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P42574

- CASP3_HUMAN

UniProt

P42574 - CASP3_HUMAN

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Protein

Caspase-3

Gene

CASP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

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 DNA fragmentation Source: Ensembl
  33. regulation of apoptotic process Source: Reactome
  34. regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Reactome
  35. release of cytochrome c from mitochondria Source: Ensembl
  36. response to tumor necrosis factor Source: BHF-UCL
  37. response to UV Source: Ensembl
  38. response to wounding Source: Ensembl
  39. sensory perception of sound Source: Ensembl
  40. T cell homeostasis Source: Ensembl
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP42574.
CleanExiHS_CASP3.
ExpressionAtlasiP42574. baseline and differential.
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 – 5111Combined sources
Helixi57 – 593Combined sources
Helixi67 – 8014Combined sources
Beta strandi84 – 907Combined sources
Helixi93 – 10513Combined sources
Helixi108 – 1103Combined sources
Beta strandi111 – 12010Combined sources
Beta strandi126 – 1294Combined sources
Beta strandi132 – 1354Combined sources
Helixi136 – 1416Combined sources
Turni145 – 1473Combined sources
Helixi149 – 1513Combined sources
Beta strandi156 – 1627Combined sources
Beta strandi165 – 1673Combined sources
Beta strandi178 – 1814Combined sources
Turni183 – 1853Combined sources
Turni189 – 1924Combined sources
Beta strandi193 – 1997Combined sources
Beta strandi206 – 2083Combined sources
Turni209 – 2113Combined sources
Helixi214 – 22613Combined sources
Turni227 – 2293Combined sources
Helixi232 – 24615Combined sources
Helixi254 – 2563Combined sources
Beta strandi264 – 2674Combined sources
Beta strandi270 – 2723Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118912.
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

        10         20         30         40         50
MENTENSVDS KSIKNLEPKI IHGSESMDSG ISLDNSYKMD YPEMGLCIII
60 70 80 90 100
NNKNFHKSTG MTSRSGTDVD AANLRETFRN LKYEVRNKND LTREEIVELM
110 120 130 140 150
RDVSKEDHSK RSSFVCVLLS HGEEGIIFGT NGPVDLKKIT NFFRGDRCRS
160 170 180 190 200
LTGKPKLFII QACRGTELDC GIETDSGVDD DMACHKIPVE ADFLYAYSTA
210 220 230 240 250
PGYYSWRNSK DGSWFIQSLC AMLKQYADKL EFMHILTRVN RKVATEFESF
260 270
SFDATFHAKK QIPCIVSMLT KELYFYH
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 DB01017. Minocycline.
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.
GeneTreei ENSGT00760000118912.
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

Bgeei P42574.
CleanExi HS_CASP3.
ExpressionAtlasi P42574. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 177 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