| IED ID | IndEnz0002013193 |
| Enzyme Type ID | protease013193 |
| Protein Name |
Ubiquitin carboxyl-terminal hydrolase 14 EC 3.4.19.12 Deubiquitinating enzyme 14 Ubiquitin thioesterase 14 Ubiquitin-specific-processing protease 14 |
| Gene Name | USP14 TGT |
| Organism | Homo sapiens (Human) |
| 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) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MPLYSVTVKWGKEKFEGVELNTDEPPMVFKAQLFALTGVQPARQKVMVKGGTLKDDDWGNIKIKNGMTLLMMGSADALPEEPSAKTVFVEDMTEEQLASAMELPCGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRASGEMASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQFAEKGEQGQYLQQDANECWIQMMRVLQQKLEAIEDDSVKETDSSSASAATPSKKKSLIDQFFGVEFETTMKCTESEEEEVTKGKENQLQLSCFINQEVKYLFTGLKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYKEKESVNAKVLKDVKFPLMLDMYELCTPELQEKMVSFRSKFKDLEDKKVNQQPNTSDKKSSPQKEVKYEPFSFADDIGSNNCGYYDLQAVLTHQGRSSSSGHYVSWVKRKQDEWIKFDDDKVSIVTPEDILRLSGGGDWHIAYVLLYGPRRVEIMEEESEQ |
| Enzyme Length | 494 |
| Uniprot Accession Number | P54578 |
| Absorption | |
| Active Site | ACT_SITE 114; /note="Nucleophile"; /evidence="ECO:0000305|PubMed:16211010"; ACT_SITE 435; /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:16211010}; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme Function | FUNCTION: Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. Ensures the regeneration of ubiquitin at the proteasome (PubMed:18162577, PubMed:28396413). Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell (PubMed:18162577). Required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis (PubMed:19106094). Serves also as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1 (PubMed:19135427). Indispensable for synaptic development and function at neuromuscular junctions (NMJs) (By similarity). Plays a role in the innate immune defense against viruses by stabilizing the viral DNA sensor CGAS and thus inhibiting its autophagic degradation (PubMed:27666593). {ECO:0000250|UniProtKB:Q9JMA1, ECO:0000269|PubMed:18162577, ECO:0000269|PubMed:19106094, ECO:0000269|PubMed:19135427, ECO:0000269|PubMed:27666593, ECO:0000269|PubMed:28396413}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Alternative sequence (2); Beta strand (22); Chain (1); Domain (2); Frameshift (1); Helix (12); Modified residue (8); Turn (3) |
| Keywords | 3D-structure;Acetylation;Alternative splicing;Cell membrane;Cytoplasm;Hydrolase;Immunity;Innate immunity;Membrane;Phosphoprotein;Protease;Proteasome;Reference proteome;Thiol protease;Ubl conjugation pathway |
| Interact With | Q08209 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19106094}. Cell membrane {ECO:0000269|PubMed:19106094}; Peripheral membrane protein {ECO:0000269|PubMed:19106094}. |
| Modified Residue | MOD_RES 52; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 143; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 148; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q9JMA1"; MOD_RES 235; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"; MOD_RES 237; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 302; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 432; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 449; /note="N6-acetyllysine"; /evidence="ECO:0007744|PubMed:19608861" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | Electron microscopy (1); X-ray crystallography (7) |
| Cross Reference PDB | 2AYN; 2AYO; 5GJQ; 6IIK; 6IIL; 6IIM; 6IIN; 6LVS; |
| Mapped Pubmed ID | 11566882; 16465409; 17079671; 17353931; 17553343; 18234856; 18624398; 19490896; 19549727; 19615732; 19726649; 19896943; 20237496; 21627382; 23291607; 23615914; 23702845; 24319254; 24556800; 24811749; 25429837; 26397990; 26496610; 26523394; 26710889; 26712154; 26782643; 26817839; 26938858; 27428775; 27448976; 27542828; 27592452; 27629392; 27813535; 27884201; 28151478; 28364380; 28416611; 28509417; 29581427; 29702194; 29703842; 29995557; 30021169; 30249595; 30254335; 30296012; 30466171; 30487212; 30550885; 30910023; 31653087; 31703099; 31740976; 31970862; 32033748; 32471496; 32632734; 32887472; 33212146; 33360745; 33737492; 34089575; 34948233; 8579355; |
| Motif | |
| Gene Encoded By | |
| Mass | 56,069 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |