| IED ID | IndEnz0002010934 |
| Enzyme Type ID | protease010934 |
| Protein Name |
26S proteasome non-ATPase regulatory subunit 2 26S proteasome regulatory subunit RPN1 26S proteasome regulatory subunit S2 26S proteasome subunit p97 Protein 55.11 Tumor necrosis factor type 1 receptor-associated protein 2 |
| Gene Name | PSMD2 TRAP2 |
| 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 | MEEGGRDKAPVQPQQSPAAAPGGTDEKPSGKERRDAGDKDKEQELSEEDKQLQDELEMLVERLGEKDTSLYRPALEELRRQIRSSTTSMTSVPKPLKFLRPHYGKLKEIYENMAPGENKRFAADIISVLAMTMSGERECLKYRLVGSQEELASWGHEYVRHLAGEVAKEWQELDDAEKVQREPLLTLVKEIVPYNMAHNAEHEACDLLMEIEQVDMLEKDIDENAYAKVCLYLTSCVNYVPEPENSALLRCALGVFRKFSRFPEALRLALMLNDMELVEDIFTSCKDVVVQKQMAFMLGRHGVFLELSEDVEEYEDLTEIMSNVQLNSNFLALARELDIMEPKVPDDIYKTHLENNRFGGSGSQVDSARMNLASSFVNGFVNAAFGQDKLLTDDGNKWLYKNKDHGMLSAAASLGMILLWDVDGGLTQIDKYLYSSEDYIKSGALLACGIVNSGVRNECDPALALLSDYVLHNSNTMRLGSIFGLGLAYAGSNREDVLTLLLPVMGDSKSSMEVAGVTALACGMIAVGSCNGDVTSTILQTIMEKSETELKDTYARWLPLGLGLNHLGKGEAIEAILAALEVVSEPFRSFANTLVDVCAYAGSGNVLKVQQLLHICSEHFDSKEKEEDKDKKEKKDKDKKEAPADMGAHQGVAVLGIALIAMGEEIGAEMALRTFGHLLRYGEPTLRRAVPLALALISVSNPRLNILDTLSKFSHDADPEVSYNSIFAMGMVGSGTNNARLAAMLRQLAQYHAKDPNNLFMVRLAQGLTHLGKGTLTLCPYHSDRQLMSQVAVAGLLTVLVSFLDVRNIILGKSHYVLYGLVAAMQPRMLVTFDEELRPLPVSVRVGQAVDVVGQAGKPKTITGFQTHTTPVLLAHGERAELATEEFLPVTPILEGFVILRKNPNYDL |
| Enzyme Length | 908 |
| Uniprot Accession Number | Q13200 |
| 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. {ECO:0000269|PubMed:1317798}.; FUNCTION: Binds to the intracellular domain of tumor necrosis factor type 1 receptor. The binding domain of TRAP1 and TRAP2 resides outside the death domain of TNFR1. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (2); Chain (1); Compositional bias (1); Erroneous initiation (1); Modified residue (9); Natural variant (3); Region (2); Repeat (7); Sequence conflict (14) |
| Keywords | 3D-structure;Acetylation;Alternative splicing;Direct protein sequencing;Phosphoprotein;Proteasome;Reference proteome;Repeat |
| Interact With | Q16186; Q99933; P27797; P36957; Q9H8Y8; P58340; Q8TDX7; P17612; P62191; Q53XL8; P35998; P62195; P55036; P54725; P50454; Q13148; Q6DHY5; P37173; Q8WVY7; Q9UHD9; Q9Y5K5; Q9Y2B5; O15060; Q53HB3; Q8AZK7; Q8K2C9 |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 1; /note="N-acetylmethionine"; /evidence="ECO:0000250|UniProtKB:Q8VDM4"; MOD_RES 16; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17323924, ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 24; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:17323924, ECO:0007744|PubMed:20068231"; MOD_RES 29; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17323924"; MOD_RES 147; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 194; /note="Phosphotyrosine"; /evidence="ECO:0007744|PubMed:17323924"; MOD_RES 361; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 363; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 551; /note="N6-acetyllysine"; /evidence="ECO:0000250|UniProtKB:Q8VDM4" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | Electron microscopy (34) |
| Cross Reference PDB | 5GJQ; 5GJR; 5L4K; 5LN3; 5T0C; 5T0G; 5T0H; 5T0I; 5T0J; 5VFP; 5VFQ; 5VFR; 5VFS; 5VFT; 5VFU; 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; 14676825; 14684739; 14707141; 14734113; 14743216; 14757770; 15014503; 15029244; 15084608; 15161933; 15224091; 15224092; 15226418; 15257295; 15282312; 15469984; 15571818; 15678106; 15678131; 15735756; 15781449; 16169070; 16171779; 16189514; 16371461; 16413484; 16421275; 16547521; 16611981; 16705181; 16707496; 16728642; 16763564; 16818754; 16931761; 16990800; 17110338; 17115028; 17139257; 17183061; 17187060; 17218260; 17220478; 17234884; 17283082; 17314511; 17353931; 18337449; 18457437; 18497827; 18541707; 18922472; 18997794; 19060904; 19214193; 19379695; 19473982; 19490896; 19573811; 19615732; 19626040; 19638347; 19684112; 19759537; 19805454; 19808967; 19815544; 19881955; 19955409; 20028659; 20085233; 20154143; 20360384; 20467437; 20562859; 20711500; 20800603; 20818436; 20858899; 20956384; 21150319; 21357747; 21465578; 21478859; 21532586; 21799911; 21911578; 21921029; 22304920; 22306028; 22306998; 22427670; 22623428; 22653443; 22682247; 22901813; 23333871; 23606334; 23650620; 23661552; 23667555; 23867461; 24012004; 24019521; 24189400; 24725412; 25036637; 25260729; 25416956; 25547115; 25604459; 25609649; 25654763; 26091038; 26183061; 26496610; 26514267; 26542806; 26638075; 26778333; 27791164; 28292943; 28689658; 29636472; 29777785; 29804830; 30479383; 31136974; 31703613; 32566659; 32783951; 7479848; 7479976; 7575604; 7628694; 7809113; 7831327; 7862124; 7957109; 9362451; 9380723; 9635433; 9660940; 9859996; 9990853; |
| Motif | |
| Gene Encoded By | |
| Mass | 100,200 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |