Detail Information for IndEnz0002010026
IED ID IndEnz0002010026
Enzyme Type ID protease010026
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 GF23992
Organism Drosophila ananassae (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 ananassae subgroup ananassae species complex Drosophila ananassae (Fruit fly)
Enzyme Sequence MPVSVAVCETTNVVNAALRESLGVGIGSGGASSDDKSAGEDTNSLQNHIVANAKRILMTKIEYEEVPNYQEAVLENLKSKYIVIKPTNPTNGCNLNGNTANTFGNKNNAGKIVGANGHDNNGRKLSDHPNQNHNHANPNGHHANPNELPKPKRVLYPRENIRIGWKQSERKWQVGSGMINAGNTCYLNSTLQALFHIPALANWLVSEQAHMENCNVSESGSFCIICAMAKTLQATQTTQSAVRPFLIYTKLKQICKHMIVGRQEDAHEFLRFLVEAMERAYLMRFRNYKELDQLVKETTPLGQIFGGYLRSEVRCLSCNHVSITFQHFQDLLLDIRKSDSLEEAFEGYFSREKLEDFGYKCEGCKKKVSATKQFRLERAPITLCIQLKRFSMMGNKLTKQITFKPRIDLSKFAARSPAASVQPLIYRLVSMVTHLGVSQHCGHYTAIGSTEAGSYYNFDDSYVRPIAIQSVCNTNAYIMFYELDPLQTSSPAAARANGLRLTNGHGPVPVAVPATVSSPLPSPAKFIGPQLPPGGINGYSNGHGPKTTIQFKPQHQPSHQQNGVQQSAKSPLLSTHVKVEAAAGAAALAASAAPTANGNKSSSNHSNHKSVNQQHYLPISSEDEDSEDEVKARPTVQLPSMPKMDDCMDSGKPKSPVKTPVKTPLKSLVPYESASEEEEVVPLPNPNARKRSSDSSDSEHEPTTSSVQLNGHSKTNGSLSNGSSKSTDAIDEIFKSLKGYQAKKKSADSEDDDDDEDEPNNQLTNGWHPQKQSQSQSRSGPPSPKTPPSPAVIKSKTGIWKVTRDDGDDDEDDDDDDDEVVEEARAVRTPVKNHRNPFASSKTATDSPTTPGAKRQKLLNGSAIKTQQQPRAGNGYQSEATANGGTVNELLKQSHRGYSSSVLSWNGKPAELEKEPFVLVCAKRIAGHGSLDGSGSGSNTDIIDTEIPAAAVNFPSGSCSFSLLADARDQRQRDLADDEENEMDRGRQRKVKSGSAKISNSTPGYNPFMEFENQKRWHKNGGGGGFPRFYQNQNFRQGFQQRNKFKFNRFGGPGSAKFQQQRALQRHLAAGGGFTRRQPTHSAQQQQQQQS
Enzyme Length 1091
Uniprot Accession Number B3M3M6
Absorption
Active Site ACT_SITE 185; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 443; /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 (9); Domain (1); Modified residue (13); Region (5)
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 518; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 522; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 659; /note=Phosphothreonine; /evidence=ECO:0000250; MOD_RES 663; /note=Phosphothreonine; /evidence=ECO:0000250; MOD_RES 673; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 675; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 749; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 783; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 786; /note=Phosphothreonine; /evidence=ECO:0000250; MOD_RES 789; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 829; /note=Phosphothreonine; /evidence=ECO:0000250; MOD_RES 847; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 850; /note=Phosphothreonine; /evidence=ECO:0000250
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 119,512
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda