| IED ID | IndEnz0002016568 |
| Enzyme Type ID | protease016568 |
| Protein Name |
Caspase-2 CASP-2 EC 3.4.22.55 Neural precursor cell expressed developmentally down-regulated protein 2 NEDD-2 Protease ICH-1 Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12 |
| Gene Name | CASP2 ICH1 NEDD2 |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MAAPSAGSWSTFQHKELMAADRGRRILGVCGMHPHHQETLKKNRVVLAKQLLLSELLEHLLEKDIITLEMRELIQAKVGSFSQNVELLNLLPKRGPQAFDAFCEALRETKQGHLEDMLLTTLSGLQHVLPPLSCDYDLSLPFPVCESCPLYKKLRLSTDTVEHSLDNKDGPVCLQVKPCTPEFYQTHFQLAYRLQSRPRGLALVLSNVHFTGEKELEFRSGGDVDHSTLVTLFKLLGYDVHVLCDQTAQEMQEKLQNFAQLPAHRVTDSCIVALLSHGVEGAIYGVDGKLLQLQEVFQLFDNANCPSLQNKPKMFFIQACRGDETDRGVDQQDGKNHAGSPGCEESDAGKEKLPKMRLPTRSDMICGYACLKGTAAMRNTKRGSWYIEALAQVFSERACDMHVADMLVKVNALIKDREGYAPGTEFHRCKEMSEYCSTLCRHLYLFPGHPPT |
| Enzyme Length | 452 |
| Uniprot Accession Number | P42575 |
| Absorption | |
| Active Site | ACT_SITE 277; /evidence=ECO:0000250; ACT_SITE 320; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Strict requirement for an Asp residue at P1, with 316-asp being essential for proteolytic activity and has a preferred cleavage sequence of Val-Asp-Val-Ala-Asp-|-.; EC=3.4.22.55; |
| DNA Binding | |
| EC Number | 3.4.22.55 |
| Enzyme Function | FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. Might function by either activating some proteins required for cell death or inactivating proteins necessary for cell survival (PubMed:15073321). Associates with PIDD1 and CRADD to form the PIDDosome, a complex that activates CASP2 and triggers apoptosis in response to genotoxic stress (PubMed:15073321). {ECO:0000269|PubMed:15073321}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Alternative sequence (5); Beta strand (12); Chain (3); Domain (1); Erroneous initiation (5); Helix (9); Initiator methionine (1); Modified residue (3); Mutagenesis (9); Natural variant (4); Propeptide (2); Region (1); Sequence conflict (1); Turn (4) |
| Keywords | 3D-structure;Acetylation;Alternative splicing;Apoptosis;Hydrolase;Phosphoprotein;Protease;Reference proteome;Thiol protease;Zymogen |
| Interact With | O95429; Itself; P42575-1; P78560; O43741 |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0007744|PubMed:19413330; MOD_RES 157; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:23186163; MOD_RES 340; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21406692 |
| Post Translational Modification | PTM: The mature protease can process its own propeptide, but not that of other caspases. {ECO:0000269|PubMed:8654923}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (15) |
| Cross Reference PDB | 1PYO; 2P2C; 3R5J; 3R6G; 3R6L; 3R7B; 3R7N; 3R7S; 3RJM; 6GKF; 6GKG; 6S9K; 6SAD; 6Y8B; 6Y8D; |
| Mapped Pubmed ID | 10329646; 11830582; 16183742; 16193064; 17502107; 19203584; 19730412; 19773279; 21726810; 21828056; 21900206; 21903398; 21988832; 22531785; 22854598; 25416956; 30281929; 31961068; 32811973; 33006579; 33011746; 9261102; |
| Motif | |
| Gene Encoded By | |
| Mass | 50,685 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.55; |