| IED ID | IndEnz0002009760 |
| Enzyme Type ID | protease009760 |
| Protein Name |
Ubiquitin carboxyl-terminal hydrolase 14 EC 3.4.19.12 Deubiquitinating enzyme 14 Glucose-induced degradation protein 6 Ubiquitin thioesterase 14 Ubiquitin-specific-processing protease 14 |
| Gene Name | UBP14 GID6 YBR058C YBR0515 |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MAEAVLENVNVPAVVSKDECIYCFESPYNEPLALNASPKHSLNICLNCFQATCNRHVPLHIRVTEYACDTIHSNYLTIAKVEKPKQENVEENNNNKKIKLQVIETSEDDTHNTIWSLQRFNGENVPRTVLSKSTDSDISSTALEKIEKILKAKSQDFEDKKNSWVLEISTCPHTENFQIPSKPENTVNLNQCSSCDLTQNLWLCLHCGNIGCGREQIGIDGHSHALDHYRSNNNHPLAIKLGSLSSSTYDLYCYACDDETRFPDNVNLGSALQIYGINIQEKIADEKTLVQLQVEQNENWQFRMVDSSGKEFEKLSASKNYGCGLINLGNSCYLNSVIQSLVNGGVPNWSLDFLGSKFPLDVVYPDNNLKCQWIKLLNAMKCEPELYPNGIKPTTFKKCIGQNHQEFSSNRQQDAMEFLTFLLDLLDKKFFSSSSSGIPNPNDLVRFMMEDRLQCNICGKVKYSYEPTEAIQIPLEENDEPQDMLERIKAYFEGQTIEFKCANCKEKVTANKKPGFKSLPQTLILNPIRIRLQNWIPVKTSNELSLPGLIDRDDMLDVSSYLSQGFDPQTENLLPDEDENRSSFTPNQCSISQLIEMGFTQNASVRALFNTGNQDAESAMNWLFQHMDDPDLNDPFVPPPNVPKKDKREVDEVSLTSMLSMGLNPNLCRKALILNNGDVNRSVEWVFNNMDDDGTFPEPEVPNEEQQQKKDLGYSTAKPYALTAVICHKGNSVHSGHYVVFIRKLVADKWKWVLYNDEKLVAADSIEDMKKNGYIYFYTRC |
| Enzyme Length | 781 |
| Uniprot Accession Number | P38237 |
| Absorption | |
| Active Site | ACT_SITE 332; /note="Nucleophile"; /evidence="ECO:0000305|PubMed:9305625"; ACT_SITE 737; /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:9305625}; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme Function | FUNCTION: Required for the adaptation to the presence of glucose in the growth medium; mediates the degradation of enzymes involved in gluconeogenesis when cells are shifted to glucose-containing medium (PubMed:12686616). Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBP1) (PubMed:12686616). Accelerates proteasomal breakdown of ubiquitinated proteins as it disassembles free ubiquitin chains that would compete with ubiquitinated proteins to bind to the proteasome (PubMed:9305625). {ECO:0000269|PubMed:12686616, ECO:0000269|PubMed:9305625}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (3); Erroneous initiation (2); Metal binding (12); Mutagenesis (1); Zinc finger (1) |
| Keywords | Cytoplasm;Direct protein sequencing;Hydrolase;Metal-binding;Nucleus;Protease;Reference proteome;Repeat;Thiol protease;Ubl conjugation pathway;Zinc;Zinc-finger |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11076031; 11283351; 11805826; 15451116; 16361226; 16429126; 16554755; 16563434; 16897085; 17010312; 19410548; 19489724; 19536198; 19734957; 20074044; 21288874; 21427232; 22952687; 23208446; 24586198; 26503604; 26503781; 27693354; 8982460; 9786928; |
| Motif | |
| Gene Encoded By | |
| Mass | 88,630 |
| Kinetics | |
| Metal Binding | METAL 171; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 173; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 192; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 195; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 204; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 207; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 212; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 224; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 228; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 235; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 253; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 256; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502 |
| Rhea ID | |
| Cross Reference Brenda |