Detail Information for IndEnz0002012618
IED ID IndEnz0002012618
Enzyme Type ID protease012618
Protein Name Ubiquitin carboxyl-terminal hydrolase 36
EC 3.4.19.12
Deubiquitinating enzyme 36
Protein scrawny
Ubiquitin thioesterase 36
Ubiquitin-specific-processing protease 36
Gene Name scny Usp36 CG5505
Organism Drosophila melanogaster (Fruit fly)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora melanogaster group melanogaster subgroup Drosophila melanogaster (Fruit fly)
Enzyme Sequence MPVSMAVCETANVVNAALRESLGGNSSAGSSTDQAKSGEDTNGSLQNHIVANAKRILMAKIEYEEVPNYHESVLENLKSKYIVIKPGNPGAINGFSGKNNTGKLVGANGHDNNGARKQAEHPNNQSHHINHHNHQHPTSNPNELPKPKRVLYPRENIRIGWKQSERKWQVGTGMINVGNTCYLNSTLQALLHIPALANWLVSEQAHLADCNVAEPGSGCIICAMTKTLLATQSNQSAVRPFLIYSKLKQICKHMVVGRQEDAHEFLRFLVEAMERAYLMRFRNYKELDQLVKETTPLGQIFGGYLRSEVRCLSCNHVSITFQHFQDLLLDIRKADSLEDAFEGHFSRERLEDMGYKCEGCKKKVSATKQFSLERAPITLCIQLKRFSMIGNKLTKQISFKSRIDLSKYAARSQAAQAQPLTYRLVSMVTHLGASQHCGHYTAIGSTDTGSFYNFDDSYVRPIAMHSVCNTNAYIMFFELDLSQAASPAANRPNGVRLTNGHSTTPVPAATVSSPSPTRFIGPQLPAGGANGYTNGNAQKTAIQFKQQNQQSPQNGLQLGTGKFQDTAKPPLVGAHAKGEATSAPTANGNKSSSPSSNSSSNHKSINQQQYLPISSDDEDIEDEMKPRPTTAQLPSMPNMTENHTEPKAKSPVKIQVKTPVKTPLKSLVPYESASEEEEAPLPNPRKRPSGEDSSESDQESGQTNGHSKTNGSHTNGSASSSVHVNNSKQKTDAIDEIFKSLKKSADSDEDDDEEEPSIQLTNGWHPQKQSQSQSKAPPSPKTPPSPAVIKSKTGIWKVTRNDEVDAIEDDVDVVVVEGSPVKIPTPNKNHRNPFSSSKPSTDSPATPGAKRQKLLNGSALKSHQQPRVGNGYQSNATSNGSTINELLKQSYRGYGSPVLSWNGKPAELEKELLVDAREQRQRDIDDDEENEMDRGRQRKVKSGSAKGNNASNSTPGYNPFQEYEGQKRWNKNGGGGGFPRFYNQNYRQNFQQRNKFKFNRFGGPGSAKFQQQRALQRHLSAGGGFSRRQPSAQQQQQT
Enzyme Length 1038
Uniprot Accession Number Q9VRP5
Absorption
Active Site ACT_SITE 181; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01035, ECO:0000305|PubMed:19039105, ECO:0000305|PubMed:19837371"; ACT_SITE 439; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093, ECO:0000305|PubMed:19837371"
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: Hydrolase that deubiquitinates polyubiquitinated target proteins including imd (PubMed:19837371, PubMed:19039105). Required for preventing the constitutive activation of the imd/NF-kappa-B (Imd) signaling cascade under unchalleneged conditions (PubMed:19837371, PubMed:25027767). Deubiquitinates imd linked 'Lys-63' chains which leads its proteasomal degradation and consequently down-regulation of the Imd signaling cascade (PubMed:19837371). Removal of the activating 'Lys-63'-linked chains is likely to enable their replacement with 'Lys-48'-linked chains which act as 'tags' the for proteosomal degradation of imd (PubMed:19837371). Required for maintaining multiple types of adult stem cells, including male and female germline, epithelial follicle cell and intestinal stem cells (PubMed:19039105). May function as a transcriptional repressor by continually deubiquiting histone H2B at the promoters of genes critical for cellular differentiation, thereby preventing histone H3 'Lys-4' trimethylation (H3K4me3) (PubMed:19039105). Controls selective autophagy activation by ubiquitinated proteins (PubMed:22622177). {ECO:0000269|PubMed:19039105, ECO:0000269|PubMed:19837371, ECO:0000269|PubMed:22622177, ECO:0000269|PubMed:25027767}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Alternative sequence (5); Chain (1); Compositional bias (12); Domain (1); Modified residue (14); Mutagenesis (2); Region (6); Sequence conflict (4)
Keywords Alternative splicing;Cytoplasm;Hydrolase;Nucleus;Phosphoprotein;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:19039105}. Cytoplasm {ECO:0000269|PubMed:19837371}.
Modified Residue MOD_RES 513; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18327897; MOD_RES 515; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18327897; MOD_RES 658; /note=Phosphothreonine; /evidence=ECO:0000269|PubMed:18327897; MOD_RES 662; /note=Phosphothreonine; /evidence=ECO:0000269|PubMed:18327897; MOD_RES 672; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18327897; MOD_RES 674; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18327897; MOD_RES 747; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18327897; MOD_RES 779; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18327897; MOD_RES 782; /note=Phosphothreonine; /evidence=ECO:0000269|PubMed:18327897; MOD_RES 785; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18327897; MOD_RES 819; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18327897; MOD_RES 825; /note=Phosphothreonine; /evidence=ECO:0000269|PubMed:18327897; MOD_RES 843; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18327897; MOD_RES 846; /note=Phosphothreonine; /evidence=ECO:0000269|PubMed:18327897
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10471706; 11102377; 12593803; 12695332; 16107480; 16157870; 18407920; 19026789; 19217892; 20220848; 20371351; 21074052; 21641546; 22253573; 22494833; 22724070; 22884528; 22912810; 22937016; 23071443; 23087835; 23124073; 23173095; 23275879; 23721820; 23899565; 24244183; 24362437; 24380076; 24576427; 24777180; 24949430; 25242144; 25294943; 25294944; 25628309; 26120032; 26431326; 26483546; 26507797; 26551273; 26979755; 27124581; 27507044; 27866148; 28084990; 28441530; 28674274; 29050293; 29146454; 30012668; 31068592; 31722958; 32573431; 32637412; 32656090; 32774336; 33561251; 33988679; 9584098;
Motif
Gene Encoded By
Mass 114,088
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda