Detail Information for IndEnz0002010947
IED ID IndEnz0002010947
Enzyme Type ID protease010947
Protein Name Ubiquitin carboxyl-terminal hydrolase RPN11
EC 3.4.19.12
26S proteasome regulatory subunit RPN11
Protein MPR1
Gene Name RPN11 MPR1 YFR004W
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Enzyme Sequence MERLQRLMMNSKVGSADTGRDDTKETVYISSIALLKMLKHGRAGVPMEVMGLMLGEFVDDYTVNVVDVFAMPQSGTGVSVEAVDDVFQAKMMDMLKQTGRDQMVVGWYHSHPGFGCWLSSVDVNTQKSFEQLNSRAVAVVVDPIQSVKGKVVIDAFRLIDTGALINNLEPRQTTSNTGLLNKANIQALIHGLNRHYYSLNIDYHKTAKETKMLMNLHKEQWQSGLKMYDYEEKEESNLAATKSMVKIAEQYSKRIEEEKELTEEELKTRYVGRQDPKKHLSETADETLENNIVSVLTAGVNSVAIK
Enzyme Length 306
Uniprot Accession Number P43588
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12;
DNA Binding
EC Number 3.4.19.12
Enzyme Function FUNCTION: Component of the lid subcomplex of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. RPN11 is the only catalytically active member of the lid and serves as the essential deubiquitinase of the proteasome. {ECO:0000269|PubMed:12183636, ECO:0000269|PubMed:21075847, ECO:0000269|PubMed:24463465}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (8); Chain (1); Domain (1); Helix (11); Metal binding (3); Modified residue (1); Motif (1); Mutagenesis (2); Natural variant (4); Region (1); Turn (1)
Keywords 3D-structure;Acetylation;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Proteasome;Reference proteome;Thiol protease;Ubl conjugation pathway;Zinc
Interact With Q12250; Q08723; Q04062; P33299; P40327; P33298; P53549; Q01939
Induction
Subcellular Location
Modified Residue MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0000269|PubMed:12504901
Post Translational Modification PTM: N-acetylated by NAT3. {ECO:0000269|PubMed:12504901}.
Signal Peptide
Structure 3D Electron microscopy (26); X-ray crystallography (8)
Cross Reference PDB 3J47; 3JCK; 3JCO; 3JCP; 4CR2; 4CR3; 4CR4; 4O8X; 4O8Y; 4OCL; 4OCM; 4OCN; 4OWP; 5A5B; 5MPB; 5MPC; 5MPD; 5MPE; 5U4P; 5W83; 5WVI; 5WVK; 6EF3; 6FVT; 6FVU; 6FVV; 6FVW; 6FVX; 6FVY; 6J2C; 6J2N; 6J2Q; 6J2X; 6J30;
Mapped Pubmed ID 10363642; 10664589; 10688190; 10757750; 10913188; 11062549; 11157770; 11283351; 11595789; 11742986; 11805826; 11805837; 11943459; 12353019; 12353037; 12370088; 12386321; 12477409; 14581483; 14759368; 15018611; 15188770; 15210724; 15571806; 15905137; 16269334; 16284124; 16429126; 16554755; 16869714; 16922378; 17004651; 17499717; 17900906; 18172023; 18315532; 18373682; 18467557; 18504300; 18604275; 18757749; 19153599; 19194013; 19446322; 19446323; 19489724; 19536198; 19683491; 19773362; 20061387; 20074027; 20170199; 20550582; 20800707; 20941496; 21059189; 21139140; 21278740; 21321079; 21543789; 21572441; 21619884; 21685082; 21931558; 21966278; 22237024; 22350874; 22350895; 22412391; 22842922; 22956996; 23202731; 23545412; 23545414; 23672618; 23770819; 23936414; 24384752; 24429290; 24516147; 24598877; 24681338; 24706844; 24857655; 24997605; 25218923; 25333764; 25389291; 25540361; 26130806; 26182356; 26262643; 26301997; 26327695; 26339477; 26365526; 26451487; 26642761; 26744777; 26929360; 27053109; 27092291; 27677933; 28106073; 28115689; 28844860; 30067984; 30309908; 30792173; 7565661; 9584156; 9647729; 9741626; 9763452;
Motif MOTIF 109..122; /note=JAMM motif; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182
Gene Encoded By
Mass 34,398
Kinetics
Metal Binding METAL 109; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 111; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 122; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182
Rhea ID
Cross Reference Brenda