| IED ID | IndEnz0002010054 |
| Enzyme Type ID | protease010054 |
| Protein Name |
26S proteasome regulatory subunit 4 P26s4 26S proteasome AAA-ATPase subunit RPT2 Proteasome 26S subunit ATPase 1 |
| Gene Name | PSMC1 |
| 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 | MGQSQSGGHGPGGGKKDDKDKKKKYEPPVPTRVGKKKKKTKGPDAASKLPLVTPHTQCRLKLLKLERIKDYLLMEEEFIRNQEQMKPLEEKQEEERSKVDDLRGTPMSVGTLEEIIDDNHAIVSTSVGSEHYVSILSFVDKDLLEPGCSVLLNHKVHAVIGVLMDDTDPLVTVMKVEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICTEAGLMALRERRMKVTNEDFKKSKENVLYKKQEGTPEGLYL |
| Enzyme Length | 440 |
| Uniprot Accession Number | P62191 |
| 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. PSMC1 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides. {ECO:0000269|PubMed:1317798}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 226..233; /note=ATP; /evidence=ECO:0000255 |
| Features | Alternative sequence (1); Chain (1); Compositional bias (2); Cross-link (1); Initiator methionine (1); Lipidation (1); Modified residue (5); Nucleotide binding (1); Region (2); Sequence conflict (3) |
| Keywords | 3D-structure;ATP-binding;Acetylation;Alternative splicing;Cytoplasm;Direct protein sequencing;Isopeptide bond;Lipoprotein;Membrane;Myristate;Nucleotide-binding;Nucleus;Phosphoprotein;Proteasome;Reference proteome;Ubl conjugation |
| Interact With | O60341; Q8TBB1; P43356; P50222; Q3KNR5; P35998; P43686; P62333; Q13200; P55036; Q16401; P37840; P00441; O43463; P55072; Q96BR9 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. |
| Modified Residue | MOD_RES 4; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19690332"; MOD_RES 53; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 258; /note="N6-acetyllysine"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 434; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 439; /note="Phosphotyrosine"; /evidence="ECO:0007744|PubMed:15144186" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | Electron microscopy (36) |
| Cross Reference PDB | 5GJQ; 5GJR; 5L4G; 5LN3; 5M32; 5T0C; 5T0G; 5T0H; 5T0I; 5T0J; 5VFP; 5VFQ; 5VFR; 5VFS; 5VFT; 5VFU; 5VGZ; 5VHF; 5VHH; 5VHI; 5VHJ; 5VHM; 5VHN; 5VHO; 5VHP; 5VHQ; 5VHR; 5VHS; 6MSB; 6MSD; 6MSG; 6MSH; 6MSJ; 6MSK; 6WJD; 6WJN; |
| 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; 12600938; 12660156; 12682069; 12738770; 12750368; 12808096; 12816948; 12853446; 14508489; 14508490; 14528300; 14561893; 14564014; 14578856; 14676825; 14684739; 14707141; 14734113; 14743216; 14757770; 15014503; 15029244; 15084608; 15215856; 15224091; 15224092; 15226418; 15257295; 15282312; 15362974; 15469984; 15571818; 15678106; 15678131; 15735756; 15781449; 16055502; 16168377; 16171779; 16189514; 16371461; 16413484; 16421275; 16547521; 16611981; 16705181; 16707496; 16728642; 16818754; 16931761; 16990800; 17115028; 17139257; 17183061; 17187060; 17218260; 17234884; 17283082; 17314511; 17353931; 18497827; 18541707; 18701681; 18922472; 18997794; 19060904; 19214193; 19379695; 19473982; 19490896; 19573811; 19615732; 19684112; 19759537; 19805454; 19808967; 19955409; 20028659; 20154143; 20195357; 20360384; 20379614; 20424172; 20467437; 20562859; 20818436; 20858899; 20956384; 21150319; 21357747; 21478859; 21532586; 21799911; 21900206; 21921029; 22306028; 22306998; 22427670; 22653443; 22901813; 22948515; 23333871; 23455924; 23661552; 23867461; 24012004; 24019521; 24189400; 24811749; 25260729; 25277244; 25416956; 25519916; 25547115; 25604459; 25609649; 25654763; 25665578; 25814554; 26091038; 26183061; 26496610; 26542806; 26611529; 26778333; 26872363; 27791164; 28292943; 28541292; 28689658; 29636472; 30479383; 32783951; 33634591; 7479848; 7479976; 7575604; 7628694; 7809113; 7831327; 7862124; 7957109; 9362451; 9374493; 9380723; 9635433; 9660940; 9859996; 9990853; |
| Motif | |
| Gene Encoded By | |
| Mass | 49,185 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |