Q2KHV7 · UBP2_BOVIN
- ProteinUbiquitin carboxyl-terminal hydrolase 2
- GeneUSP2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids606 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
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 BMAL1.
Catalytic activity
Activity regulation
Cleavage is inhibited by ubiquitin in a dosage-dependent manner. Cleavage is blocked by ubiquitin aldehyde.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 277 | Nucleophile | ||||
Sequence: C | ||||||
Binding site | 426 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 429 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 477 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 480 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Active site | 558 | Proton acceptor | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | perinuclear region of cytoplasm | |
Molecular Function | cysteine-type deubiquitinase activity | |
Molecular Function | metal ion binding | |
Biological Process | circadian behavior | |
Biological Process | circadian regulation of gene expression | |
Biological Process | entrainment of circadian clock by photoperiod | |
Biological Process | locomotor rhythm | |
Biological Process | muscle organ development | |
Biological Process | negative regulation of transcription by RNA polymerase II | |
Biological Process | positive regulation of mitotic cell cycle | |
Biological Process | protein deubiquitination | |
Biological Process | protein stabilization | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameUbiquitin carboxyl-terminal hydrolase 2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionQ2KHV7
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes in the spermatid head in late-elongating spermatids in the thin area between the outer acrosomal membrane and the plasma membrane.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000395965 | 1-606 | Ubiquitin carboxyl-terminal hydrolase 2 | |||
Sequence: MSQLSSTLKRYTESARFTDAPFTKSSYGTYTPSSYGTNLAASFLEKEKFGFKPSPPTSYLTRPRTYGPPSILDYDRGRPLLRPDVIGGGKRAESQTRGTERPSGSGLSGGSGFSYGVTTSSVSYLPVSARDQGVTLTQKKSNSQSDLARDFSSLQTSDSYRLDSGNLGRSPMLARTRKELCALQGLYQAASRSEYLADYLENYGRKASAPQVPTPTPPSRAPEVLSPTYRPSGRYSLWEKGKGQALVSSRSSSPGRDTMNSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYLRDLSHSSRAHTALMEEFAKLIQTIWTSSPNDVVSPSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRVIARPKSNTENLDHLPDDEKGRQMWRKYLEREDSRIGDLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPITKRGYPEVTLMDCMRLFTKEDVLDGDEKPTCCRCRARKRCIKKFSIQRFPKILVLHLKRFSESRIRTSKLTAFVNFPLRDLDLREFASENTNHAVYNLYAVSNHSGTTMGGHYTAYCRSPVTGEWHTFNDSSVSPMSSSQVRTSDAYLLFYELASPPSRM |
Proteomic databases
Expression
Gene expression databases
Interaction
Subunit
Homooligomer. Found in trimeric complex with MDM2 and MDM4 and USP2. Interacts with CCND1; the interaction is direct and promotes its stabilization by antagonizing ubiquitin-dependent degradation. Interacts (via N-terminus and C-terminus) with MDM2. Interacts with MDM4 and PER1. Interacts with KCNQ1; counteracts the NEDD4L-specific down-regulation of I(Ks) and restores plasma membrane localization of KCNQ1 (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-201 | Necessary for interaction with MDM4 | ||||
Sequence: MSQLSSTLKRYTESARFTDAPFTKSSYGTYTPSSYGTNLAASFLEKEKFGFKPSPPTSYLTRPRTYGPPSILDYDRGRPLLRPDVIGGGKRAESQTRGTERPSGSGLSGGSGFSYGVTTSSVSYLPVSARDQGVTLTQKKSNSQSDLARDFSSLQTSDSYRLDSGNLGRSPMLARTRKELCALQGLYQAASRSEYLADYLE | ||||||
Region | 53-112 | Disordered | ||||
Sequence: PSPPTSYLTRPRTYGPPSILDYDRGRPLLRPDVIGGGKRAESQTRGTERPSGSGLSGGSG | ||||||
Compositional bias | 98-112 | Polar residues | ||||
Sequence: GTERPSGSGLSGGSG | ||||||
Region | 207-228 | Disordered | ||||
Sequence: ASAPQVPTPTPPSRAPEVLSPT | ||||||
Domain | 268-600 | USP | ||||
Sequence: AGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYLRDLSHSSRAHTALMEEFAKLIQTIWTSSPNDVVSPSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRVIARPKSNTENLDHLPDDEKGRQMWRKYLEREDSRIGDLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPITKRGYPEVTLMDCMRLFTKEDVLDGDEKPTCCRCRARKRCIKKFSIQRFPKILVLHLKRFSESRIRTSKLTAFVNFPLRDLDLREFASENTNHAVYNLYAVSNHSGTTMGGHYTAYCRSPVTGEWHTFNDSSVSPMSSSQVRTSDAYLLFYELA | ||||||
Region | 404-504 | Necessary for interaction with MDM4 | ||||
Sequence: YLEREDSRIGDLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPITKRGYPEVTLMDCMRLFTKEDVLDGDEKPTCCRCRARKRCIKKFSIQRFPKILVLHLK |
Sequence similarities
Belongs to the peptidase C19 family. USP2 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length606
- Mass (Da)68,101
- Last updated2006-03-07 v1
- Checksum4713919E8BDEE909
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A3Q1MXE5 | A0A3Q1MXE5_BOVIN | USP2 | 668 | ||
A0A3Q1ME39 | A0A3Q1ME39_BOVIN | USP2 | 416 | ||
A0AAA9TNR1 | A0AAA9TNR1_BOVIN | USP2 | 362 | ||
A0AAA9RVB7 | A0AAA9RVB7_BOVIN | USP2 | 396 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 98-112 | Polar residues | ||||
Sequence: GTERPSGSGLSGGSG |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BC112866 EMBL· GenBank· DDBJ | AAI12867.1 EMBL· GenBank· DDBJ | mRNA |