| IED ID | IndEnz0002018741 |
| Enzyme Type ID | protease018741 |
| Protein Name |
Caspase-9 CASP-9 EC 3.4.22.62 Apoptotic protease Mch-6 Apoptotic protease-activating factor 3 APAF-3 ICE-like apoptotic protease 6 ICE-LAP6 Cleaved into: Caspase-9 subunit p35; Caspase-9 subunit p10 |
| Gene Name | Casp9 Mch6 |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MDEADRQLLRRCRVRLVSELQVAELWDALLSRELFTRDMIEDIQQAGSGSRRDQARQLVTDLETRGRQALPLFISCLEDTGQGTLASLLQSGRQAAKQDPEAVKPLDHLVPVVLGPMGLTAKEQRVVKLDPSQPAVGNLTPVVLGPEELWPARLKPEVLRPETPRPVDIGSGGAHDVCVPGKIRGHADMAYTLDSDPCGHCLIINNVNFCPSSGLGTRTGSNLDRDKLEHRFRWLRFMVEVKNDLTAKKMVTALMEMAHRNHRALDCFVVVILSHGCQASHLQFPGAVYGTDGCSVSIEKIVNIFNGSGCPSLGGKPKLFFIQACGGEQKDHGFEVACTSSQGRTLDSDSEPDAVPYQEGPRPLDQLDAVSSLPTPSDILVSYSTFPGFVSWRDKKSGSWYIETLDGILEQWARSEDLQSLLLRVANAVSAKGTYKQIPGCFNFLRKKLFFKTS |
| Enzyme Length | 454 |
| Uniprot Accession Number | Q8C3Q9 |
| Absorption | |
| Active Site | ACT_SITE 275; /evidence=ECO:0000250; ACT_SITE 325; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Strict requirement for an Asp residue at position P1 and with a marked preference for His at position P2. It has a preferred cleavage sequence of Leu-Gly-His-Asp-|-Xaa.; EC=3.4.22.62; |
| DNA Binding | |
| EC Number | 3.4.22.62 |
| Enzyme Function | FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. Binding of caspase-9 to Apaf-1 leads to activation of the protease which then cleaves and activates caspase-3. Promotes DNA damage-induced apoptosis in a ABL1/c-Abl-dependent manner. Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (2); Domain (1); Modified residue (4); Propeptide (2) |
| Keywords | Apoptosis;Hydrolase;Phosphoprotein;Protease;Reference proteome;Thiol protease;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 163; /note=Phosphothreonine; by MAPK1; /evidence=ECO:0000250|UniProtKB:P55211; MOD_RES 191; /note=Phosphotyrosine; by ABL1; /evidence=ECO:0000269|PubMed:15657060; MOD_RES 340; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P55211; MOD_RES 348; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P55211 |
| Post Translational Modification | PTM: Cleavages at Asp-353 by granzyme B and at Asp-368 by caspase-3 generate the two active subunits. Caspase-8 and -10 can also be involved in these processing events (By similarity). {ECO:0000250}.; PTM: Phosphorylated at Thr-163 by MAPK1/ERK2. Phosphorylation at Thr-163 is sufficient to block caspase-9 processing and subsequent caspase-3 activation (By similarity). Phosphorylation on Tyr-191 by ABL1/c-Abl; occurs in the response of cells to DNA damage. {ECO:0000250, ECO:0000269|PubMed:15657060}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10087912; 10403638; 10452843; 10498280; 10529400; 10578172; 10671365; 10687948; 10739648; 10739653; 10960682; 11062535; 11092819; 11150333; 11279485; 11425902; 11514563; 11526440; 11549720; 11550085; 11739563; 11937545; 12097332; 12107826; 12142566; 12218135; 12374983; 12466851; 12581736; 12616497; 12646305; 12660414; 12667446; 12717433; 12801416; 12819136; 12847083; 12851714; 12904583; 14534531; 14561754; 14604764; 14657037; 14681479; 14709542; 14713951; 14747474; 14993216; 15105372; 15118096; 15156583; 15210718; 15210727; 15210730; 15214581; 15271982; 15531372; 15776018; 15861188; 15944155; 16007191; 16094404; 16183742; 16260615; 16291596; 16362053; 16397188; 16469926; 16514420; 16602821; 16764683; 16777102; 16857965; 16932756; 16966373; 17189626; 17265069; 17297564; 17371867; 17403866; 17417788; 17488888; 17562856; 17565040; 17652622; 17699753; 17823781; 17901126; 18037375; 18053235; 18467326; 18617322; 18636075; 18802096; 18802959; 18957517; 18979186; 19015276; 19029301; 19035350; 19074731; 19081073; 19194987; 19291307; 19325570; 19586613; 19621384; 19671668; 19682497; 19741144; 19801895; 19911005; 20372860; 20471954; 20624980; 20662604; 20972334; 21221781; 21267068; 21352494; 21731673; 21791606; 22294729; 22613767; 22679284; 23152605; 23159925; 23197294; 23223278; 23384561; 23834359; 23842495; 23922164; 23943790; 24362031; 24369835; 24752940; 25100655; 25285627; 25292199; 25349173; 25356864; 25516968; 25525875; 25583186; 25763592; 26290316; 26657770; 26938720; 27121492; 27480124; 27580936; 27709293; 27811852; 27848932; 28073913; 28187946; 29563882; 29600001; 29775594; 30381458; 30449657; 30911956; 31624230; 32321712; 32471877; 32576823; 34197726; 34672258; 9654089; 9708735; 9708736; |
| Motif | |
| Gene Encoded By | |
| Mass | 49,979 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |