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Protein Page:
Casp3 (mouse)
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: Apoptosis; Protease; Motility/polarity/chemotaxis; EC 3.4.22.-; EC 3.4.22.56
Cellular Component: mitochondrion; cytoplasm; nucleus; cytosol
Molecular Function: cyclin-dependent protein kinase inhibitor activity; peptidase activity; protein binding; phospholipase A2 activator activity; hydrolase activity; cysteine-type endopeptidase activity; aspartic-type endopeptidase activity; cysteine-type peptidase activity
Biological Process: positive regulation of catalytic activity; positive regulation of apoptosis; apoptosis; negative regulation of activated T cell proliferation; heart development; negative regulation of B cell proliferation; proteolysis; negative regulation of cell cycle; sensory perception of sound; learning and/or memory; B cell homeostasis; regulation of catalytic activity; positive regulation of neuron apoptosis; response to wounding; response to glucose stimulus; erythrocyte differentiation; T cell homeostasis; response to UV; 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; response to hydrogen peroxide; protein processing; induction of apoptosis by oxidative stress; response to DNA damage stimulus; negative regulation of apoptosis
Reference #:  P70677 (UniProtKB)
Alt. Names/Synonyms: A830040C14Rik; Apopain; CASP-3; Casp3; caspase 3; caspase 3, apoptosis related cysteine protease; Caspase-3; Caspase-3 subunit p12; Caspase-3 subunit p17; CC3; CPP-32; Cpp32; Cysteine protease CPP32; LICE; mldy; Protein Yama; SCA-1; SREBP cleavage activity 1; Yama
Gene Symbols: Casp3
Molecular weight: 31,475 Da
Basal Isoelectric point: 6.46  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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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.


       mouse

 
0 2 S7 _MENNKTSVDSKsIN
0 4 S12-p KTSVDSKsINNFEVk
0 1 K19-u sINNFEVkTIHGSks
0 1 K25-u VkTIHGSksVDSGIY
0 8 S26-p kTIHGSksVDSGIYL
0 3 K57-u INNKNFHkSTGMSSR
0 1 K82 RETFMGLKYQVRNKN
0 2 K82-u RETFMGLkYQVRNKN
0 3 K105 ELMDSVSKEDHSKRS
1 0 S150 FRGDYCRSLTGKPKL
0 1 K229 MLKLYAHKLEFMHIL
  human

 
S7-p _MENTENsVDSKsIK
S12-p ENsVDSKsIKNLEPK
K19 sIKNLEPKIIHGSEs
E25 PKIIHGSEsMDSGIS
S26-p KIIHGSEsMDSGISL
K57-u INNKNFHkSTGMTSR
K82-a RETFRNLkYEVRNKN
K82-u RETFRNLkYEVRNKN
K105-u ELMRDVSkEDHSKRS
S150-p FRGDRCRsLTGKPKL
K229-u MLKQYADkLEFMHIL
  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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