Detail Information for IndEnz0002012642
IED ID IndEnz0002012642
Enzyme Type ID protease012642
Protein Name Ubiquitin carboxyl-terminal hydrolase isozyme L5
UCH-L5
EC 3.4.19.12
Ubiquitin C-terminal hydrolase UCH37
Ubiquitin thioesterase L5
Gene Name Uchl5 Uch37
Organism Mus musculus (Mouse)
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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MSSNAGEWCLMESDPGVFTELIKGFGCRGAQVEEIWSLEPESFEKLKPVHGLIFLFKWQPGEEPAGSVVQDSRLETIFFAKQVINNACATQAIVSVLLNCTHQDVHLGETLSEFKEFSQSFDAAMKGLALSNSDVIRQVHNSFARQQMFEFDTKTPAKEEDAFHFVSYVPVNGRLYELDGLREGPIDLGACNQDDWITAVRPVIEKRIQKYSEGEIRFNLMAIVSDRKMIYEQKIAELQRQLAEEEPMDTDQGSTVLSAIQSEVARNQMLIEEEVQKLKRYKIENIRRKHNYLPFIMELLKTLAEHQQLIPLVEKAKEKQNAKKAQETK
Enzyme Length 329
Uniprot Accession Number Q9WUP7
Absorption
Active Site ACT_SITE 88; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 164; /note=Proton donor; /evidence=ECO:0000250
Activity Regulation ACTIVITY REGULATION: Activated by ADRM1. Inhibited by interaction with NFRKB (By similarity). {ECO:0000250}.
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: Protease that specifically cleaves 'Lys-48'-linked polyubiquitin chains. Deubiquitinating enzyme associated with the 19S regulatory subunit of the 26S proteasome. Putative regulatory component of the INO80 complex; however is inactive in the INO80 complex and is activated by a transient interaction of the INO80 complex with the proteasome via ADRM1 (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Alternative sequence (1); Beta strand (9); Chain (1); Helix (13); Modified residue (3); Region (1); Sequence conflict (3); Site (1)
Keywords 3D-structure;Acetylation;Alternative splicing;Cytoplasm;DNA damage;DNA recombination;DNA repair;Hydrolase;Nucleus;Protease;Proteasome;Reference proteome;Thiol protease;Transcription;Transcription regulation;Ubl conjugation pathway
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Associates with the proteasome 19S subunit in the cytoplasm. Associates with the INO80 complex in the nucleus (By similarity). {ECO:0000250}.
Modified Residue MOD_RES 47; /note=N6-succinyllysine; /evidence=ECO:0007744|PubMed:23806337; MOD_RES 158; /note=N6-acetyllysine; /evidence=ECO:0007744|PubMed:23806337; MOD_RES 289; /note=N6-succinyllysine; /evidence=ECO:0007744|PubMed:23806337
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (2)
Cross Reference PDB 4WLQ; 4WLR;
Mapped Pubmed ID 11217851; 11389549; 12466851; 14610273; 15489855; 16027725; 18799693; 21048919; 21267068; 23341450; 23500140; 23892456; 23979016; 25702872; 26222436; 26514267; 26811477; 27626380; 27764765; 32296042;
Motif
Gene Encoded By
Mass 37,617
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda