IED ID | IndEnz0002013521 |
Enzyme Type ID | protease013521 |
Protein Name |
Ubiquitin carboxyl-terminal hydrolase YUH1 UCH EC 3.4.19.12 Ubiquitin thioesterase |
Gene Name | YUH1 YJR099W J1941 |
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 | MSGENRAVVPIESNPEVFTNFAHKLGLKNEWAYFDIYSLTEPELLAFLPRPVKAIVLLFPINEDRKSSTSQQITSSYDVIWFKQSVKNACGLYAILHSLSNNQSLLEPGSDLDNFLKSQSDTSSSKNRFDDVTTDQFVLNVIKENVQTFSTGQSEAPEATADTNLHYITYVEENGGIFELDGRNLSGPLYLGKSDPTATDLIEQELVRVRVASYMENANEEDVLNFAMLGLGPNWE |
Enzyme Length | 236 |
Uniprot Accession Number | P35127 |
Absorption | |
Active Site | ACT_SITE 90; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10091; ACT_SITE 166; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10091 |
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; Evidence={ECO:0000269|PubMed:10527495}; |
DNA Binding | |
EC Number | 3.4.19.12 |
Enzyme Function | FUNCTION: Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or RUB1. Preferentially cleaves ubiquitin from peptides and small adducts. {ECO:0000269|PubMed:12455997, ECO:0000269|PubMed:17709260, ECO:0000269|PubMed:21762696, ECO:0000269|PubMed:2555355}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 27 degrees Celsius. {ECO:0000269|PubMed:17709260}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. Inactive at a pH below 6.5. {ECO:0000269|PubMed:17709260}; |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Beta strand (8); Chain (1); Helix (9); Region (3); Site (2) |
Keywords | 3D-structure;Hydrolase;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 1CMX; |
Mapped Pubmed ID | 10413498; 10512618; 10953877; 11283351; 1429680; 14690591; 18802447; 19489724; 19520148; 19536198; 20954264; 23208446; 23966878; 24040173; 24961813; 27693354; 30137960; 8408016; 9521656; |
Motif | |
Gene Encoded By | |
Mass | 26,385 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.4.19.12; |