Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
CASP3 (mouse)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

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; Motility/polarity/chemotaxis; Protease; EC 3.4.22.56
Cellular Component: cytoplasm; cytosol; nucleus; lipid raft
Molecular Function: cyclin-dependent protein kinase inhibitor activity; peptidase activity; phospholipase A2 activator activity; protein binding; protease binding; hydrolase activity; cysteine-type endopeptidase activity; death receptor binding; protein complex binding; 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; neuron differentiation; learning and/or memory; sensory perception of sound; B cell homeostasis; 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; response to DNA damage stimulus; induction of apoptosis by oxidative stress; 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.


STRING  |  Reactome  |  BioGPS  |  Scansite  |  Pfam  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  Source  |  UCSD-Nature  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


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 1 N4 ____MENNKTSVDSK
0 2 S7 _MENNKTSVDSKsIN
0 1 S10 NNKTSVDSKsINNFE
0 4 S12-p KTSVDSKsINNFEVk
0 1 K19-ub sINNFEVkTIHGSks
0 1 S24 EVkTIHGSksVDSGI
0 1 K25-ub VkTIHGSksVDSGIY
1 9 S26-p kTIHGSksVDSGIYL
0 1 Y41 DSSYKMDYPEMGICI
0 3 K57-ub INNKNFHkSTGMSSR
0 1 S65 STGMSSRSGTDVDAA
0 1 T67 GMSSRSGTDVDAANL
0 1 K82 RETFMGLKYQVRNKN
0 2 K82-ub RETFMGLkYQVRNKN
0 1 K88 LkYQVRNKNDLTRED
0 3 K105 ELMDSVSKEDHSKRS
1 0 S150 FRGDYCRSLTGKPKL
0 1 K229 MLKLYAHKLEFMHIL
  human

 
T4-p ____MENtENsVDsK
S7-p _MENtENsVDsKsIK
S10-p NtENsVDsKsIKNLE
S12-p ENsVDsKsIKNLEPK
K19 sIKNLEPKIIHGsEs
S24-p EPKIIHGsEsMDSGI
E25 PKIIHGsEsMDSGIS
S26-p KIIHGsEsMDSGISL
Y41-p DNSYKMDyPEMGLCI
K57-ub INNKNFHkSTGMTSR
S65-p STGMTSRsGtDVDAA
T67-p GMTSRsGtDVDAANL
K82-ac RETFRNLkYEVRNkN
K82-ub RETFRNLkYEVRNkN
K88-ub LkYEVRNkNDLTREE
K105-ub ELMRDVSkEDHSKRS
S150-p FRGDRCRsLTGKPKL
K229-ub MLKQYADkLEFMHIL
  rat

 
N4 ____MDNNETSVDSk
S7 _MDNNETSVDSkSIN
S10 NNETSVDSkSINNFE
S12 ETSVDSkSINNFETK
K19 SINNFETKTIHGSkS
S24 ETKTIHGSkSMDSGI
K25 TKTIHGSKSMDSGIY
S26 KTIHGSkSMDSGIYL
Y41 DSSYKMDYPEMGLCI
K57 INNKNFHKSTGMSAR
N65 STGMSARNGTDVDAA
T67 GMSARNGTDVDAANL
K82 RETFMALKYEVRNKN
K82 RETFMALKYEVRNKN
K88 LKYEVRNKNDLTREE
K105 ELMDSVSKEDHSKRS
S150 FRGDYCRSLTGKPKL
K229 MLKLYAHKLEFMHIL
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.