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Protein Page:
Casp3 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
Casp3 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. 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. 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. Inhibited by isatin sulfonamides. Belongs to the peptidase C14A family. Note: This description may include information from UniProtKB.
Protein type: EC 3.4.22.56; Apoptosis; Protease; EC 3.4.22.-; Motility/polarity/chemotaxis
Cellular Component: nucleoplasm; plasma membrane; nucleus; cytosol
Molecular Function: cyclin-dependent protein kinase inhibitor activity; peptidase activity; protein binding; cysteine-type endopeptidase activity; aspartic-type endopeptidase activity
Biological Process: extracellular matrix organization and biogenesis; nerve growth factor receptor signaling pathway; positive regulation of apoptosis; apoptosis; negative regulation of activated T cell proliferation; heart development; negative regulation of B cell proliferation; regulation of caspase activity; proteolysis; neuron differentiation; regulation of apoptosis; extracellular matrix disassembly; sensory perception of sound; B cell homeostasis; positive regulation of neuron apoptosis; response to wounding; erythrocyte differentiation; T cell homeostasis; DNA fragmentation during apoptosis; response to UV; cell structure disassembly during apoptosis; release of cytochrome c from mitochondria; cell fate commitment; negative regulation of cyclin-dependent protein kinase activity; keratinocyte differentiation; neuron apoptosis; induction of apoptosis via death domain receptors; caspase activation via cytochrome c; platelet formation; response to DNA damage stimulus; induction of apoptosis by oxidative stress; negative regulation of apoptosis
Reference #:  P42574 (UniProtKB)
Alt. Names/Synonyms: Apopain; CASP-3; CASP3; caspase 3, apoptosis-related cysteine peptidase; caspase 3, apoptosis-related cysteine protease; Caspase-3; Caspase-3 subunit p12; Caspase-3 subunit p17; CPP-32; CPP32; CPP32B; Cysteine protease CPP32; PARP cleavage protease; procaspase3; Protein Yama; SCA-1; SREBP cleavage activity 1; Yama
Gene Symbols: CASP3
Molecular weight: 31,608 Da
Basal Isoelectric point: 6.09  Predict pI for various phosphorylation states
CST Pathways:  Alzheimer's Disease  |  Apoptosis Regulation  |  Death Receptor Signaling  |  ErbB/HER Signaling  |  Inhibition of Apoptosis  |  Mitochondrial Control of Apoptosis
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Casp3

Protein Structure Not Found.


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Sites Implicated In
apoptosis, inhibited: S150‑p
activity, inhibited: S150‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 S7-p _MENTENsVDSKsIK
0 4 S12-p ENsVDSKsIKNLEPK
0 1 K19 sIKNLEPKIIHGSEs
0 1 E25 PKIIHGSEsMDSGIS
0 8 S26-p KIIHGSEsMDSGISL
0 3 K57-u INNKNFHkSTGMTSR
0 1 K82-a RETFRNLkYEVRNKN
0 2 K82-u RETFRNLkYEVRNKN
0 3 K105-u ELMRDVSkEDHSKRS
1 0 S150-p FRGDRCRsLTGKPKL
0 1 K229-u MLKQYADkLEFMHIL
  mouse

 
S7 _MENNKTSVDSKsIN
S12-p KTSVDSKsINNFEVk
K19-u sINNFEVkTIHGSks
K25-u VkTIHGSksVDSGIY
S26-p kTIHGSksVDSGIYL
K57-u INNKNFHkSTGMSSR
K82 RETFMGLKYQVRNKN
K82-u RETFMGLkYQVRNKN
K105 ELMDSVSKEDHSKRS
S150 FRGDYCRSLTGKPKL
K229 MLKLYAHKLEFMHIL
  rat

 
S7 _MDNNETSVDSKSIN
S12 ETSVDSKSINNFETK
K19 SINNFETKTIHGSKS
K25 TKTIHGSKSMDSGIY
S26 KTIHGSKSMDSGIYL
K57 INNKNFHKSTGMSAR
K82 RETFMALKYEVRNKN
K82 RETFMALKYEVRNKN
K105 ELMDSVSKEDHSKRS
S150 FRGDYCRSLTGKPKL
K229 MLKLYAHKLEFMHIL
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