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Protein Page:
CASP9 (human)

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; cytosol; nucleus; apoptosome
Molecular Function: peptidase activity; protein binding; cysteine-type endopeptidase activity; enzyme activator activity; SH3 domain binding; protein kinase binding
Biological Process: epidermal growth factor receptor signaling pathway; phosphoinositide-mediated signaling; fibroblast growth factor receptor signaling pathway; nerve growth factor receptor signaling pathway; positive regulation of apoptosis; apoptosis; DNA damage response, signal transduction; response to lipopolysaccharide; proteolysis; response to estradiol stimulus; regulation of apoptosis; response to antibiotic; DNA damage response, signal transduction resulting in induction of apoptosis; positive regulation of neuron apoptosis; response to cobalt ion; innate immune response; caspase activation via cytochrome c; platelet formation; response to DNA damage stimulus; aging
Reference #:  P55211 (UniProtKB)
Alt. Names/Synonyms: APAF-3; APAF3; apoptotic protease activating factor 3; Apoptotic protease Mch-6; Apoptotic protease-activating factor 3; CASP-9; CASP9; caspase 9, apoptosis-related cysteine peptidase; caspase 9, apoptosis-related cysteine protease; Caspase-9; Caspase-9 subunit p10; Caspase-9 subunit p35; CASPASE-9c; ICE-LAP6; ICE-like apoptotic protease 6; MCH6
Gene Symbols: CASP9
Molecular weight: 46,281 Da
Basal Isoelectric point: 5.73  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: T125‑p, S144‑p
apoptosis, induced: T125‑p, Y153‑p, S196‑p
activity, induced: Y153‑p
activity, inhibited: T125‑p, S144‑p, S196‑p
enzymatic activity, inhibited: S183‑p
molecular association, regulation: Y153‑p, S183‑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.


       human

 
1 0 S99-p NRQAAKLsKPTLENL
6 5 T125-p PEVLRPEtPRPVDIG
0 1 S133-p PRPVDIGsGGFGDVG
1 0 S144-p GDVGALEsLRGNADL
1 0 Y153-p RGNADLAyILSMEPC
0 1 S175-p NVNFCREsGLRTRTG
1 0 S183-p GLRTRTGsNIDCEKL
1 1 S195-p EKLRRRFssLHFMVE
3 1 S196-p KLRRRFssLHFMVEV
0 1 T208-p VEVKGDLtAKKMVLA
0 1 T301-p HGFEVAStsPEDEsP
0 2 S302-p GFEVAStsPEDEsPG
0 4 S307-p StsPEDEsPGsNPEP
1 3 S310-p PEDEsPGsNPEPDAT
  mouse

 
S132 RVVKLEPSQPAVGNL
T163-p PEVLRPEtPRPVDIG
S171 PRPVDIGSGGAHDVC
K182 HDVCVPGKIRGHADM
Y191 RGHADMAYTLDSDPC
S213 NVNFCPSSGLGTRTG
S221 GLGTRTGSNLDRDKL
R233 DKLEHRFRWLRFMVE
W234 KLEHRFRWLRFMVEV
T246 VEVKNDLTAKKMVTA
T339 HGFEVACTSSQGRTL
S340 GFEVACTSSQGRTLD
T345 CTSSQGRTLDsDSEP
S348-p SQGRTLDsDSEPDAV
  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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