| IED ID | IndEnz0002011761 |
| Enzyme Type ID | protease011761 |
| Protein Name |
Ubiquitin carboxyl-terminal hydrolase 2 EC 3.4.19.12 41 kDa ubiquitin-specific protease Deubiquitinating enzyme 2 Ubiquitin thioesterase 2 Ubiquitin-specific-processing protease 2 |
| Gene Name | USP2 UBP41 |
| Organism | Bos taurus (Bovine) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine) |
| Enzyme Sequence | MSQLSSTLKRYTESARFTDAPFTKSSYGTYTPSSYGTNLAASFLEKEKFGFKPSPPTSYLTRPRTYGPPSILDYDRGRPLLRPDVIGGGKRAESQTRGTERPSGSGLSGGSGFSYGVTTSSVSYLPVSARDQGVTLTQKKSNSQSDLARDFSSLQTSDSYRLDSGNLGRSPMLARTRKELCALQGLYQAASRSEYLADYLENYGRKASAPQVPTPTPPSRAPEVLSPTYRPSGRYSLWEKGKGQALVSSRSSSPGRDTMNSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYLRDLSHSSRAHTALMEEFAKLIQTIWTSSPNDVVSPSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRVIARPKSNTENLDHLPDDEKGRQMWRKYLEREDSRIGDLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPITKRGYPEVTLMDCMRLFTKEDVLDGDEKPTCCRCRARKRCIKKFSIQRFPKILVLHLKRFSESRIRTSKLTAFVNFPLRDLDLREFASENTNHAVYNLYAVSNHSGTTMGGHYTAYCRSPVTGEWHTFNDSSVSPMSSSQVRTSDAYLLFYELASPPSRM |
| Enzyme Length | 606 |
| Uniprot Accession Number | Q2KHV7 |
| Absorption | |
| Active Site | ACT_SITE 277; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 558; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093" |
| Activity Regulation | ACTIVITY REGULATION: Cleavage is inhibited by ubiquitin in a dosage-dependent manner. Cleavage is blocked by ubiquitin aldehyde. {ECO:0000250|UniProtKB:O75604, ECO:0000250|UniProtKB:Q5U349}. |
| 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 such as MDM2, MDM4 and CCND1. Possesses both ubiquitin-specific peptidase and isopeptidase activities. Deubiquitinates MDM2 without reversing MDM2-mediated p53/TP53 ubiquitination and thus indirectly promotes p53/TP53 degradation and limits p53 activity. Has no deubiquitinase activity against p53/TP53. Prevents MDM2-mediated degradation of MDM4. Plays a role in the G1/S cell-cycle progression in normal and cancer cells. Plays a role in the regulation of myogenic differentiation of embryonic muscle cells. Regulates the circadian clock by modulating its intrinsic circadian rhythm and its capacity to respond to external cues. Associates with clock proteins and deubiquitinates core clock component PER1 but does not affect its overall stability. Regulates the nucleocytoplasmic shuttling and nuclear retention of PER1 and its repressive role on the clock transcription factors CLOCK and ARNTL/BMAL1. {ECO:0000250|UniProtKB:O75604, ECO:0000250|UniProtKB:O88623}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (1); Domain (1); Metal binding (4); Region (4) |
| Keywords | Biological rhythms;Cell cycle;Cytoplasm;Hydrolase;Metal-binding;Myogenesis;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway;Zinc;Zinc-finger |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O88623}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O88623}. Note=Localizes in the spermatid head in late-elongating spermatids in the thin area between the outer acrosomal membrane and the plasma membrane. {ECO:0000250|UniProtKB:Q5U349}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 68,101 |
| Kinetics | |
| Metal Binding | METAL 426; /note=Zinc; /evidence=ECO:0000250|UniProtKB:O75604; METAL 429; /note=Zinc; /evidence=ECO:0000250|UniProtKB:O75604; METAL 477; /note=Zinc; /evidence=ECO:0000250|UniProtKB:O75604; METAL 480; /note=Zinc; /evidence=ECO:0000250|UniProtKB:O75604 |
| Rhea ID | |
| Cross Reference Brenda |