| IED ID | IndEnz0002007566 |
| Enzyme Type ID | protease007566 |
| Protein Name |
26S proteasome non-ATPase regulatory subunit 4 26S proteasome regulatory subunit RPN10 26S proteasome regulatory subunit S5A Antisecretory factor 1 AF ASF Multiubiquitin chain-binding protein |
| Gene Name | PSMD4 MCB1 |
| 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 | MVLESTMVCVDNSEYMRNGDFLPTRLQAQQDAVNIVCHSKTRSNPENNVGLITLANDCEVLTTLTPDTGRILSKLHTVQPKGKITFCTGIRVAHLALKHRQGKNHKMRIIAFVGSPVEDNEKDLVKLAKRLKKEKVNVDIINFGEEEVNTEKLTAFVNTLNGKDGTGSHLVTVPPGPSLADALISSPILAGEGGAMLGLGASDFEFGVDPSADPELALALRVSMEEQRQRQEEEARRAAAASAAEAGIATTGTEDSDDALLKMTISQQEFGRTGLPDLSSMTEEEQIAYAMQMSLQGAEFGQAESADIDASSAMDTSEPAKEEDDYDVMQDPEFLQSVLENLPGVDPNNEAIRNAMGSLASQATKDGKKDKKEEDKK |
| Enzyme Length | 377 |
| Uniprot Accession Number | P55036 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMD4 acts as an ubiquitin receptor subunit through ubiquitin-interacting motifs and selects ubiquitin-conjugates for destruction. Displays a preferred selectivity for longer polyubiquitin chains. {ECO:0000269|PubMed:1317798, ECO:0000269|PubMed:15826667}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (2); Beta strand (7); Chain (1); Compositional bias (1); Cross-link (1); Domain (3); Helix (3); Modified residue (6); Region (6); Turn (1) |
| Keywords | 3D-structure;Alternative splicing;Direct protein sequencing;Isopeptide bond;Phosphoprotein;Proteasome;Reference proteome;Repeat;Ubl conjugation |
| Interact With | Q16186; P42858; P28066; P62191; P62195; O00232; Q13200; Itself; P54725; P54727; P0DPB3; Q9BYB0; Q9NUJ3; P0CG48; Q05086; Q05086-2; Q9UMX0; Q9Y5K5; P24610; Q62921 |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 250; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:O35226"; MOD_RES 253; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:O35226"; MOD_RES 256; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:O35226"; MOD_RES 266; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"; MOD_RES 358; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17323924, ECO:0007744|PubMed:23186163"; MOD_RES 361; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17323924, ECO:0007744|PubMed:23186163" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (10); Electron microscopy (30) |
| Cross Reference PDB | 1P9C; 1P9D; 1UEL; 1YX4; 1YX5; 1YX6; 2KDE; 2KDF; 5GJQ; 5GJR; 5L4K; 5LN3; 5M32; 5T0C; 5T0G; 5T0H; 5T0I; 5T0J; 5VFP; 5VFQ; 5VFR; 5VFS; 5VFT; 5VFU; 5VGZ; 5VHF; 5VHH; 5VHI; 5VHS; 6MSB; 6MSD; 6MSE; 6MSG; 6MSH; 6MSJ; 6MSK; 6MUN; 6U19; 6WJD; 6WJN; |
| Mapped Pubmed ID | 10075690; 10205060; 10375532; 10488153; 10514433; 10559916; 10693759; 10797013; 10828887; 10918611; 11046155; 11259415; 11285280; 11292861; 11292862; 11350924; 11454738; 11566882; 11585921; 11739726; 11842200; 11931757; 12070128; 12101228; 12136087; 12600938; 12660156; 12682069; 12738770; 12750368; 12808096; 12816948; 12853446; 14508489; 14508490; 14528300; 14561893; 14564014; 14676825; 14684739; 14707141; 14734113; 14743216; 14757770; 15014503; 15029244; 15084608; 15224091; 15224092; 15226418; 15257295; 15282312; 15469984; 15571818; 15678106; 15678131; 15735756; 15781449; 16171779; 16189514; 16371461; 16413484; 16421275; 16547521; 16611981; 16705181; 16707496; 16728642; 16818754; 16931761; 16990800; 17082820; 17115028; 17139257; 17183061; 17187060; 17218260; 17234884; 17283082; 17314511; 17353931; 17500595; 17662948; 17891176; 18497827; 18541707; 18922472; 18997794; 19379695; 19473982; 19490896; 19573811; 19615732; 19684112; 19759537; 19796170; 19798103; 19808967; 19931242; 19955409; 20028659; 20029029; 20059542; 20154143; 20195357; 20360384; 20711500; 20818436; 20858899; 20936779; 20956384; 21357747; 21478859; 21532586; 21799911; 21921029; 21988832; 22306028; 22306998; 22427670; 23333871; 23487458; 23661552; 23867461; 24012004; 24019521; 24189400; 24656813; 24811749; 25036637; 25260729; 25260751; 25547115; 25604459; 25609649; 25654763; 26091038; 26183061; 26496610; 26542806; 26638075; 26778333; 27791164; 28292943; 28541292; 28689658; 29636472; 30479383; 30664872; 32157086; 32783951; 7479848; 7479976; 7575604; 7628694; 7809113; 7831327; 7862124; 7957109; 8570649; 9362451; 9380723; 9635433; 9660940; 9859996; 9990853; |
| Motif | |
| Gene Encoded By | |
| Mass | 40,737 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |