Detail Information for IndEnz0002009065
IED ID IndEnz0002009065
Enzyme Type ID protease009065
Protein Name Proteasome subunit beta type-5
EC 3.4.25.1
Macropain epsilon chain
Multicatalytic endopeptidase complex epsilon chain
Proteasome chain 6
Proteasome epsilon chain
Proteasome subunit MB1
Proteasome subunit X
Gene Name PSMB5 LMPX MB1 X
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 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP
Enzyme Length 263
Uniprot Accession Number P28074
Absorption
Active Site ACT_SITE 60; /note="Nucleophile"; /evidence="ECO:0000269|PubMed:25599644, ECO:0000269|PubMed:27493187"
Activity Regulation
Binding Site BINDING 108; /note=Bortezomib; via amide nitrogen; /evidence=ECO:0000250
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.; EC=3.4.25.1; Evidence={ECO:0000269|PubMed:27176742};
DNA Binding
EC Number 3.4.25.1
Enzyme Function FUNCTION: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Within the 20S core complex, PSMB5 displays a chymotrypsin-like activity. {ECO:0000269|PubMed:15244466, ECO:0000269|PubMed:18502982, ECO:0000269|PubMed:18565852, ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Alternative sequence (2); Beta strand (13); Binding site (1); Chain (1); Erroneous initiation (3); Helix (5); Mutagenesis (3); Natural variant (1); Propeptide (1); Sequence conflict (5); Turn (1)
Keywords 3D-structure;Alternative splicing;Cytoplasm;Direct protein sequencing;Host-virus interaction;Hydrolase;Nucleus;Protease;Proteasome;Reference proteome;Threonine protease;Zymogen
Interact With O95429; Q8NCX0-3; Q92989; Q68J44; Q9Y6K9; O15116; Q96HA8; Q9Y244; P20618; P49720; Q99436; Q9BT92
Induction INDUCTION: Down-regulated by IFNG/IFN-gamma (at protein level). Induced in breast cancer tissue. Up-regulated by sulforaphane in breast cancer cells. {ECO:0000269|PubMed:17004105, ECO:0000269|PubMed:18602823, ECO:0000269|PubMed:8066462, ECO:0000269|PubMed:8663318}.
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12181345}. Nucleus {ECO:0000269|PubMed:12181345}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D Electron microscopy (37); X-ray crystallography (21)
Cross Reference PDB 4R3O; 4R67; 5A0Q; 5GJQ; 5GJR; 5L4G; 5L5W; 5L5X; 5L5Y; 5L5Z; 5L60; 5L61; 5L62; 5L63; 5L64; 5LE5; 5LEX; 5LEY; 5LEZ; 5LF0; 5LF1; 5LF3; 5LF4; 5LF6; 5LF7; 5LN3; 5M32; 5T0C; 5T0G; 5T0H; 5T0I; 5T0J; 5VFO; 5VFP; 5VFQ; 5VFR; 5VFS; 5VFT; 5VFU; 6KWY; 6MSB; 6MSD; 6MSE; 6MSG; 6MSH; 6MSJ; 6MSK; 6R70; 6REY; 6RGQ; 6WJD; 6WJN; 6XMJ; 7LXV; 7NHT; 7PG9; 7V5G; 7V5M;
Mapped Pubmed ID 10075690; 10205060; 10375532; 10514433; 10559916; 10693759; 10797013; 10828887; 10918611; 11046155; 11259415; 11285280; 11292861; 11292862; 11350924; 11454738; 11566882; 11585840; 11585921; 11739726; 11842200; 11931757; 12070128; 12101228; 12136087; 12376572; 12600938; 12660156; 12682069; 12738770; 12750368; 12808096; 12816948; 12853446; 14508489; 14508490; 14528300; 14561893; 14564014; 14676825; 14684739; 14707141; 14733938; 14734113; 14743216; 14757770; 15014503; 15029244; 15084608; 15224091; 15224092; 15226418; 15231747; 15257295; 15282312; 15469984; 15571818; 15678106; 15678131; 15735756; 15781449; 15887188; 16171779; 16263121; 16371461; 16413484; 16421275; 16547521; 16611981; 16705181; 16707496; 16728642; 16818754; 16931761; 17115028; 17139257; 17183061; 17187060; 17218260; 17234884; 17262013; 17283082; 17314511; 17353931; 17948026; 18497827; 18519783; 18541707; 18562081; 18922472; 18997794; 19243813; 19379695; 19473982; 19573811; 19596235; 19615732; 19684112; 19738201; 19759537; 19808967; 19955409; 20028659; 20154143; 20360384; 20555361; 20562859; 20723761; 20818436; 20858899; 20956384; 21289309; 21357747; 21478859; 21532586; 21565611; 21799911; 21920470; 21921029; 21978467; 22028648; 22306028; 22306998; 22427670; 22523338; 22781773; 22901813; 23018640; 23333871; 23602568; 23661552; 23867461; 24012004; 24019521; 24393841; 24627483; 25260729; 25547115; 25609649; 25654763; 25852190; 26091038; 26183061; 26496610; 26542806; 26778333; 27789522; 27791164; 28143565; 28292943; 28453575; 28541292; 28623645; 29365400; 29636472; 30026573; 30479383; 31292253; 31473102; 31562641; 32134919; 32783951; 34702852; 34711951; 7479848; 7479976; 7575604; 7628694; 7809113; 7831327; 7862124; 7957109; 9362451; 9380723; 9635433; 9660940; 9859996; 9990853;
Motif
Gene Encoded By
Mass 28,480
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda