Detail Information for IndEnz0002009233
IED ID IndEnz0002009233
Enzyme Type ID protease009233
Protein Name Ubiquitin thioesterase OTU1
EC 3.4.19.12
OTU domain-containing protein 1
Gene Name OTU1 YFL044C
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 MKLKVTGAGINQVVTLKQDATLNDLIEHINVDVKTMRFGYPPQRINLQGEDASLGQTQLDELGINSGEKITIESSDSNESFSLPPPQPKPKRVLKSTEMSIGGSGENVLSVHPVLDDNSCLFHAIAYGIFKQDSVRDLREMVSKEVLNNPVKFNDAILDKPNKDYAQWILKMESWGGAIEIGIISDALAVAIYVVDIDAVKIEKFNEDKFDNYILILFNGIHYDSLTMNEFKTVFNKNQPESDDVLTAALQLASNLKQTGYSFNTHKAQIKCNTCQMTFVGEREVARHAESTGHVDFGQNR
Enzyme Length 301
Uniprot Accession Number P43558
Absorption
Active Site ACT_SITE 117; /evidence=ECO:0000250|UniProtKB:Q96FW1; ACT_SITE 120; /note=Nucleophile; /evidence=ECO:0000305; ACT_SITE 222; /evidence=ECO:0000250|UniProtKB:Q5VVQ6; ACT_SITE 294; /evidence=ECO:0000250|UniProtKB:Q96FW1
Activity Regulation
Binding Site BINDING 221; /note=Substrate; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q5VVQ6
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:0000250|UniProtKB:Q5VVQ6};
DNA Binding
EC Number 3.4.19.12
Enzyme Function FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Participates in the regulation of the ubiquitin conjugation pathway involving CDC48 by hindering multiubiquitination of substrates at the CDC48 chaperone. May be indirectly involved in PIS1 gene expression. {ECO:0000269|PubMed:15755922, ECO:0000269|PubMed:16427015}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (4); Beta strand (11); Binding site (1); Chain (1); Cross-link (1); Domain (1); Helix (9); Mutagenesis (1); Region (5); Turn (6); Zinc finger (1)
Keywords 3D-structure;Cytoplasm;Hydrolase;Isopeptide bond;Metal-binding;Nucleus;Protease;Reference proteome;Thiol protease;Ubl conjugation;Ubl conjugation pathway;Zinc;Zinc-finger
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (4)
Cross Reference PDB 3BY4; 3C0R; 4KDI; 4KDL;
Mapped Pubmed ID 10664582; 11283351; 14690591; 16429126; 16554755; 17142044; 18270205; 18315532; 18719252; 19489724; 19536198; 21741246; 22842922; 23217712; 24610782; 25084388; 25215493; 26503604; 27787227; 9171100;
Motif
Gene Encoded By
Mass 33,510
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda