Q5R5Z6 · UBP20_PONAB
- ProteinUbiquitin carboxyl-terminal hydrolase 20
- GeneUSP20
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids913 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Deubiquitinating enzyme that plays a role in many cellular processes including autophagy, cellular antiviral response or membrane protein biogenesis. Attenuates TLR4-mediated NF-kappa-B signaling by cooperating with beta-arrestin-2/ARRB2 and inhibiting TRAF6 autoubiquitination. Promotes cellular antiviral responses by deconjugating 'Lys-33' and 'Lys-48'-linked ubiquitination of STING1 leading to its stabilization. Plays an essential role in autophagy induction by regulating the ULK1 stability through deubiquitination of ULK1. Acts as a positive regulator for NF-kappa-B activation by TNF-alpha through deubiquitinating 'Lys-48'-linked polyubiquitination of SQSTM1, leading to its increased stability. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination 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, possibly 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. Deubiquitinates HIF1A, leading to stabilize HIF1A and enhance HIF1A-mediated activity. Deubiquitinates MCL1, a pivotal member of the anti-apoptotic Bcl-2 protein family to regulate its stability. Within the endoplasmic reticulum, participates with USP33 in the rescue of post-translationally targeted membrane proteins that are inappropriately ubiquitinated by the cytosolic protein quality control in the cytosol.
Catalytic activity
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 8 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 10 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 30 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 33 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 43 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 48 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 53 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 60 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 64 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 70 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 83 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 86 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Active site | 153 | Nucleophile | ||||
Sequence: C | ||||||
Active site | 642 | Proton acceptor | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | centrosome | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | perinuclear region of cytoplasm | |
Molecular Function | cysteine-type deubiquitinase activity | |
Molecular Function | cysteine-type endopeptidase activity | |
Molecular Function | zinc ion binding | |
Biological Process | endocytosis | |
Biological Process | protein deubiquitination | |
Biological Process | protein K48-linked deubiquitination | |
Biological Process | protein K63-linked deubiquitination | |
Biological Process | proteolysis | |
Biological Process | regulation of G protein-coupled receptor signaling pathway |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameUbiquitin carboxyl-terminal hydrolase 20
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Pongo
Accessions
- Primary accessionQ5R5Z6
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000390419 | 1-913 | Ubiquitin carboxyl-terminal hydrolase 20 | |||
Sequence: MGDSRDLCPHLDSIGEVTKEDLLLKSMGTCQSCGVTGPNLWACLQVACPYVGCGESFADHSTIHAQAKKHNLTVNLTTFRLWCYACEKEVFLEQRLAAPLLGSSKFSEQDSPPPSHPLKAVPIAVADEGESESEDDDLKPRGLTGMKNLGNSCYMNAALQALSNCPPLTQFFLECGGLVRTDKKPALCKSYQKLVSEVWHKKRPSYVVPTSLSHGIKLVNPMFRGYAQQDTQEFLRCLMDQLHEELKEPVVATVALTEARDSDSSDTDEKREGDRSPSEDEFLSCDSSSDRGEGDGQGRGGGSSQAETELLIPDEASRAISEKERMKDRKFSWGQQRTNSEQVDEDADVDTTMAALDDQPAEAQPPSPRSSSPCRTPEPDNDAHLCSSSRPCSPVHHHEGHAKLSSSPPRASPVRMAPSYVLKKAQVLSAGSRRRKEQRYRSVISDIFDGSILSLVQCLTCDRVSATVETFQDLSLPIPGKEDLAKLHSAIYQNVPAKPGTCGDSYAAQGWLAFIVEYIRRFVVSCTPSWFWGPVVTLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLRLPEILCIHLKRFRHEVMYSFKINSHVSFPLEGLDLRPFLAKECTSQITTYDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEVHETVVQNAEGYVLFYRKSSEEAVRERQQVVSLAAMREPSLLRFYVSREWLNKFNTFAEPGPITNQTFLCSHGGIPPHKYHYIDDLVVILPQNVWEHLYNRFGGGPAVNHLYVCSICQVEIEALAKRRRIEIDTFIKLNKAFQAEESPGIIYCISMQWFREWEAFVKGKDNEPPGPIDNSRIAQVKGSGHVQLKQGADYGQISEETWTYLNSLYGGGPEIAIRQSVAQPLGPESLHGEQKIEAEARAV | ||||||
Modified residue | 111 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 131 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 133 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 257 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 304 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 367 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 376 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 407 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 412 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Ubiquitinated via a VHL-dependent pathway for proteasomal degradation.
Keywords
- PTM
Interaction
Subunit
Interacts with VHL, leading to its ubiquitination and subsequent degradation. Interacts with CCP110. Interacts with DIO2. Interacts with HIF1A. Interacts with ADRB2. Interacts with USP18.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for zinc finger, domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 6-111 | UBP-type | ||||
Sequence: DLCPHLDSIGEVTKEDLLLKSMGTCQSCGVTGPNLWACLQVACPYVGCGESFADHSTIHAQAKKHNLTVNLTTFRLWCYACEKEVFLEQRLAAPLLGSSKFSEQDS | ||||||
Domain | 144-684 | USP | ||||
Sequence: TGMKNLGNSCYMNAALQALSNCPPLTQFFLECGGLVRTDKKPALCKSYQKLVSEVWHKKRPSYVVPTSLSHGIKLVNPMFRGYAQQDTQEFLRCLMDQLHEELKEPVVATVALTEARDSDSSDTDEKREGDRSPSEDEFLSCDSSSDRGEGDGQGRGGGSSQAETELLIPDEASRAISEKERMKDRKFSWGQQRTNSEQVDEDADVDTTMAALDDQPAEAQPPSPRSSSPCRTPEPDNDAHLCSSSRPCSPVHHHEGHAKLSSSPPRASPVRMAPSYVLKKAQVLSAGSRRRKEQRYRSVISDIFDGSILSLVQCLTCDRVSATVETFQDLSLPIPGKEDLAKLHSAIYQNVPAKPGTCGDSYAAQGWLAFIVEYIRRFVVSCTPSWFWGPVVTLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLRLPEILCIHLKRFRHEVMYSFKINSHVSFPLEGLDLRPFLAKECTSQITTYDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEVHETVVQNAEGYVLFYRKS | ||||||
Region | 256-414 | Disordered | ||||
Sequence: LTEARDSDSSDTDEKREGDRSPSEDEFLSCDSSSDRGEGDGQGRGGGSSQAETELLIPDEASRAISEKERMKDRKFSWGQQRTNSEQVDEDADVDTTMAALDDQPAEAQPPSPRSSSPCRTPEPDNDAHLCSSSRPCSPVHHHEGHAKLSSSPPRASPV | ||||||
Compositional bias | 261-288 | Basic and acidic residues | ||||
Sequence: DSDSSDTDEKREGDRSPSEDEFLSCDSS | ||||||
Compositional bias | 316-334 | Basic and acidic residues | ||||
Sequence: ASRAISEKERMKDRKFSWG | ||||||
Compositional bias | 374-388 | Polar residues | ||||
Sequence: CRTPEPDNDAHLCSS | ||||||
Domain | 686-779 | DUSP 1 | ||||
Sequence: EEAVRERQQVVSLAAMREPSLLRFYVSREWLNKFNTFAEPGPITNQTFLCSHGGIPPHKYHYIDDLVVILPQNVWEHLYNRFGGGPAVNHLYVC | ||||||
Domain | 788-891 | DUSP 2 | ||||
Sequence: ALAKRRRIEIDTFIKLNKAFQAEESPGIIYCISMQWFREWEAFVKGKDNEPPGPIDNSRIAQVKGSGHVQLKQGADYGQISEETWTYLNSLYGGGPEIAIRQSV |
Domain
The UBP-type zinc finger binds 3 zinc ions. However, it does not bind ubiquitin, probably because the conserved Arg in position 55 is replaced by a Glu residue (By similarity).
Sequence similarities
Belongs to the peptidase C19 family. USP20/USP33 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length913
- Mass (Da)101,851
- Last updated2004-12-21 v1
- Checksum54CA311FD1D3E626
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 261-288 | Basic and acidic residues | ||||
Sequence: DSDSSDTDEKREGDRSPSEDEFLSCDSS | ||||||
Compositional bias | 316-334 | Basic and acidic residues | ||||
Sequence: ASRAISEKERMKDRKFSWG | ||||||
Compositional bias | 374-388 | Polar residues | ||||
Sequence: CRTPEPDNDAHLCSS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CR860704 EMBL· GenBank· DDBJ | CAH92820.1 EMBL· GenBank· DDBJ | mRNA |