Detail Information for IndEnz0002018741
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