Detail Information for IndEnz0002008701
IED ID IndEnz0002008701
Enzyme Type ID protease008701
Protein Name Proteasome subunit beta type-10
EC 3.4.25.1
Proteasome subunit beta-2i
Gene Name PSMB10
Organism Bos taurus (Bovine)
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 Laurasiatheria Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine)
Enzyme Sequence MQKTVLEPQRGFSFENCERNAALQRALPGLRVPHARKTGTTIAGLVFQDGVILGADTRATNDSVVADKICEKIHFIAPKIYCCGAGVAADAEMTTRMAASNMELHALSTGRECRVATVTRMLRQTLFRYQGYVGASLIVGGVDFTGPQLYSVHPHGSYSRLPFTALGSGQDAAIAVLEDRFQPNMTLEAAQELLVEAITAGILGDLGSGGNVDACVITAAGAKMLRALSSPTKPIERSSQYRFAPGTTPVLSQTVVPLTLELVEETVQAMDVE
Enzyme Length 273
Uniprot Accession Number Q3T0T1
Absorption
Active Site ACT_SITE 40; /note=Nucleophile; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.; EC=3.4.25.1;
DNA Binding
EC Number 3.4.25.1
Enzyme Function FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Beta strand (11); Chain (1); Helix (4); Modified residue (2); Propeptide (1); Site (1); Turn (2)
Keywords 3D-structure;Acetylation;Cytoplasm;Hydrolase;Nucleus;Phosphoprotein;Protease;Proteasome;Reference proteome;Threonine protease;Zymogen
Interact With
Induction INDUCTION: Up-regulated by interferon gamma (at protein level).
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}.
Modified Residue MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0000250|UniProtKB:P40306; MOD_RES 230; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P40306
Post Translational Modification PTM: Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity. {ECO:0000250|UniProtKB:O35955}.
Signal Peptide
Structure 3D Electron microscopy (3)
Cross Reference PDB 7DR6; 7DR7; 7DRW;
Mapped Pubmed ID 23706739; 33531497;
Motif
Gene Encoded By
Mass 29,099
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda