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Protein Page:
CASP9 (mouse)

Overview
CASP9 a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce 2 subunits, large and small, that dimerize to form the active enzyme. This protein is processed by caspase APAF1; this step is thought to be one of the earliest in the caspase activation cascade. Alternative splicing results in two isoforms. Note: This description may include information from UniProtKB.
Protein type: EC 3.4.22.62; Protease; Apoptosis
Cellular Component: mitochondrion; cytoplasm; intracellular; nucleus; cytosol; apoptosome
Molecular Function: peptidase activity; protein binding; hydrolase activity; cysteine-type endopeptidase activity; SH3 domain binding; protein kinase binding; cysteine-type peptidase activity
Biological Process: caspase activation; regulation of apoptosis; DNA damage response, signal transduction resulting in induction of apoptosis; positive regulation of apoptosis; apoptosis; positive regulation of neuron apoptosis; DNA damage response, signal transduction; proteolysis; response to organic cyclic substance; response to DNA damage stimulus; response to UV
Reference #:  Q8C3Q9 (UniProtKB)
Alt. Names/Synonyms: AI115399; APAF-3; Apoptotic protease Mch-6; Apoptotic protease-activating factor 3; AW493809; Casp9; caspase 9; Caspase-9; Caspase9; ICE-LAP6; ICE-like apoptotic protease 6; Mch6; OTTMUSP00000010525
Gene Symbols: Casp9
Molecular weight: 50,051 Da
Basal Isoelectric point: 6.24  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

CASP9

Protein Structure Not Found.


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Sites Implicated In
apoptosis, altered: T163‑p
apoptosis, inhibited: S348‑p
enzymatic activity, inhibited: T163‑p
protein processing: S348‑p

Modification Sites and Domains  

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

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

 
1 0 S132 RVVKLEPSQPAVGNL
6 5 T163-p PEVLRPEtPRPVDIG
0 1 S171 PRPVDIGSGGAHDVC
1 0 K182 HDVCVPGKIRGHADM
1 0 Y191 RGHADMAYTLDSDPC
0 1 S213 NVNFCPSSGLGTRTG
1 0 S221 GLGTRTGSNLDRDKL
1 1 R233 DKLEHRFRWLRFMVE
3 1 W234 KLEHRFRWLRFMVEV
0 1 T246 VEVKNDLTAKKMVTA
0 1 T339 HGFEVACTSSQGRTL
0 2 S340 GFEVACTSSQGRTLD
0 4 T345 CTSSQGRTLDsDSEP
1 3 S348-p SQGRTLDsDSEPDAV
  human

 
S99-p NRQAAKLsKPTLENL
T125-p PEVLRPEtPRPVDIG
S133-p PRPVDIGsGGFGDVG
S144-p GDVGALEsLRGNADL
Y153-p RGNADLAyILSMEPC
S175-p NVNFCREsGLRTRTG
S183-p GLRTRTGsNIDCEKL
S195-p EKLRRRFssLHFMVE
S196-p KLRRRFssLHFMVEV
T208-p VEVKGDLtAKKMVLA
T301-p HGFEVAStsPEDEsP
S302-p GFEVAStsPEDEsPG
S307-p StsPEDEsPGsNPEP
S310-p PEDEsPGsNPEPDAT
  rat

 
S132 KVVKLDPSQPALGNL
T163 PEVLTPETPRPVDIG
S171 PRPVDIGSGRAHDVC
K182 HDVCTPGKIERHADM
Y191 ERHADMAYTLDSDPC
S213 NVNFCPSSGLSTRIG
S221 GLSTRIGSHVDCEKL
C233 EKLQHRFCWLRFMVE
W234 KLQHRFCWLRFMVEV
T246 VEVKNDLTAKKMVTA
T339 HGFEVAFTSSQDKAF
S340 GFEVAFTSSQDKAFD
A345 FTSSQDKAFDsDSEP
S348-p SQDKAFDsDSEPDAV
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