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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: Protease; EC 3.4.22.62; Apoptosis
Cellular Component: mitochondrion; cytoplasm; intracellular; nucleus; cytosol; apoptosome
Molecular Function: peptidase activity; protein binding; hydrolase activity; cysteine-type endopeptidase activity; protein kinase binding; SH3 domain 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
0 1 T140 QPAVGNLTPVVLGPE
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 5 T345 CTSSQGRTLDsDSEP
1 5 S348-p SQGRTLDsDSEPDAV
0 2 S350 GRTLDsDSEPDAVPY
  human

 
S99-p NRQAAKLsKPTLENL
T107-p KPTLENLtPVVLRPE
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
P312 DEsPGsNPEPDATPF
  rat

 
S132 KVVKLDPSQPALGNL
T140 QPALGNLTPVVLGPE
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
S350-p DKAFDsDsEPDAVPY
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