IED ID | IndEnz0002001857 |
Enzyme Type ID | protease001857 |
Protein Name |
Proteasome subunit beta type-6 EC 3.4.25.1 Macropain delta chain Multicatalytic endopeptidase complex delta chain Proteasome delta chain Proteasome subunit Y |
Gene Name | PSMB6 LMPY Y |
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 | MAATLLAARGAGPAPAWGPEAFTPDWESREVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDRIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANALALAMERDGSSGGVIRLAAIAESGVERQVLLGDQIPKFAVATLPPA |
Enzyme Length | 239 |
Uniprot Accession Number | P28072 |
Absorption | |
Active Site | ACT_SITE 35; /note="Nucleophile"; /evidence="ECO:0000269|PubMed:25599644, ECO:0000269|PubMed:27493187" |
Activity Regulation | |
Binding Site | |
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, PSMB6 displays a peptidylglutamyl-hydrolizing activity also termed postacidic or caspase-like activity, meaning that the peptides bond hydrolysis occurs directly after acidic residues. {ECO:0000269|PubMed:15244466, ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Beta strand (12); Chain (1); Helix (7); Initiator methionine (1); Modified residue (2); Natural variant (1); Propeptide (1); Sequence conflict (1); Turn (1) |
Keywords | 3D-structure;Acetylation;Cytoplasm;Direct protein sequencing;Host-virus interaction;Hydrolase;Nucleus;Phosphoprotein;Protease;Proteasome;Reference proteome;Threonine protease;Zymogen |
Interact With | P42858; Q9UHB4; Q99436 |
Induction | INDUCTION: Down-regulated by IFNG/IFN-gamma (at protein level). Up-regulated in anaplastic thyroid cancer cell lines. {ECO:0000269|PubMed:15613457, ECO:0000269|PubMed:8066462}. |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12181345}. Nucleus {ECO:0000269|PubMed:12181345}. |
Modified Residue | MOD_RES 2; /note="N-acetylalanine"; /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:22814378"; MOD_RES 69; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:23186163" |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | Electron microscopy (37); X-ray crystallography (12) |
Cross Reference PDB | 4R3O; 4R67; 5A0Q; 5GJQ; 5GJR; 5L4G; 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; 15257295; 15282312; 15469984; 15571818; 15678106; 15678131; 15735756; 15781449; 15887188; 16169070; 16171779; 16371461; 16413484; 16421275; 16547521; 16611981; 16705181; 16707496; 16728642; 16818754; 16931761; 17115028; 17139257; 17183061; 17187060; 17218260; 17234884; 17283082; 17353931; 17948026; 18457437; 18497827; 18541707; 18922472; 18997794; 19379695; 19473982; 19573811; 19615732; 19684112; 19738201; 19759537; 19808967; 19955409; 20028659; 20154143; 20360384; 20661134; 20818436; 20858899; 20956384; 21357747; 21478859; 21532586; 21565611; 21799911; 21921029; 22190034; 22306028; 22306998; 22427670; 22623428; 22659184; 23018640; 23333871; 23661552; 23867461; 24012004; 24019521; 25260729; 25547115; 25604459; 25609649; 25654763; 26091038; 26183061; 26496610; 26542806; 26778333; 27791164; 28292943; 28541292; 29636472; 30479383; 31292253; 31473102; 32134919; 32783951; 34702852; 34711951; 7479848; 7479976; 7575604; 7628694; 7809113; 7831327; 7862124; 7957109; 9362451; 9380723; 9635433; 9660940; 9859996; 9990853; |
Motif | |
Gene Encoded By | |
Mass | 25,358 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |