Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
logos LINCs Logo Mt Sinai Logo NIH Logo NCI Logo
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; Apoptosis; Protease
Cellular Component: apoptosome; cytoplasm; cytosol; mitochondrion; nucleus
Molecular Function: cysteine-type endopeptidase activity; cysteine-type peptidase activity; hydrolase activity; peptidase activity; protein binding; protein kinase binding; SH3 domain binding
Biological Process: 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; regulation of apoptosis; response to DNA damage stimulus; response to organic cyclic substance; response to UV
Reference #:  Q8C3Q9 (UniProtKB)
Alt. Names/Synonyms: AI115399; AW493809; Casp9; caspase 9; Caspase-9; Caspase9; ICE-LAP6; Mch6; OTTMUSP00000010525
Gene Symbols: Casp9
Molecular weight: 49,979 Da
Basal Isoelectric point: 6.39  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.
Download PyMol Script
Download ChimeraX Script


STRING  |  Reactome  |  BioGPS  |  Scansite  |  Pfam  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  Ensembl Protein


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


 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.


       mouse

 
1 0 S132 RVVKLDPSQPAVGNL
0 2 T140‑p QPAVGNLtPVVLGPE
6 6 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 6 S348‑p SQGRTLDsDSEPDAV
0 2 S350 GRTLDsDSEPDAVPY
  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
  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
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.