IED ID | IndEnz0002010732 |
Enzyme Type ID | protease010732 |
Protein Name |
Ubiquitin carboxyl-terminal hydrolase 17-like protein B USP17-B EC 3.4.19.12 Deubiquitinating enzyme 1A |
Gene Name | Usp17lb Dub1a |
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 | MVVALSFPEADPAMSPPSAPELHQDEAQVVEELAANGKHSLSWESPQGPGCGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSQTCCSPEGCKMCAMEAHVTQSLLHTHSGDVMKPSQNLTSAFHKRKQEDAHEFLMFTLETMHESCLQVHRQSEPTSEDSSPIHDIFGGWWRSQIKCHHCQGTSYSYDPFLDIPLDISSVQSVKQALQDTEKAEELCGENSYYCGRCRQKKPASKTLKLYSAPKVLMLVLKRFSGSMGKKLDRKVSYPEFLDLKPYLSQPTGGPLPYALYAVLVHEGATCHSGHYFCCVKAGHGKWYKMDDTKVTSCDVTSVLNENAYVLFYVQQNDLKKGSINMPEGRIHEVLDAKYQLKKSGEKKHNKSPCTEDAGEPCENREKRSSKETSLGEGKVLQEQDHQKAGQKQENTKLTPQEQNHEKGGQNLRNTEGELDRLSGAIVVYQPICTAN |
Enzyme Length | 468 |
Uniprot Accession Number | E9Q9U0 |
Absorption | |
Active Site | ACT_SITE 60; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01035, ECO:0000305|PubMed:14583620"; ACT_SITE 307; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01035" |
Activity Regulation | ACTIVITY REGULATION: Inhibited by ubiquitin aldehyde. {ECO:0000269|PubMed:14583620}. |
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:14583620}; |
DNA Binding | |
EC Number | 3.4.19.12 |
Enzyme Function | FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes. {ECO:0000269|PubMed:14583620}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Alternative sequence (1); Chain (1); Compositional bias (2); Domain (1); Mutagenesis (1); Region (2); Sequence conflict (8) |
Keywords | Alternative splicing;Hydrolase;Protease;Reference proteome;Thiol protease;Ubl conjugation;Ubl conjugation pathway |
Interact With | |
Induction | INDUCTION: Up-regulated by interleukin-3 (IL-3) in the B-lymphocyte cell line Ba/F3. May also be up-regulated in response to JAK2. {ECO:0000269|PubMed:14583620}. |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | PTM: Ubiquitinated. {ECO:0000269|PubMed:14583620}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 11468161; 15780755; 20403174; 8756639; 8995226; |
Motif | |
Gene Encoded By | |
Mass | 52,114 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |