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Protein

Caspase-3

Gene

CASP3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei121By similarity1
Active sitei163By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

BioCyciZFISH:HS09058-MONOMER.
BRENDAi3.4.22.56. 2681.
ReactomeiR-HSA-111459. Activation of caspases through apoptosome-mediated cleavage.
R-HSA-111463. SMAC binds to IAPs.
R-HSA-111464. SMAC-mediated dissociation of IAP:caspase complexes.
R-HSA-111465. Apoptotic cleavage of cellular proteins.
R-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-2028269. Signaling by Hippo.
R-HSA-205025. NADE modulates death signalling.
R-HSA-211227. Activation of DNA fragmentation factor.
R-HSA-211736. Stimulation of the cell death response by PAK-2p34.
R-HSA-264870. Caspase-mediated cleavage of cytoskeletal proteins.
R-HSA-351906. Apoptotic cleavage of cell adhesion proteins.
R-HSA-418889. Ligand-independent caspase activation via DCC.
R-HSA-449147. Signaling by Interleukins.
SABIO-RKP42574.
SIGNORiP42574.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:1504. CASP3.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • death-inducing signaling complex Source: Ensembl
  • membrane raft Source: Ensembl
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi836.
OpenTargetsiENSG00000164305.
PharmGKBiPA26087.

Chemistry databases

ChEMBLiCHEMBL2334.
DrugBankiDB01017. Minocycline.
GuidetoPHARMACOLOGYi1619.

Polymorphism and mutation databases

BioMutaiCASP3.
DMDMi77416852.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000045691 – 99
PropeptideiPRO_000000457010 – 281 PublicationAdd BLAST19
ChainiPRO_000000457129 – 175Caspase-3 subunit p17Add BLAST147
ChainiPRO_0000004572176 – 277Caspase-3 subunit p12Add BLAST102

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei11N6-acetyllysineBy similarity1
Modified residuei26PhosphoserineCombined sources1
Modified residuei163S-nitrosocysteine; in inhibited form1 Publication1

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

EPDiP42574.
MaxQBiP42574.
PaxDbiP42574.
PeptideAtlasiP42574.
PRIDEiP42574.

2D gel databases

OGPiP42574.

PTM databases

iPTMnetiP42574.
PhosphoSitePlusiP42574.

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

BgeeiENSG00000164305.
CleanExiHS_CASP3.
ExpressionAtlasiP42574. baseline and differential.
GenevisibleiP42574. HS.

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
AKAP8O438235EBI-524064,EBI-1237481
AKT3Q9Y2432EBI-524064,EBI-296115
MDM2Q009872EBI-524064,EBI-389668
WNK3Q9BYP72EBI-524064,EBI-1182602
XIAPP981702EBI-524064,EBI-517127

Protein-protein interaction databases

BioGridi107286. 99 interactors.
DIPiDIP-268N.
IntActiP42574. 42 interactors.
MINTiMINT-147180.
STRINGi9606.ENSP00000311032.

Chemistry databases

BindingDBiP42574.

Structurei

Secondary structure

1277
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi41 – 51Combined sources11
Helixi57 – 59Combined sources3
Helixi67 – 80Combined sources14
Beta strandi84 – 90Combined sources7
Helixi93 – 105Combined sources13
Helixi108 – 110Combined sources3
Beta strandi111 – 120Combined sources10
Beta strandi126 – 129Combined sources4
Beta strandi132 – 135Combined sources4
Helixi136 – 141Combined sources6
Turni145 – 147Combined sources3
Helixi149 – 151Combined sources3
Beta strandi156 – 162Combined sources7
Beta strandi165 – 167Combined sources3
Beta strandi178 – 181Combined sources4
Turni183 – 185Combined sources3
Turni189 – 192Combined sources4
Beta strandi193 – 199Combined sources7
Beta strandi206 – 208Combined sources3
Turni209 – 211Combined sources3
Helixi214 – 226Combined sources13
Turni227 – 229Combined sources3
Helixi232 – 246Combined sources15
Helixi254 – 256Combined sources3
Beta strandi264 – 267Combined sources4
Beta strandi270 – 272Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4PRYX-ray1.70A1-277[»]
4PS0X-ray1.63A/B1-277[»]
4QTXX-ray1.97A1-277[»]
4QTYX-ray1.60A29-277[»]
4QU0X-ray1.95A1-277[»]
4QU5X-ray1.91A1-277[»]
4QU8X-ray1.72A1-277[»]
4QU9X-ray1.56A1-277[»]
4QUAX-ray1.89A1-277[»]
4QUBX-ray1.69A1-277[»]
4QUDX-ray2.00A/B1-277[»]
4QUEX-ray1.84A/C1-277[»]
4QUGX-ray1.92A/C1-277[»]
4QUHX-ray1.76A/C1-277[»]
4QUIX-ray1.76A/B1-277[»]
4QUJX-ray1.50A1-277[»]
4QULX-ray1.90A/C1-277[»]
5IC4X-ray2.65A/C/E/G1-175[»]
B/D/F/H176-276[»]
ProteinModelPortaliP42574.
SMRiP42574.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42574.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C14A family.Curated

Phylogenomic databases

eggNOGiKOG3573. Eukaryota.
ENOG410ZQIE. LUCA.
GeneTreeiENSGT00760000118912.
HOGENOMiHOG000231878.
HOVERGENiHBG050802.
InParanoidiP42574.
KOiK02187.
OMAiDDDMACH.
OrthoDBiEOG091G05YD.
PhylomeDBiP42574.
TreeFamiTF102023.

Family and domain databases

CDDicd00032. CASc. 1 hit.
Gene3Di3.40.50.1460. 1 hit.
InterProiIPR029030. Caspase-like_dom.
IPR015470. Caspase_3.
IPR033139. Caspase_cys_AS.
IPR016129. Caspase_his_AS.
IPR002138. Pept_C14_p10.
IPR001309. Pept_C14_p20.
IPR015917. Pept_C14A.
[Graphical view]
PANTHERiPTHR10454:SF30. PTHR10454:SF30. 1 hit.
PRINTSiPR00376. IL1BCENZYME.
SMARTiSM00115. CASc. 1 hit.
[Graphical view]
SUPFAMiSSF52129. SSF52129. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti31 – 36ISLDNS → MSWDTG in CAC88866 (PubMed:15003516).Curated6

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04861622H → R.Corresponds to variant rs35578277dbSNPEnsembl.1
Natural variantiVAR_001401190E → D.3 PublicationsCorresponds to variant rs1049210dbSNPEnsembl.1

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.
XP_011530603.1. XM_011532301.1.
UniGeneiHs.141125.

Genome annotation databases

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

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.
CCDSiCCDS3836.1.
PIRiA55315.
RefSeqiNP_004337.2. NM_004346.3.
NP_116786.1. NM_032991.2.
XP_011530603.1. XM_011532301.1.
UniGeneiHs.141125.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4PRYX-ray1.70A1-277[»]
4PS0X-ray1.63A/B1-277[»]
4QTXX-ray1.97A1-277[»]
4QTYX-ray1.60A29-277[»]
4QU0X-ray1.95A1-277[»]
4QU5X-ray1.91A1-277[»]
4QU8X-ray1.72A1-277[»]
4QU9X-ray1.56A1-277[»]
4QUAX-ray1.89A1-277[»]
4QUBX-ray1.69A1-277[»]
4QUDX-ray2.00A/B1-277[»]
4QUEX-ray1.84A/C1-277[»]
4QUGX-ray1.92A/C1-277[»]
4QUHX-ray1.76A/C1-277[»]
4QUIX-ray1.76A/B1-277[»]
4QUJX-ray1.50A1-277[»]
4QULX-ray1.90A/C1-277[»]
5IC4X-ray2.65A/C/E/G1-175[»]
B/D/F/H176-276[»]
ProteinModelPortaliP42574.
SMRiP42574.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107286. 99 interactors.
DIPiDIP-268N.
IntActiP42574. 42 interactors.
MINTiMINT-147180.
STRINGi9606.ENSP00000311032.

Chemistry databases

BindingDBiP42574.
ChEMBLiCHEMBL2334.
DrugBankiDB01017. Minocycline.
GuidetoPHARMACOLOGYi1619.

Protein family/group databases

MEROPSiC14.003.

PTM databases

iPTMnetiP42574.
PhosphoSitePlusiP42574.

Polymorphism and mutation databases

BioMutaiCASP3.
DMDMi77416852.

2D gel databases

OGPiP42574.

Proteomic databases

EPDiP42574.
MaxQBiP42574.
PaxDbiP42574.
PeptideAtlasiP42574.
PRIDEiP42574.

Protocols and materials databases

DNASUi836.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi836.
DisGeNETi836.
GeneCardsiCASP3.
HGNCiHGNC:1504. CASP3.
HPAiCAB000091.
CAB008381.
HPA002643.
MIMi600636. gene.
neXtProtiNX_P42574.
OpenTargetsiENSG00000164305.
PharmGKBiPA26087.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3573. Eukaryota.
ENOG410ZQIE. LUCA.
GeneTreeiENSGT00760000118912.
HOGENOMiHOG000231878.
HOVERGENiHBG050802.
InParanoidiP42574.
KOiK02187.
OMAiDDDMACH.
OrthoDBiEOG091G05YD.
PhylomeDBiP42574.
TreeFamiTF102023.

Enzyme and pathway databases

BioCyciZFISH:HS09058-MONOMER.
BRENDAi3.4.22.56. 2681.
ReactomeiR-HSA-111459. Activation of caspases through apoptosome-mediated cleavage.
R-HSA-111463. SMAC binds to IAPs.
R-HSA-111464. SMAC-mediated dissociation of IAP:caspase complexes.
R-HSA-111465. Apoptotic cleavage of cellular proteins.
R-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-2028269. Signaling by Hippo.
R-HSA-205025. NADE modulates death signalling.
R-HSA-211227. Activation of DNA fragmentation factor.
R-HSA-211736. Stimulation of the cell death response by PAK-2p34.
R-HSA-264870. Caspase-mediated cleavage of cytoskeletal proteins.
R-HSA-351906. Apoptotic cleavage of cell adhesion proteins.
R-HSA-418889. Ligand-independent caspase activation via DCC.
R-HSA-449147. Signaling by Interleukins.
SABIO-RKP42574.
SIGNORiP42574.

Miscellaneous databases

EvolutionaryTraceiP42574.
GeneWikiiCaspase_3.
GenomeRNAii836.
PMAP-CutDBP42574.
PROiP42574.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000164305.
CleanExiHS_CASP3.
ExpressionAtlasiP42574. baseline and differential.
GenevisibleiP42574. HS.

Family and domain databases

CDDicd00032. CASc. 1 hit.
Gene3Di3.40.50.1460. 1 hit.
InterProiIPR029030. Caspase-like_dom.
IPR015470. Caspase_3.
IPR033139. Caspase_cys_AS.
IPR016129. Caspase_his_AS.
IPR002138. Pept_C14_p10.
IPR001309. Pept_C14_p20.
IPR015917. Pept_C14A.
[Graphical view]
PANTHERiPTHR10454:SF30. PTHR10454:SF30. 1 hit.
PRINTSiPR00376. IL1BCENZYME.
SMARTiSM00115. CASc. 1 hit.
[Graphical view]
SUPFAMiSSF52129. SSF52129. 1 hit.
PROSITEiPS01122. CASPASE_CYS. 1 hit.
PS01121. CASPASE_HIS. 1 hit.
PS50207. CASPASE_P10. 1 hit.
PS50208. CASPASE_P20. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 30, 2016
This is version 199 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.