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Protein Page:
CASP3 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
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: EC 3.4.22.56; Motility/polarity/chemotaxis; Apoptosis; Protease
Chromosomal Location of Human Ortholog: 4q34
Cellular Component: cytosol; nucleoplasm; nucleus; plasma membrane
Molecular Function: aspartic-type endopeptidase activity; caspase activator activity; cysteine-type endopeptidase activity; peptidase activity; protein binding
Biological Process: apoptosis; caspase activation; caspase activation via cytochrome c; cell structure disassembly during apoptosis; DNA fragmentation during apoptosis; erythrocyte differentiation; keratinocyte differentiation; negative regulation of apoptosis; nerve growth factor receptor signaling pathway; neuron differentiation; platelet formation; proteolysis; regulation of macroautophagy
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
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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



 LTP 

LTP: 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.


 HTP 

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


       human

 
0 1 T4‑p ____MENtENsVDsk
0 2 S7‑p _MENtENsVDsksIK
0 1 S10‑p NtENsVDsksIKNLE
0 2 K11‑ac tENsVDsksIKNLEP
0 1 K11‑ub tENsVDsksIKNLEP
0 6 S12‑p ENsVDsksIKNLEPK
0 1 K19 sIKNLEPKIIHGsEs
1 0 I20 IKNLEPKIIHGsEsM
0 1 S24‑p EPKIIHGsEsMDSGI
0 1 E25 PKIIHGsEsMDSGIS
0 1 E25 PKIIHGsEsMDSGIS
1 12 S26‑p KIIHGsEsMDSGISL
0 1 Y41‑p DNSYKMDyPEMGLCI
0 4 K57‑ub INNKNFHkSTGMTSR
0 1 S65‑p STGMTSRsGtDVDAA
0 1 T67‑p GMTSRsGtDVDAANL
0 1 K82‑ac RETFRNLkYEVRNkN
0 3 K82‑ub RETFRNLkYEVRNkN
0 1 K88‑ub LkYEVRNkNDLTREE
0 3 K105‑ub ELMRDVSkEDHSKRS
0 1 K138‑ub NGPVDLKkITNFFRG
1 0 S150‑p FRGDRCRsLTGKPKL
0 1 K229 MLKQYADKLEFMHIL
0 1 K229‑ub MLKQYADkLEFMHIL
  mouse

 
N4 ____MENNKTSVDSK
S7 _MENNKTSVDSKsIN
S10 NNKTSVDSKsINNFE
K11 NKTSVDSKsINNFEV
K11 NKTSVDSKsINNFEV
S12‑p KTSVDSKsINNFEVk
K19‑ub sINNFEVktIHGSks
T20‑p INNFEVktIHGSksV
S24 EVktIHGSksVDSGI
K25 VktIHGSKsVDSGIY
K25‑ub VktIHGSksVDSGIY
S26‑p ktIHGSksVDSGIYL
Y41 DSSYKMDYPEMGICI
K57‑ub INNKNFHkSTGMSSR
S65 STGMSSRSGTDVDAA
T67 GMSSRSGTDVDAANL
K82 RETFMGLKYQVRNKN
K82‑ub RETFMGLkYQVRNKN
K88 LkYQVRNKNDLTRED
K105 ELMDSVSKEDHSKRS
K138 NGPVELKKLTSFFRG
S150 FRGDYCRSLTGKPKL
K229 MLKLYAHKLEFMHIL
K229 MLKLYAHKLEFMHIL
  rat

 
N4 ____MDNNETSVDSk
S7 _MDNNETSVDSkSIN
S10 NNETSVDSkSINNFE
K11‑ac NETSVDSkSINNFET
K11 NETSVDSKSINNFET
S12 ETSVDSkSINNFETK
K19 SINNFETKTIHGSkS
T20 INNFETKTIHGSkSM
S24 ETKTIHGSkSMDSGI
K25‑ac TKTIHGSkSMDSGIY
K25 TKTIHGSKSMDSGIY
S26 KTIHGSkSMDSGIYL
Y41 DSSYKMDYPEMGLCI
K57 INNKNFHKSTGMSAR
N65 STGMSARNGTDVDAA
T67 GMSARNGTDVDAANL
K82 RETFMALKYEVRNKN
K82 RETFMALKYEVRNKN
K88 LKYEVRNKNDLTREE
K105 ELMDSVSKEDHSKRS
K138 NGPVDLKKLTSFFRG
S150 FRGDYCRSLTGKPKL
K229‑ac MLKLYAHkLEFMHIL
K229 MLKLYAHKLEFMHIL
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