Detail Information for IndEnz0002011239
IED ID IndEnz0002011239
Enzyme Type ID protease011239
Protein Name Ubiquitin carboxyl-terminal hydrolase 5
EC 3.4.19.12
Deubiquitinating enzyme 5
Ubiquitin thioesterase 5
Ubiquitin-specific-processing protease 5
Gene Name UBP5
Organism Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
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) Ponginae Pongo Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Enzyme Sequence MAELSEEALLSVLPTIRVPKAGDRVHKDECAFSFDTPESEGGLYICMNTFLGFGKQYVERHFNKTGPRVYLHLRRTRRPKEEDPTTGTGDPPRKKPTRLAIGVEGGFDLSEEKFELDEDVKIVILPDYLEIARDGLGGLPDIVRDRVTSAVEALLSADSASRKQEVQAWDGEVRQVSKHAFSLKQLDNPARIPPCGWECSKCDMRENLWLNLTDGSILCGRRYFDGSGGNNHAVEHYRETGYPLAVKLGTITPDGADVYSYDEDDMVLDPSLAEHLSHFGIDMLKMQKTDKTMTELEIDMNQRIGEWELIQESGVPLKPLFGPGYTGIRNLGNSCYLNSVVLVLFSIPDFQRKYVDKLEKIFQNAPTDPTQDFSTQVAKLGHGLLSGEYSKPVPESGDGERVPEQKEVQDGIAPRMFKALIGKGHPEFSTNRQQDAQEFFLHLINMVERNCRSSENPNEVFRFLVEEKIKCLATEKVKYTQRVDYIMQLPVPMDAALNKEELLEYEEKKRQAEEEKMALPELVRAQVPFSSCLEAYGAPEQVDDFWSTALQAKSVAVKTTRFASFPDYLVIQIKKFTFGLDWVPKKLDVSIEMPEELDISQLRGTGLQPGEEELPDIAPPLVTPDEPKGSLGFYGNEDEDSFCSPHFSSPTSPMLDESVIIQLVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSHMDDPDFANPLILPGSSGPGSTSAAADPPPEDCVTTIVSMGFSRDQALKALRATNNSLERAVDWIFSHIDDLDAEAAMDISEGRSAADSISESVPVGPKVRDGPGKYQLFAFISHMGTSTMCGHYVCHIKKEGRWVIYNDQKVCASEKPPKDLGYIYFYQRVAS
Enzyme Length 858
Uniprot Accession Number Q5R407
Absorption
Active Site ACT_SITE 335; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10093; ACT_SITE 818; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10093
Activity Regulation
Binding Site BINDING 209; /note=Substrate; /evidence=ECO:0000250; BINDING 259; /note=Substrate; /evidence=ECO:0000250; BINDING 261; /note=Substrate; via carbonyl oxygen; /evidence=ECO:0000250; BINDING 264; /note=Substrate; /evidence=ECO:0000250
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: Cleaves linear and branched multiubiquitin polymers with a marked preference for branched polymers. Involved in unanchored 'Lys-48'-linked polyubiquitin disassembly. Binds linear and 'Lys-63'-linked polyubiquitin with a lower affinity (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Binding site (4); Chain (1); Compositional bias (1); Disulfide bond (1); Domain (3); Initiator methionine (1); Metal binding (4); Modified residue (7); Region (2); Zinc finger (1)
Keywords Acetylation;Disulfide bond;Hydrolase;Metal-binding;Phosphoprotein;Protease;Reference proteome;Repeat;Thiol protease;Ubl conjugation pathway;Zinc;Zinc-finger
Interact With
Induction
Subcellular Location
Modified Residue MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0000250|UniProtKB:P45974; MOD_RES 156; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P45974; MOD_RES 292; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P45974; MOD_RES 623; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P56399; MOD_RES 779; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P45974; MOD_RES 783; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P45974; MOD_RES 785; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P45974
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 95,771
Kinetics
Metal Binding METAL 199; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 202; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 219; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 232; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502
Rhea ID
Cross Reference Brenda