ID:UBP33_HUMAN DESCRIPTION: RecName: Full=Ubiquitin carboxyl-terminal hydrolase 33; EC=3.4.19.12; AltName: Full=Deubiquitinating enzyme 33; AltName: Full=Ubiquitin thioesterase 33; AltName: Full=Ubiquitin-specific-processing protease 33; AltName: Full=VHL-interacting deubiquitinating enzyme 1; Short=hVDU1; FUNCTION: Deubiquitinating enzyme involved in various processes such as cellular migration and beta-2 adrenergic receptor/ADRB2 recycling. Involved in cell migration via its interaction with intracellular domain of ROBO1, leading to regulate the Slit signaling. Plays a role in commissural axon guidance cross the ventral midline of the neural tube in a Slit-dependent manner, possibly by mediating the deubiquitination of ROBO1. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination of beta-arrestins (ARRB1 and ARRB2) and beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta- arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. CATALYTIC ACTIVITY: 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). SUBUNIT: Interacts with VHL, leading to its ubiquitination and subsequent degradation. Interacts with ARRB1, ARRB2, ADRB2, DIO2 and ROBO1. Interacts with SELENBP1; in a selenium-dependent manner. INTERACTION: Q13228:SELENBP1; NbExp=5; IntAct=EBI-719307, EBI-711619; SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Note=According to PubMed:12865408, it localizes in the endoplasmic reticulum; however the relevance of such result is unclear. TISSUE SPECIFICITY: Widely expressed. DOMAIN: The UBP-type zinc finger binds 3 zinc ions. However, it does not bind ubiquitin, probably because the conserved Arg in position 86 is replaced by a Glu residue. PTM: Ubiquitinated via a VHL-dependent pathway for proteasomal degradation. SIMILARITY: Belongs to the peptidase C19 family. USP20/USP33 subfamily. SIMILARITY: Contains 2 DUSP domains. SIMILARITY: Contains 1 UBP-type zinc finger. SEQUENCE CAUTION: Sequence=BAA83049.1; Type=Erroneous initiation;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q8TEY7
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Biological Process: GO:0006508 proteolysis GO:0006511 ubiquitin-dependent protein catabolic process GO:0006897 endocytosis GO:0007411 axon guidance GO:0008277 regulation of G-protein coupled receptor protein signaling pathway GO:0009267 cellular response to starvation GO:0010506 regulation of autophagy GO:0016477 cell migration GO:0016579 protein deubiquitination GO:0032091 negative regulation of protein binding GO:0032092 positive regulation of protein binding GO:0050821 protein stabilization GO:0051298 centrosome duplication GO:0070536 protein K63-linked deubiquitination GO:0071108 protein K48-linked deubiquitination
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Sequence and Links to Tools and Databases 
Common Gene Haplotype Alleles 
