Detail Information for IndEnz0002013191
IED ID IndEnz0002013191
Enzyme Type ID protease013191
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
Organism Pan troglodytes (Chimpanzee)
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 Pan (chimpanzees) Pan troglodytes (Chimpanzee)
Enzyme Sequence MPLYSVTVKWGKEKFEGVELNTDEPPMVFKAQLFALTGVQPARQKVMVKGGTLKDDDWGNIKIKNGMTLLMMGSADALPEEPSAKTVFVEDMTEEQLASAMELPCGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRASGEMASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQFAEKGEQGQYLQQDANECWIQMMRVLQQKLEAIEDDSVKETDSSSASAATPSKKKSLIDQFFGVEFETTMKCTESEEEEVTKGKENQLQLSCFINQEVKYLFTGLKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYKEKESVNAKVLKDVKFPLMLDMYELCTPELQEKMVSFRSKFKDLEDKKVNQQPNTSDKKSSPQKEVKYEPFSFADDIGSNNCGYYDLQAVLTHQGRSSSSGHYVSWVKRKQDEWIKFDDDKVSIVTPEDILRLSGGGDWHIAYVLLYGPRRVEIMEEESE
Enzyme Length 493
Uniprot Accession Number P60051
Absorption
Active Site ACT_SITE 114; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; 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;
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. Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell. Required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis. 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 (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:P54578, ECO:0000250|UniProtKB:Q9JMA1}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Domain (2); Modified residue (8)
Keywords Acetylation;Cell membrane;Cytoplasm;Hydrolase;Immunity;Innate immunity;Membrane;Phosphoprotein;Protease;Proteasome;Reference proteome;Thiol protease;Ubl conjugation pathway
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Modified Residue MOD_RES 52; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P54578; MOD_RES 143; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P54578; MOD_RES 148; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9JMA1; MOD_RES 235; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P54578; MOD_RES 237; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P54578; MOD_RES 302; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P54578; MOD_RES 432; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P54578; MOD_RES 449; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P54578
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 55,941
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda