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Protein Page:
CASP9 (rat)

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; Apoptosis; Protease
Cellular Component: apoptosome; cytoplasm; cytosol; mitochondrion; nucleus
Molecular Function: cysteine-type endopeptidase activity; cysteine-type peptidase activity; peptidase activity; protein binding; protein kinase binding; SH3 domain binding
Biological Process: aging; apoptosis; caspase activation; DNA damage response, signal transduction; DNA damage response, signal transduction resulting in induction of apoptosis; positive regulation of apoptosis; positive regulation of neuron apoptosis; proteolysis; response to antibiotic; response to cobalt ion; response to DNA damage stimulus; response to estradiol stimulus; response to lipopolysaccharide; response to organic cyclic substance; response to UV
Reference #:  Q9JHK1 (UniProtKB)
Alt. Names/Synonyms: 25 kDa caspase-9 dominant negative protein; Apaf3; apoptotic protease activating factor 3; apoptotic protease Mch-6; Casp-9-CTD; Casp9; Casp9_v1; caspase 9, apoptosis-related cysteine peptidase; Caspase 9, isoform CRA_a; Caspase-9; caspase-9 dominant negative form; Caspase-9 long isoform; caspase-9-carboxyl-terminal divergent; Ice-Lap6; Ice-like apoptotic protease 6; Mch6; RNCASP9
Gene Symbols: Casp9
Molecular weight: 50,400 Da
Basal Isoelectric point: 6.04  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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Modification Sites and Domains  

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

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.


       rat

 
1 0 S132 KVVKLDPSQPALGNL
0 1 T140 QPALGNLTPVVLGPE
6 5 T163 PEVLTPETPRPVDIG
0 1 S171 PRPVDIGSGRAHDVC
1 0 K182 HDVCTPGKIERHADM
1 0 Y191 ERHADMAYTLDSDPC
0 1 S213 NVNFCPSSGLSTRIG
1 0 S221 GLSTRIGSHVDCEKL
1 1 C233 EKLQHRFCWLRFMVE
3 1 W234 KLQHRFCWLRFMVEV
0 1 T246 VEVKNDLTAKKMVTA
0 1 T339 HGFEVAFTSSQDKAF
0 2 S340 GFEVAFTSSQDKAFD
0 5 A345 FTSSQDKAFDsDsEP
1 6 S348‑p SQDKAFDsDsEPDAV
0 2 S350‑p DKAFDsDsEPDAVPY
  human

► Hide Isoforms
 
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
  CASP9 iso2  
S99 NRQAAKLSKPTLENL
T107 KPTLENLTPVVLRPE
T125 PEVLRPETPRPVDIG
S133 PRPVDIGSGGFGDVE
- gap
- gap
- gap
- gap
- gap
- gap
- gap
T151 HGFEVASTSPEDESP
S152 GFEVASTSPEDESPG
S157 STSPEDESPGSNPEP
S160 PEDESPGSNPEPDAT
P162 DESPGSNPEPDATPF
  CASP9 iso3  
S99 NRQAAKLSKPTLENL
T107 KPTLENLTPVVLRPE
T125 PEVLRPETPRPVDIG
S133 PRPVDIGSGGFGDVG
S144 GDVGALESLRGNADL
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
  CASP9 iso4  
S16 NRQAAKLSKPTLENL
T24 KPTLENLTPVVLRPE
T42 PEVLRPETPRPVDIG
S50 PRPVDIGSGGFGDVG
S61 GDVGALESLRGNADL
Y70 RGNADLAYILSMEPC
S92 NVNFCRESGLRTRTG
S100 GLRTRTGSNIDCEKL
S112 EKLRRRFSSLHFMVE
S113 KLRRRFSSLHFMVEV
T125 VEVKGDLTAKKMVLA
T218 HGFEVASTSPEDESP
S219 GFEVASTSPEDESPG
S224 STSPEDESPGSNPEP
S227 PEDESPGSNPEPDAT
P229 DESPGSNPEPDATPF
  mouse

 
S132 RVVKLDPSQPAVGNL
T140 QPAVGNLTPVVLGPE
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
S350 GRTLDsDSEPDAVPY
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