Detail Information for IndEnz0002011083
IED ID IndEnz0002011083
Enzyme Type ID protease011083
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 GK17299
Organism Drosophila willistoni (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 willistoni group willistoni subgroup Drosophila willistoni (Fruit fly)
Enzyme Sequence MPVSLAVCETTTTTTANVVNAALRESLLGGSRSGAAVAGSGSASSLISGAGGAGASAANDDDSSSTATANTNLQNQIVASAKRVLLAKIEYEEVENYNDSVLDNLKTKYVVIKSPTPAAAAAATNNGNSNSAGSKILGANGHDNRQKQQNANGGCSTPTTTTTQTSSSSTSSSSIEHNNNPNELPKPKRVLYQRENIRIGWKQSERKWQIGAGMINVGNTCYLNSTLQALFHIPALANWLNSEQSHLENCNIGGESGGGGGGGGGNNGGFCIICAMAKTLQSTQSNASAIRPYHIYSKLKQICKHMVIGRQEDAHEFLRFLVEAMEKAYLMRYRNYKELDQLVKETTPLNQIFGGYLRSEVRCLSCNHVSITFQHFQDLLLDIRKSDTLDEAFDGYFSRERLEDMGYKCEGCKKKVSATKQFSLQRAPITLCIQLKRFSMIGNKLTKQISFKPRIDLSRFAARSPTAQGQLPLTYRLVSLVTHLGVSQHCGHYTAIGLTESGSYYNFDDSYVRPIAMQSVCSTNSYIMFYELDLNQPLATPANKLNGLRQLSNGHHHHQQQQQQHQQQQQQQPTVVATIASSPMATTRFIGPQLPPGGLNGYAMTTTTTATNNTTNGHSQKTAIQFKPQQNGILTVGSGKFQESGQQKSPLVGTNHKNEAPAVAPNANANANGKSSSNPNTNTTINTNTNNGNSNNNNTNATTANNSNKLNQQQQQYLPMSSSDEEDSDEEKMKRPTTTTPQLPSMPKMDGGGDEKPKTLTLTPTTTPTASTPTVSNPLKRLVPYESASEEEESSSGTPSSSTPTTTTTAAAAAASSPMQATAAATLPPPPTPTNARKRSLPDHHHHHPHHHVMVNGHGKSPKPASMPPATNFNSSSSKQKTDAIDEIFKSLNNFNKKRINNKNQKHNEGDEEEDDEETLEKETNNSSRLVSSSTNTSPTTNGWKQSQIVSSSSSNSKNVSTSAAAAAATTSSSTSTSAPPSPKTPPSPAVINSKTGLWKVTRNLDDDDDEEEEDEDDEEHIAPTPPPVVAKTHKNPFSSQQKPTPSPSTEAAPKRQKLFNGTSSSTPHVGNGYQSEPSTPNGGGSGSGSNGCLNELLKQSHRGYGSSSVLSWNGKQTELDKEPFELVCAKRIAVDHGDHDDGGGGDDGGGVGVVTTTTTTTTTTKNTTKTLTADAQEQRQRDLDDDEENEMDRGRQRKVKTATANGKSSGNSNNTTPGYNPFQEYESQKRWHNKSSNGPPRFYTQHASSSYRSNFHQRNKFKCNRGGNGGGGSGGISKFDHRHGLQRHLAAGGGFPRRPNANQQQQQQQS
Enzyme Length 1311
Uniprot Accession Number B4MLR8
Absorption
Active Site ACT_SITE 221; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 492; /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 (15); Domain (1); Modified residue (9); Region (5)
Keywords Hydrolase;Nucleus;Phosphoprotein;Protease;Thiol protease;Ubl conjugation pathway
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
Modified Residue MOD_RES 581; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 767; /note=Phosphothreonine; /evidence=ECO:0000250; MOD_RES 787; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 789; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 982; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 985; /note=Phosphothreonine; /evidence=ECO:0000250; MOD_RES 988; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 1047; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 1050; /note=Phosphothreonine; /evidence=ECO:0000250
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 141,002
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda