IED ID | IndEnz0002011576 |
Enzyme Type ID | protease011576 |
Protein Name |
Proteasome activator complex subunit 2 11S regulator complex subunit beta REG-beta Activator of multicatalytic protease subunit 2 Proteasome activator 28 subunit beta PA28b PA28beta |
Gene Name | PSME2 |
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 | MAKPCGVRLSGEARKQVEVFRQNLFQEAEEFLYRFLPQKIIYLNQLLQEDSLNVADLTSLRAPLDIPIPDPPPKDDEMETDKQEKKEVHKCGFLPGNEKVLSLLALVKPEVWTLKEKCILVITWIQHLIPKIEDGNDFGVAIQEKVLERVNAVKTKVEAFQTTISKYFSERGDAVAKASKETHVMDYRALVHERDEAAYGELRAMVLDLRAFYAELYHIISSNLEKIVNPKGEEKPSMY |
Enzyme Length | 239 |
Uniprot Accession Number | Q9UL46 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Implicated in immunoproteasome assembly and required for efficient antigen processing. The PA28 activator complex enhances the generation of class I binding peptides by altering the cleavage pattern of the proteasome. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Initiator methionine (1); Modified residue (2); Natural variant (1); Sequence conflict (1) |
Keywords | 3D-structure;Acetylation;Direct protein sequencing;Phosphoprotein;Proteasome;Reference proteome |
Interact With | Q9BVJ7; Q8TBB1; Q06323; Itself; O00560; Q9BZL1 |
Induction | INDUCTION: By IFNG/IFN-gamma. |
Subcellular Location | |
Modified Residue | MOD_RES 2; /note="N-acetylalanine"; /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:22814378"; MOD_RES 10; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | Electron microscopy (2) |
Cross Reference PDB | 7DR6; 7DRW; |
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; 12200048; 12519221; 12600938; 12660156; 12682069; 12738770; 12750368; 12808096; 12816948; 12853446; 14508489; 14508490; 14528300; 14561893; 14564014; 14676825; 14684739; 14707141; 14734113; 14757770; 15014503; 15029244; 15084608; 15224091; 15224092; 15226418; 15257295; 15282312; 15469984; 15571818; 15678106; 15678131; 15735756; 15781449; 16038020; 16171779; 16189514; 16371461; 16413484; 16421275; 16547521; 16611981; 16705181; 16707496; 16728642; 16818754; 16931761; 17110338; 17115028; 17139257; 17183061; 17187060; 17218260; 17234884; 17283082; 17353931; 18497827; 18541707; 18997794; 19379695; 19473982; 19573811; 19684112; 19759537; 19808967; 19955409; 20028659; 20154143; 20360384; 20711500; 20818436; 20858899; 20956384; 21357747; 21478859; 21532586; 21799911; 21921029; 21988832; 22173998; 22306028; 22306998; 22427670; 23333871; 23624078; 23661552; 23867461; 24012004; 24019521; 24811749; 25260729; 25547115; 25654763; 26091038; 26183061; 26496610; 26542806; 26778333; 26944190; 29020885; 33262340; 33531497; 34257557; 7479848; 7479976; 7575604; 7628694; 7809113; 7831327; 7862124; 7957109; 9362451; 9380723; 9635433; 9660940; 9859996; 9990853; |
Motif | |
Gene Encoded By | |
Mass | 27,402 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |