| IED ID | IndEnz0002011521 |
| Enzyme Type ID | protease011521 |
| Protein Name |
26S proteasome regulatory subunit 7 26S proteasome AAA-ATPase subunit RPT1 Proteasome 26S subunit ATPase 2 |
| Gene Name | Psmc2 Mss1 |
| 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 | MPDYLGADQRKTKEEEKDDKPIRALDEGDIALLKTYGQSTYSRQIKQVEDDIQQLLKKINELTGIKESDTGLAPPALWDLAADKQTLQSEQPLQVARCTKIINADSEDPKYIINVKQFAKFVVDLSDQVAPTDIEEGMRVGVDRNKYQIHIPLPPKIDPTVTMMQVEEKPDVTYSDVGGCKEQIEKLREVVETPLLHPERFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMARTKKACLIFFDEIDAIGGARFDDGAGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPGRLDRKIEFSLPDLEGRTHIFKIHARSMSVERDIRFELLARLCPNSTGAEIRSVCTEAGMFAIRARRKIATEKDFLEAVNKVIKSYAKFSATPRYMTYN |
| Enzyme Length | 433 |
| Uniprot Accession Number | P46471 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC2 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides. {ECO:0000250|UniProtKB:P35998}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 216..223; /note=ATP; /evidence=ECO:0000255 |
| Features | Chain (1); Modified residue (2); Nucleotide binding (1); Region (1); Sequence conflict (13) |
| Keywords | ATP-binding;Acetylation;Cytoplasm;Direct protein sequencing;Nucleotide-binding;Proteasome;Reference proteome;Ubl conjugation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P35998}. Note=Colocalizes with TRIM5 in cytoplasmic bodies. {ECO:0000250|UniProtKB:P35998}. |
| Modified Residue | MOD_RES 116; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P35998; MOD_RES 422; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P35998 |
| Post Translational Modification | PTM: Monoubiquitinated by RNF181. {ECO:0000250|UniProtKB:P35998}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10614646; 11217851; 11597142; 11741941; 12466851; 12904583; 14595844; 14610273; 17500595; 18799693; 19334288; 20498273; 21565611; 21743439; 23032291; 33625534; 9107682; |
| Motif | |
| Gene Encoded By | |
| Mass | 48,648 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |