IED ID | IndEnz0002011963 |
Enzyme Type ID | protease011963 |
Protein Name |
Ubiquitin carboxyl-terminal hydrolase 17-like protein A USP17-A EC 3.4.19.12 Deubiquitinating enzyme 1 Ubiquitin carboxyl-terminal hydrolase DUB-1 Ubiquitin thioesterase DUB-1 Ubiquitin-specific-processing protease DUB-1 |
Gene Name | Usp17la Dub-1 Dub1 |
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 | MVVALSFPEADPALSSPDAPELHQDEAQVVEELTVNGKHSLSWESPQGPGCGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSQTCCSPEGCKLCAMEALVTQSLLHSHSGDVMKPSHILTSAFHKHQQEDAHEFLMFTLETMHESCLQVHRQSKPTSEDSSPIHDIFGGWWRSQIKCLLCQGTSDTYDRFLDIPLDISSAQSVKQALWDTEKSEELCGDNAYYCGKCRQKMPASKTLHVHIAPKVLMVVLNRFSAFTGNKLDRKVSYPEFLDLKPYLSEPTGGPLPYALYAVLVHDGATSHSGHYFCCVKAGHGKWYKMDDTKVTRCDVTSVLNENAYVLFYVQQANLKQVSIDMPEGRINEVLDPEYQLKKSRRKKHKKKSPFTEDLGEPCENRDKRAIKETSLGKGKVLQEVNHKKAGQKHGNTKLMPQKQNHQKAGQNLRNTEVELDLPADAIVIHQPRSTANWGRDSPDKENQPLHNADRLLTSQGPVNTWQLCRQEGRRRSKKGQNKNKQGQRLLLVC |
Enzyme Length | 526 |
Uniprot Accession Number | Q61068 |
Absorption | |
Active Site | ACT_SITE 60; /note="Nucleophile"; ACT_SITE 307; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093" |
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:8622927}; |
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. Has deubiquitinating enzyme activity for DNAH5, suggesting a role in the regulation of DNAH5 degradation by the ubiquitin-proteasome pathway. Has growth-suppressing activity; induces arrest in G1 phase upon controlled expression. {ECO:0000269|PubMed:18980247, ECO:0000269|PubMed:8622927}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Domain (1); Mutagenesis (1); Region (3) |
Keywords | Hydrolase;Protease;Reference proteome;Thiol protease;Ubl conjugation;Ubl conjugation pathway |
Interact With | |
Induction | INDUCTION: Up-regulated by IL3, IL5 and CSF2. {ECO:0000269|PubMed:8622927, ECO:0000269|PubMed:8756639}. |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | PTM: Polyubiquitinated; ubiquitination leads to its subsequent degradation. {ECO:0000269|PubMed:18980247}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 11468161; 12447969; 14583620; 15780755; 20403174; 31806660; 32527007; 8995226; 9154835; |
Motif | |
Gene Encoded By | |
Mass | 59,073 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |