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Protein Page:
USP2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
USP2 Hydrolase that deubiquitinates polyubiquitinated target proteins such as MDM2, MDM4 and CCND1. Isoform 1 and isoform 4 possess 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. Homooligomer. Found in trimeric complex with MDM2 and MDM4 and UPB2. 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. Down-regulated by cisplatin. Expressed in mesangial cells of the kidney and in different types of glomerulonephritides. Cleavage is inhibited by ubiquitin in a dosage- dependent manner. Cleavage is blocked by ubiquitin aldehyde. Belongs to the peptidase C19 family. USP2 subfamily. 4 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 3.1.2.15; Ubiquitin-specific protease; Protease; EC 3.4.19.12
Cellular Component: centrosome; perinuclear region of cytoplasm; cell cortex; nucleus
Molecular Function: ubiquitin thiolesterase activity; identical protein binding; cyclin binding; protein binding; ubiquitin protein ligase binding; metal ion binding; cysteine-type endopeptidase activity; ubiquitin-specific protease activity
Biological Process: ubiquitin-dependent protein catabolic process; negative regulation of skeletal muscle development; muscle development; protein deubiquitination; protein stabilization; negative regulation of transcription from RNA polymerase II promoter; positive regulation of skeletal muscle development; cell cycle; positive regulation of mitotic cell cycle
Reference #:  O75604 (UniProtKB)
Alt. Names/Synonyms: 41 kDa ubiquitin-specific protease; Deubiquitinating enzyme 2; Ubiquitin carboxyl-terminal hydrolase 2; ubiquitin specific peptidase 2; ubiquitin specific protease 12; ubiquitin specific protease 2; ubiquitin specific protease 9; Ubiquitin thioesterase 2; Ubiquitin-specific-processing protease 2; UBP2; UBP41; USP2; USP9
Gene Symbols: USP2
Molecular weight: 68,072 Da
Basal Isoelectric point: 9.15  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

USP2

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 1 - gap
0 4 - gap
0 4 - gap
0 1 - gap
0 1 R160 LRTSDSYRIDPRNLG
0 1 Y300-p DYCLQRLyMRDLHHG
0 1 S490 KRCIKKFSIQRFPKI
0 1 K514 ESRIRTSKLTTFVNF
0 1 Y596-p SDAYLLFyELASPPS
  USP2 iso4  
S34-p PRSPLSPsLLLstFV
S38-p LSPsLLLstFVGLLL
T39-p SPsLLLstFVGLLLN
- gap
- gap
Y91 DYCLQRLYMRDLHHG
S281 KRCIKKFSIQRFPKI
K305 ESRIRTSKLTTFVNF
Y387 SDAYLLFYELASPPS
  mouse

 
- gap
- gap
- gap
R161-m1 LRTSDGYrTSEGFrI
R167-m1 YrTSEGFrIDPGNLG
Y308 DYCLQRLYMRDLGHT
S498-p KRCIKKFsVQRFPKI
K522-ub ESRIRTSkLTTFVNF
Y604 SDAYLLFYELASPPS
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