| IED ID | IndEnz0002000987 |
| Enzyme Type ID | protease000987 |
| Protein Name |
Proteasome subunit beta type-9 EC 3.4.25.1 Low molecular mass protein 2 Macropain chain 7 Multicatalytic endopeptidase complex chain 7 Proteasome chain 7 Proteasome subunit beta-1i Really interesting new gene 12 protein |
| Gene Name | PSMB9 LMP2 PSMB6i RING12 |
| 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 | MLRAGAPTGDLPRAGEVHTGTTIMAVEFDGGVVMGSDSRVSAGEAVVNRVFDKLSPLHERIYCALSGSAADAQAVADMAAYQLELHGIELEEPPLVLAAANVVRNISYKYREDLSAHLMVAGWDQREGGQVYGTLGGMLTRQPFAIGGSGSTFIYGYVDAAYKPGMSPEECRRFTTDAIALAMSRDGSSGGVIYLVTITAAGVDHRVILGNELPKFYDE |
| Enzyme Length | 219 |
| Uniprot Accession Number | P28065 |
| Absorption | |
| Active Site | ACT_SITE 21; /note=Nucleophile |
| 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. Replacement of PSMB6 by PSMB9 increases the capacity of the immunoproteasome to cleave model peptides after hydrophobic and basic residues. {ECO:0000269|PubMed:8163024}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (1); Beta strand (12); Chain (1); Helix (5); Modified residue (2); Mutagenesis (3); Natural variant (5); Propeptide (1); Site (1); Turn (2) |
| Keywords | 3D-structure;Acetylation;Alternative splicing;Cytoplasm;Host-virus interaction;Hydrolase;Immunity;Nucleus;Protease;Proteasome;Reference proteome;Threonine protease;Zymogen |
| Interact With | Q24JT5; Q96D03; Q9Y3R0; Q14657; Q15788; Q9Y6Q9; Q9Y244; Q99436; Q9WMX2; Q9WMX2 |
| Induction | INDUCTION: Up-regulated by interferon gamma (at protein level). Up-regulated by IRF1. Up-regulated by tumor necrosis factor-alpha (at protein level). Up-regulated by tetrodotoxin (TTX) in glial cells. Up-regulated in Crohn's bowel disease (CD). Up-regulated by heat shock treatment. Up-regulated by CD40L via the NFKB1 pathway in cancer cells. {ECO:0000269|PubMed:11493458, ECO:0000269|PubMed:15501285, ECO:0000269|PubMed:15907481, ECO:0000269|PubMed:17142736, ECO:0000269|PubMed:17262812, ECO:0000269|PubMed:18694960, ECO:0000269|PubMed:8663318}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}. |
| Modified Residue | MOD_RES 53; /note=N6-acetyllysine; /evidence=ECO:0007744|PubMed:19608861; MOD_RES 109; /note=N6-acetyllysine; /evidence=ECO:0007744|PubMed:19608861 |
| 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 (1); X-ray crystallography (2) |
| Cross Reference PDB | 6AVO; 6E5B; 7AWE; |
| Mapped Pubmed ID | 10075690; 10205060; 10375532; 10468973; 10514433; 10559916; 10693759; 10797013; 10828887; 10918611; 11046155; 11259415; 11285280; 11292861; 11292862; 11350924; 11454738; 11566882; 11585840; 11585921; 11739726; 11842200; 11931757; 12070128; 12101228; 12136087; 12600938; 12660156; 12682069; 12738770; 12750368; 12808096; 12816948; 12853446; 14508489; 14508490; 14528300; 14561893; 14564014; 14676825; 14684739; 14707141; 14733938; 14734113; 14757770; 15014503; 15029244; 15084608; 15224091; 15224092; 15226418; 15257295; 15282312; 15469984; 15488952; 15571818; 15678106; 15678131; 15686587; 15735756; 15781449; 16171779; 16371461; 16413484; 16421275; 16547521; 16611981; 16705181; 16707496; 16728642; 16818754; 16931761; 17115028; 17139257; 17183061; 17187060; 17218260; 17234884; 17283082; 17581627; 18497827; 18541707; 18985028; 18997794; 19379695; 19473982; 19573811; 19684112; 19759537; 19808967; 19955409; 20028659; 20154143; 20360384; 20723761; 20818436; 20858899; 20956384; 21357747; 21478859; 21532586; 21799911; 21921029; 22306028; 22306998; 22427670; 23333871; 23661552; 23867461; 24012004; 24019521; 25260729; 25547115; 25654763; 26091038; 26183061; 26542806; 26778333; 29167449; 31283222; 34045234; 7479848; 7479976; 7575604; 7628694; 7809113; 7831327; 7862124; 7911550; 7957109; 9348140; 9362451; 9380723; 9496154; 9635433; 9660940; 9859996; 9990853; |
| Motif | |
| Gene Encoded By | |
| Mass | 23,264 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |