| IED ID | IndEnz0002012015 |
| Enzyme Type ID | protease012015 |
| Protein Name |
Ubiquitin carboxyl-terminal hydrolase 48 EC 3.4.19.12 Deubiquitinating enzyme 48 Synaptic ubiquitin-specific protease synUSP Ubiquitin thioesterase 48 Ubiquitin-specific-processing protease 48 |
| Gene Name | Usp48 |
| Organism | Rattus norvegicus (Rat) |
| 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 Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MAPRLQLEKAAWRWAETVRPEEVSQEHIETAYRIWLEPCIRGVCRRNCRGNPNCLVGIGEHIWLGEIDENSFHNIDDPNCERRKKNSFVGLTNLGASCYVNTFLQVWFLNLELRQALYLCPSTCSDYTKGDGIRGGKDYEPQTICEHLQYLFALLQNSNRRYIDPSGFVKALGLDTGQQQDAQESSKLFMSLLEDTLSKQKNPDVRNVVQQQFCGEYAYVTVCSQCGRESKLVSKFYELELNIQGHKQLTDCISEFLKEERLEGDNRYFCENCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNAYIGFSESLDMEPYVEHKGGSFVYELSAVLIHRGVSAYSGHYIAHVKDPQSGDWYKFNDEDIEKMEGKKLQLGIEEDLTEPSKSQTRKPKCGKGTHCSRNAYMLVYRLQTQEKNHTMVQVPAFLQELVDRDNSKFEEWCVEMAEMRRQSVDKGRAKHEEVKELYQRLPAGAEPYEFVSLEWLQKWLDESTPTKPIDNNACLCSHDKLHPDKISIMKRISEYAADIFYSRYGGGPRLTVKALCKDCVVERCRILRLKNQLNEDYKTVNNLLKATMKGSDGFWVGKSSLRSWRQLALEQLDEQDGEAEQSNGKINGSPFSKDESKEEKKEEEEELNFNEDILCPHGELSISENERRLVSQEAWSKLQQYFPKAPEFPSYKECCSQCKILEREGEENEALHKMIAKEQKTSLPNLFQDKNRPCLSNWPEDTDALYIVSHFFLDEWRKFVRKPARSTPVSSVGNAALLCPHGGLMFTFPSLTKEDSKLIALIWPSEWQMIQKLFVVDKVIKITRIEVGDVNPSQTQYISEPNLCPDCREGLLCQQQKDLREYTQATIYVHKVVDNKKVMKDSAPELNVSSSETEEDKEEAKPDGEKDPDFNQSNGGTKRQKTSQQGYVAYQKQVIRRSTRHRKVRGEKALLVSANQTLKELKIQIMHAFSVAPFDQNLSIDGKILNDDCATLGTLGVIPESVILLKADEPIADYAAMDDVMQVCMPEEGFKGTGLLGH |
| Enzyme Length | 1036 |
| Uniprot Accession Number | Q76LT8 |
| Absorption | |
| Active Site | ACT_SITE 98; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10093; ACT_SITE 353; /note=Proton acceptor; /evidence=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:14535949}; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme Function | FUNCTION: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins. May be involved in the regulation of NF-kappa-B activation by TNF receptor superfamily via its interactions with RELA and TRAF2. May also play a regulatory role at postsynaptic sites. {ECO:0000269|PubMed:14535949}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (2); Domain (5); Modified residue (4); Region (2) |
| Keywords | Acetylation;Cytoplasm;Hydrolase;Nucleus;Phosphoprotein;Protease;Reference proteome;Repeat;Thiol protease;Ubl conjugation pathway |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=In neuronal cells, it localizes to dendrites, as well as somas. {ECO:0000269|PubMed:14535949}. |
| Modified Residue | MOD_RES 887; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 888; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 889; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 957; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q86UV5 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 118,787 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |