Detail Information for IndEnz0002011022
IED ID IndEnz0002011022
Enzyme Type ID protease011022
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 Usp36 scny GJ13192
Organism Drosophila virilis (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) Drosophila virilis group Drosophila virilis (Fruit fly)
Enzyme Sequence MPVSLAVCETANVVNAALRESLGSGIGGGGGCVAAAASRSSAGSGSGSVAGVDEAKIGDVSGTDNLQSQIVANAKRVLLAKIEYEEVENYHESVLAKLKSKYIVIKPDNNNGAANCNYKTNGKAVGSNGHDNNTVNGGTVNGNRKQTVDSGQSNQNSSANPNELPKPKRVLYPRENIRIGWKQSERKWQVGAGMLNVGNTCYLNSTLQALFHIPALANWLVSETSHVENCNISESCGSGGCIICAMAKTLQTTQSNQSAVRPFLIYTKLRQICKHMVVGRQEDAHEFLRFLVEAMEKAYLMRFRNFKELDQLVKETTPISQIFGGYLRSEVRCLSCNHVSITFQHFQDLLLDIRKADTLEEAFDGYFSRERLEDMGYKCEGCKKKVSATKQFSLERAPITLCIQLKRFSMMGNKLTKQISFKPRIDLSRFAARSPTAAAQPLSYRLVSMVTHLGVSQHCGHYTAIGLTEAGSYYNFDDSYVKPIAMQSVCNTNAYIMFYELDVANSSSSSTINNNSSSSSNNSVAPKLNGLRLSNGAHSPAAATVAVAATATSTSASAVSPRFIGPQLPNGYANSNGHALGGAKTTIQFKTTPQKQLQQQQQQQNGLLMGANKFQESSQSKHSLAGTLHKGEAAPNANTNANANKSSCNNNITSQHQQQHILPISSDEDEDEDDSDDDDDDDDDDVKANTAPQLPSMPKMFEDSESVAQTAKLKPKTPLKSLVPYESASEEEQEQQQQQQQQQLLQTPQQLAANPRKRRSGSDSSESEEEAPPPLPSILRNGHAKTNGSVSNTSNSSHSKAKSASNASSANVNSSKQKTDAIDEIFKSLNNYKNKHRIAADDDEDGDGDGDGHGNEQVQTEQGTKKLNSASSASASKSNGWQSQNGKAPSSPKTPPSPAVIKSKTGIWQITRTNDDDDEEDEEEDDVEADADQEDDDDEVVVVEEPQVSVTPKNPKNPFAASKSAEANATIAGAKRQKLLNGSAKSAATTRPGNGYQSESVANGSAVSELLKQNHRGYGTSVLSWNGKPSELDKESFDLVCAKRIAGHGDTDVHSDVNSSSNNSSNINSNSNSNSNGNGKRKNSTLLAEAREQRKRDAEDEEENEMDRGRQRKVKSASVKSNNSTPGYNPFQEFENQKRWHSNKSGTFPRFYHQNNRPNFQQRNKFKFNRFGGGAKFQQQRALQRHLAAGGGFTRRQQQSTGQQQQQQQQQQQS
Enzyme Length 1214
Uniprot Accession Number B4LG38
Absorption
Active Site ACT_SITE 201; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 461; /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: Required for maintaining multiple types of adult stem cells, including male and female germline, epithelial follicle cell and intestinal stem cells. 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 (H3K4). Controls selective autophagy activation by ubiquitinated proteins. {ECO:0000250|UniProtKB:Q9VRP5}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Compositional bias (14); Domain (1); Modified residue (9); Region (7)
Keywords Hydrolase;Nucleus;Phosphoprotein;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
Modified Residue MOD_RES 553; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 555; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 717; /note=Phosphothreonine; /evidence=ECO:0000250; MOD_RES 727; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 729; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 891; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 894; /note=Phosphothreonine; /evidence=ECO:0000250; MOD_RES 897; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 951; /note=Phosphothreonine; /evidence=ECO:0000250
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 132,000
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda