| IED ID | IndEnz0002006359 |
| Enzyme Type ID | protease006359 |
| Protein Name |
26S proteasome non-ATPase regulatory subunit 14 EC 3.4.19.- 26S proteasome regulatory subunit RPN11 26S proteasome-associated PAD1 homolog 1 |
| Gene Name | PSMD14 POH1 |
| 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 | MDRLLRLGGGMPGLGQGPPTDAPAVDTAEQVYISSLALLKMLKHGRAGVPMEVMGLMLGEFVDDYTVRVIDVFAMPQSGTGVSVEAVDPVFQAKMLDMLKQTGRPEMVVGWYHSHPGFGCWLSGVDINTQQSFEALSERAVAVVVDPIQSVKGKVVIDAFRLINANMMVLGHEPRQTTSNLGHLNKPSIQALIHGLNRHYYSITINYRKNELEQKMLLNLHKKSWMEGLTLQDYSEHCKHNESVVKEMLELAKNYNKAVEEEDKMTPEQLAIKNVGKQDPKRHLEEHVDVLMTSNIVQCLAAMLDTVVFK |
| Enzyme Length | 310 |
| Uniprot Accession Number | O00487 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.19.- |
| 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. The PSMD14 subunit is a metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains within the complex. Plays a role in response to double-strand breaks (DSBs): acts as a regulator of non-homologous end joining (NHEJ) by cleaving 'Lys-63'-linked polyubiquitin, thereby promoting retention of JMJD2A/KDM4A on chromatin and restricting TP53BP1 accumulation. Also involved in homologous recombination repair by promoting RAD51 loading. {ECO:0000269|PubMed:1317798, ECO:0000269|PubMed:22909820, ECO:0000269|PubMed:9374539}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (1); Metal binding (3); Modified residue (3); Motif (1); Mutagenesis (1) |
| Keywords | 3D-structure;DNA damage;DNA repair;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Proteasome;Reference proteome;Ubl conjugation pathway;Zinc |
| Interact With | Q9C005; Q8IZU0; P42858; P50222; P51665 |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 150; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17693683, ECO:0007744|PubMed:24275569"; MOD_RES 224; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17323924"; MOD_RES 266; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:23186163" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | Electron microscopy (30) |
| Cross Reference PDB | 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; 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; 12353037; 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; 16169070; 16171779; 16371461; 16413484; 16421275; 16547521; 16569633; 16611981; 16705181; 16707496; 16728642; 16818754; 16931761; 17115028; 17139257; 17183061; 17187060; 17218260; 17234884; 17237285; 17283082; 17353931; 18497827; 18541707; 18922472; 18997794; 19379695; 19419512; 19473982; 19490896; 19573811; 19615732; 19684112; 19732767; 19759537; 19808967; 19955409; 20028659; 20154143; 20195357; 20360384; 20818436; 20858899; 20956384; 21357747; 21478859; 21532586; 21799911; 21921029; 21988832; 22306028; 22306998; 22427670; 23333871; 23606334; 23650620; 23661552; 23867461; 24012004; 24019521; 24811749; 25260729; 25416956; 25547115; 25609649; 25654763; 26091038; 26183061; 26496610; 26510456; 26542806; 26638075; 26778333; 27791164; 28292943; 28535005; 28541292; 28689658; 29331416; 29573636; 29636472; 30479383; 30745168; 31212367; 31634528; 31685442; 32210007; 32783951; 33154524; 33456565; 33897885; 7479848; 7479976; 7575604; 7628694; 7809113; 7831327; 7862124; 7957109; 9362451; 9380723; 9635433; 9660940; 9859996; 9990853; |
| Motif | MOTIF 113..126; /note=JAMM motif; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182 |
| Gene Encoded By | |
| Mass | 34,577 |
| Kinetics | |
| Metal Binding | METAL 113; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 115; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 126; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182 |
| Rhea ID | |
| Cross Reference Brenda |