serine/threonine kinase inhibitor activity Source: Ensembl
    3. cysteine-type endopeptidase activity Source: UniProtKB
    4. cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    5. cysteine-type endopeptidase activity involved in execution phase of apoptosis Source: UniProtKB
    6. peptidase activity Source: UniProtKB
    7. protein binding Source: UniProtKB

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c Source: Reactome
    2. apoptotic DNA fragmentation Source: Reactome
    3. apoptotic process Source: Reactome
    4. apoptotic signaling pathway Source: BHF-UCL
    5. B cell homeostasis Source: Ensembl
    6. cell fate commitment Source: Ensembl
    7. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
    8. cellular response to DNA damage stimulus Source: Ensembl
    9. erythrocyte differentiation Source: UniProtKB
    10. execution phase of apoptosis Source: UniProtKB
    11. extracellular matrix disassembly Source: Reactome
    12. extracellular matrix organization Source: Reactome
    13. extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
    14. extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
    15. glial cell apoptotic process Source: Ensembl
    16. heart development Source: Ensembl
    17. hippo signaling Source: Reactome
    18. intrinsic apoptotic signaling pathway Source: Reactome
    19. intrinsic apoptotic signaling pathway in response to oxidative stress Source: Ensembl
    20. keratinocyte differentiation Source: RefGenome
    21. negative regulation of activated T cell proliferation Source: Ensembl
    22. negative regulation of apoptotic process Source: MGI
    23. negative regulation of B cell proliferation Source: Ensembl
    24. negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: Ensembl
    25. neuron apoptotic process Source: Ensembl
    26. neuron differentiation Source: RefGenome
    27. neurotrophin TRK receptor signaling pathway Source: Reactome
    28. platelet formation Source: UniProtKB
    29. positive regulation of apoptotic process Source: Reactome
    30. positive regulation of neuron apoptotic process Source: Ensembl
    31. proteolysis Source: UniProtKB
    32. regulation of apoptotic process Source: Reactome
    33. regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Reactome
    34. release of cytochrome c from mitochondria Source: Ensembl
    35. response to tumor necrosis factor Source: BHF-UCL
    36. response to UV Source: Ensembl
    37. response to wounding Source: Ensembl
    38. sensory perception of sound Source: Ensembl
    39. T cell homeostasis Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Apoptosis

    Enzyme and pathway databases

    BRENDAi3.4.22.56. 2681.
    ReactomeiREACT_107. Apoptotic cleavage of cellular proteins.
    REACT_118572. Degradation of the extracellular matrix.
    REACT_118607. Signaling by Hippo.
    REACT_13462. Activation of DNA fragmentation factor.
    REACT_13526. NADE modulates death signalling.
    REACT_13532. Stimulation of the cell death response by PAK-2p34.
    REACT_13541. Caspase-mediated cleavage of cytoskeletal proteins.
    REACT_13579. Apoptotic cleavage of cell adhesion proteins.
    REACT_22128. Role of DCC in regulating apoptosis.
    REACT_607. Activation of caspases through apoptosome-mediated cleavage.
    SABIO-RKP42574.

    Protein family/group databases

    MEROPSiC14.003.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Caspase-3 (EC:3.4.22.56)
    Short name:
    CASP-3
    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:
    Gene namesi
    Name:CASP3
    Synonyms:CPP32
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:1504. CASP3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB
    4. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26087.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 99PRO_0000004569
    Propeptidei10 – 28191 PublicationPRO_0000004570Add
    BLAST
    Chaini29 – 175147Caspase-3 subunit p17PRO_0000004571Add
    BLAST
    Chaini176 – 277102Caspase-3 subunit p12PRO_0000004572Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei11 – 111N6-acetyllysineBy similarity
    Modified residuei26 – 261PhosphoserineBy similarity
    Modified residuei163 – 1631S-nitrosocysteine; in inhibited form1 Publication

    Post-translational modificationi

    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.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, S-nitrosylation, Zymogen

    Proteomic databases

    MaxQBiP42574.
    PaxDbiP42574.
    PeptideAtlasiP42574.
    PRIDEiP42574.

    2D gel databases

    OGPiP42574.

    PTM databases

    PhosphoSiteiP42574.

    Miscellaneous databases

    PMAP-CutDBP42574.

    Expressioni

    Tissue specificityi

    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.

    Gene expression databases

    ArrayExpressiP42574.
    BgeeiP42574.
    CleanExiHS_CASP3.
    GenevestigatoriP42574.

    Organism-specific databases

    HPAiCAB000091.
    CAB008381.
    HPA002643.

    Interactioni

    Subunit structurei

    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.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AKT3Q9Y2432EBI-524064,EBI-296115
    MDM2Q009872EBI-524064,EBI-389668
    WNK3Q9BYP72EBI-524064,EBI-1182602
    XIAPP981702EBI-524064,EBI-517127

    Protein-protein interaction databases

    BioGridi107286. 74 interactions.
    DIPiDIP-268N.
    IntActiP42574. 39 interactions.
    MINTiMINT-147180.
    STRINGi9606.ENSP00000311032.

    Structurei

    Secondary structure

    1
    277
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi41 – 5111
    Helixi57 – 593
    Helixi67 – 8014
    Beta strandi84 – 907
    Helixi93 – 10513
    Helixi108 – 1103
    Beta strandi111 – 12010
    Beta strandi126 – 1294
    Beta strandi132 – 1354
    Helixi136 – 1416
    Turni145 – 1473
    Helixi149 – 1513
    Beta strandi156 – 1627
    Beta strandi165 – 1673
    Beta strandi178 – 1814
    Turni183 – 1853
    Turni189 – 1924
    Beta strandi193 – 1997
    Beta strandi206 – 2083
    Turni209 – 2113
    Helixi214 – 22613
    Turni227 – 2293
    Helixi232 – 24615
    Helixi254 – 2563
    Beta strandi264 – 2674
    Beta strandi270 – 2723

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    B175-277[»]
    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/C27-175[»]
    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[»]
    ProteinModelPortaliP42574.
    SMRiP42574. Positions 29-277.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP42574.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C14A family.Curated

    Phylogenomic databases

    eggNOGiNOG279444.
    HOGENOMiHOG000231878.
    HOVERGENiHBG050802.
    InParanoidiP42574.
    KOiK02187.
    OMAiSSFVCVL.
    OrthoDBiEOG7TTQ7K.
    PhylomeDBiP42574.
    TreeFamiTF102023.

    Family and domain databases

    Gene3Di3.40.50.1460. 1 hit.
    InterProiIPR029030. Caspase-like_dom.
    IPR015470. Caspase_3.
    IPR011600. 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]
    PANTHERiPTHR10454:SF30. PTHR10454:SF30. 1 hit.
    PfamiPF00656. Peptidase_C14. 1 hit.
    [Graphical view]
    PRINTSiPR00376. IL1BCENZYME.
    SMARTiSM00115. CASc. 1 hit.
    [Graphical view]
    PROSITEiPS01122. CASPASE_CYS. 1 hit.
    PS01121. CASPASE_HIS. 1 hit.
    PS50207. CASPASE_P10. 1 hit.
    PS50208. CASPASE_P20. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P42574-1 [UniParc]FASTAAdd to Basket

    « Hide

    MENTENSVDS KSIKNLEPKI IHGSESMDSG ISLDNSYKMD YPEMGLCIII    50
    NNKNFHKSTG MTSRSGTDVD AANLRETFRN LKYEVRNKND LTREEIVELM 100
    RDVSKEDHSK RSSFVCVLLS HGEEGIIFGT NGPVDLKKIT NFFRGDRCRS 150
    LTGKPKLFII QACRGTELDC GIETDSGVDD DMACHKIPVE ADFLYAYSTA 200
    PGYYSWRNSK DGSWFIQSLC AMLKQYADKL EFMHILTRVN RKVATEFESF 250
    SFDATFHAKK QIPCIVSMLT KELYFYH 277
    Length:277
    Mass (Da):31,608
    Last modified:October 11, 2005 - v2
    Checksum:i2F35CD3BCF7FF64A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti31 – 366ISLDNS → MSWDTG in CAC88866. (PubMed:15003516)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti22 – 221H → R.
    Corresponds to variant rs35578277 [ dbSNP | Ensembl ].
    VAR_048616
    Natural varianti190 – 1901E → D.3 Publications
    Corresponds to variant rs1049210 [ dbSNP | Ensembl ].
    VAR_001401

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS3836.1.
    PIRiA55315.
    RefSeqiNP_004337.2. NM_004346.3.
    NP_116786.1. NM_032991.2.
    UniGeneiHs.141125.

    Genome annotation databases

    EnsembliENST00000308394; ENSP00000311032; ENSG00000164305.
    ENST00000523916; ENSP00000428929; ENSG00000164305.
    GeneIDi836.
    KEGGihsa:836.
    UCSCiuc003iwh.3. human.

    Polymorphism databases

    DMDMi77416852.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS3836.1.
    PIRi A55315.
    RefSeqi NP_004337.2. NM_004346.3.
    NP_116786.1. NM_032991.2.
    UniGenei Hs.141125.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CP3 X-ray 2.30 A/B 1-277 [» ]
    1GFW X-ray 2.80 A 29-175 [» ]
    B 181-277 [» ]
    1I3O X-ray 2.70 A/C 1-175 [» ]
    B/D 176-277 [» ]
    1NME X-ray 1.60 A 29-174 [» ]
    B 186-277 [» ]
    1NMQ X-ray 2.40 A/B 29-277 [» ]
    1NMS X-ray 1.70 A/B 29-277 [» ]
    1PAU X-ray 2.50 A 29-175 [» ]
    B 176-277 [» ]
    1QX3 X-ray 1.90 A 29-277 [» ]
    1RE1 X-ray 2.50 A 29-175 [» ]
    B 176-277 [» ]
    1RHJ X-ray 2.20 A/C 29-175 [» ]
    B/D 176-277 [» ]
    1RHK X-ray 2.50 A 29-175 [» ]
    B 176-277 [» ]
    1RHM X-ray 2.50 A/C 29-175 [» ]
    B/D 176-277 [» ]
    1RHQ X-ray 3.00 A/D 29-175 [» ]
    B/E 176-277 [» ]
    1RHR X-ray 3.00 A 29-175 [» ]
    B 176-277 [» ]
    1RHU X-ray 2.51 A 29-175 [» ]
    B 176-277 [» ]
    2C1E X-ray 1.77 A 29-175 [» ]
    B 176-277 [» ]
    2C2K X-ray 1.87 A 29-175 [» ]
    B 176-277 [» ]
    2C2M X-ray 1.94 A 29-175 [» ]
    B 176-277 [» ]
    2C2O X-ray 2.45 A 29-175 [» ]
    B 176-277 [» ]
    2CDR X-ray 1.70 A 29-175 [» ]
    B 176-277 [» ]
    2CJX X-ray 1.70 A 29-175 [» ]
    B 176-277 [» ]
    2CJY X-ray 1.67 A 29-175 [» ]
    B 176-277 [» ]
    2CNK X-ray 1.75 A 29-175 [» ]
    B 176-277 [» ]
    2CNL X-ray 1.67 A 29-175 [» ]
    B 176-277 [» ]
    2CNN X-ray 1.70 A 29-175 [» ]
    B 176-277 [» ]
    2CNO X-ray 1.95 A 29-175 [» ]
    B 176-277 [» ]
    2DKO X-ray 1.06 A 29-174 [» ]
    B 175-277 [» ]
    2H5I X-ray 1.69 A 29-174 [» ]
    B 184-277 [» ]
    2H5J X-ray 2.00 A/C 29-174 [» ]
    B/D 184-277 [» ]
    2H65 X-ray 2.30 A/C 29-174 [» ]
    B/D 184-277 [» ]
    2J30 X-ray 1.40 A 29-277 [» ]
    2J31 X-ray 1.50 A 29-277 [» ]
    2J32 X-ray 1.30 A 29-277 [» ]
    2J33 X-ray 2.00 A 29-277 [» ]
    2XYG X-ray 1.54 A 29-174 [» ]
    B 185-277 [» ]
    2XYH X-ray 1.89 A 29-174 [» ]
    B 185-277 [» ]
    2XYP X-ray 1.86 A 29-174 [» ]
    B 185-277 [» ]
    2XZD X-ray 2.10 A/C 27-175 [» ]
    B/D 176-277 [» ]
    2XZT X-ray 2.70 A/C 29-175 [» ]
    B/D 176-277 [» ]
    2Y0B X-ray 2.10 A/C 29-175 [» ]
    B/D 176-277 [» ]
    3DEH X-ray 2.50 A/B/C/D 29-277 [» ]
    3DEI X-ray 2.80 A/B/C/D 29-277 [» ]
    3DEJ X-ray 2.60 A/B/C/D 29-277 [» ]
    3DEK X-ray 2.40 A/B/C/D 29-277 [» ]
    3EDQ X-ray 1.61 A/C 29-175 [» ]
    B/D 176-277 [» ]
    3GJQ X-ray 2.60 A/C 29-175 [» ]
    B/D 176-277 [» ]
    3GJR X-ray 2.20 A/C 29-175 [» ]
    B/D 176-277 [» ]
    3GJS X-ray 1.90 A/C 29-175 [» ]
    B/D 176-277 [» ]
    3GJT X-ray 2.20 A/C 29-175 [» ]
    B/D 176-277 [» ]
    3H0E X-ray 2.00 A/B 29-277 [» ]
    3ITN X-ray 1.63 A 29-277 [» ]
    3KJF X-ray 2.00 A 29-175 [» ]
    B 176-277 [» ]
    3PCX X-ray 1.50 A 29-277 [» ]
    3PD0 X-ray 2.00 A 29-277 [» ]
    3PD1 X-ray 1.62 A 29-277 [» ]
    4DCJ X-ray 1.70 A/D 29-175 [» ]
    B/E 176-277 [» ]
    4DCO X-ray 1.70 A/D 29-175 [» ]
    B/E 176-277 [» ]
    4DCP X-ray 1.70 A/D 29-175 [» ]
    B/E 176-277 [» ]
    4EHA X-ray 1.70 A/C 1-277 [» ]
    4EHD X-ray 1.58 A 1-277 [» ]
    4EHF X-ray 1.66 A 1-277 [» ]
    4EHH X-ray 1.78 A 1-277 [» ]
    4EHK X-ray 1.67 A/C 1-277 [» ]
    4EHL X-ray 1.80 A/C 1-277 [» ]
    4EHN X-ray 1.69 A 1-277 [» ]
    4JJE X-ray 1.48 A 29-277 [» ]
    4JQY X-ray 2.50 A/B 34-277 [» ]
    4JQZ X-ray 2.89 A/B 34-277 [» ]
    4JR0 X-ray 1.80 A/B 34-277 [» ]
    ProteinModelPortali P42574.
    SMRi P42574. Positions 29-277.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107286. 74 interactions.
    DIPi DIP-268N.
    IntActi P42574. 39 interactions.
    MINTi MINT-147180.
    STRINGi 9606.ENSP00000311032.

    Chemistry

    BindingDBi P42574.
    ChEMBLi CHEMBL2334.
    DrugBanki DB01065. Melatonin.
    DB01017. Minocycline.
    DB00641. Simvastatin.
    GuidetoPHARMACOLOGYi 1619.

    Protein family/group databases

    MEROPSi C14.003.

    PTM databases

    PhosphoSitei P42574.

    Polymorphism databases

    DMDMi 77416852.

    2D gel databases

    OGPi P42574.

    Proteomic databases

    MaxQBi P42574.
    PaxDbi P42574.
    PeptideAtlasi P42574.
    PRIDEi P42574.

    Protocols and materials databases

    DNASUi 836.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000308394 ; ENSP00000311032 ; ENSG00000164305 .
    ENST00000523916 ; ENSP00000428929 ; ENSG00000164305 .
    GeneIDi 836.
    KEGGi hsa:836.
    UCSCi uc003iwh.3. human.

    Organism-specific databases

    CTDi 836.
    GeneCardsi GC04M185548.
    HGNCi HGNC:1504. CASP3.
    HPAi CAB000091.
    CAB008381.
    HPA002643.
    MIMi 600636. gene.
    neXtProti NX_P42574.
    PharmGKBi PA26087.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG279444.
    HOGENOMi HOG000231878.
    HOVERGENi HBG050802.
    InParanoidi P42574.
    KOi K02187.
    OMAi SSFVCVL.
    OrthoDBi EOG7TTQ7K.
    PhylomeDBi P42574.
    TreeFami TF102023.

    Enzyme and pathway databases

    BRENDAi 3.4.22.56. 2681.
    Reactomei REACT_107. Apoptotic cleavage of cellular proteins.
    REACT_118572. Degradation of the extracellular matrix.
    REACT_118607. Signaling by Hippo.
    REACT_13462. Activation of DNA fragmentation factor.
    REACT_13526. NADE modulates death signalling.
    REACT_13532. Stimulation of the cell death response by PAK-2p34.
    REACT_13541. Caspase-mediated cleavage of cytoskeletal proteins.
    REACT_13579. Apoptotic cleavage of cell adhesion proteins.
    REACT_22128. Role of DCC in regulating apoptosis.
    REACT_607. Activation of caspases through apoptosome-mediated cleavage.
    SABIO-RK P42574.

    Miscellaneous databases

    EvolutionaryTracei P42574.
    GeneWikii Caspase_3.
    GenomeRNAii 836.
    NextBioi 3478.
    PMAP-CutDB P42574.
    PROi P42574.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P42574.
    Bgeei P42574.
    CleanExi HS_CASP3.
    Genevestigatori P42574.

    Family and domain databases

    Gene3Di 3.40.50.1460. 1 hit.
    InterProi IPR029030. Caspase-like_dom.
    IPR015470. Caspase_3.
    IPR011600. 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 ]
    PANTHERi PTHR10454:SF30. PTHR10454:SF30. 1 hit.
    Pfami PF00656. Peptidase_C14. 1 hit.
    [Graphical view ]
    PRINTSi PR00376. IL1BCENZYME.
    SMARTi SM00115. CASc. 1 hit.
    [Graphical view ]
    PROSITEi PS01122. CASPASE_CYS. 1 hit.
    PS01121. CASPASE_HIS. 1 hit.
    PS50207. CASPASE_P10. 1 hit.
    PS50208. CASPASE_P20. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. Cited for: PROTEIN SEQUENCE OF 29-46 AND 176-193, 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. 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. 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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

    Entry informationi

    Entry nameiCASP3_HUMAN
    AccessioniPrimary (citable) accession number: P42574
    Secondary accession number(s): A8K5M2
    , D3DP53, Q96AN1, Q96KP2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: October 11, 2005
    Last modified: October 1, 2014
    This is version 175 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3