Q5R5Z6 · UBP20_PONAB

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

  • 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 (UniProtKB | ENZYME | Rhea)

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site8Zn2+ 1 (UniProtKB | ChEBI)
Binding site10Zn2+ 1 (UniProtKB | ChEBI)
Binding site30Zn2+ 2 (UniProtKB | ChEBI)
Binding site33Zn2+ 2 (UniProtKB | ChEBI)
Binding site43Zn2+ 3 (UniProtKB | ChEBI)
Binding site48Zn2+ 3 (UniProtKB | ChEBI)
Binding site53Zn2+ 2 (UniProtKB | ChEBI)
Binding site60Zn2+ 2 (UniProtKB | ChEBI)
Binding site64Zn2+ 3 (UniProtKB | ChEBI)
Binding site70Zn2+ 3 (UniProtKB | ChEBI)
Binding site83Zn2+ 1 (UniProtKB | ChEBI)
Binding site86Zn2+ 1 (UniProtKB | ChEBI)
Active site153Nucleophile
Active site642Proton acceptor

GO annotations

AspectTerm
Cellular Componentcentrosome
Cellular Componentendoplasmic reticulum
Cellular Componentperinuclear region of cytoplasm
Molecular Functioncysteine-type deubiquitinase activity
Molecular Functioncysteine-type endopeptidase activity
Molecular Functionzinc ion binding
Biological Processendocytosis
Biological Processprotein deubiquitination
Biological Processprotein K48-linked deubiquitination
Biological Processprotein K63-linked deubiquitination
Biological Processproteolysis
Biological Processregulation of G protein-coupled receptor signaling pathway

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Ubiquitin carboxyl-terminal hydrolase 20
  • EC number
  • Alternative names
    • Deubiquitinating enzyme 20
    • Ubiquitin thioesterase 20
    • Ubiquitin-specific-processing protease 20

Gene names

    • Name
      USP20

Organism names

Accessions

  • Primary accession
    Q5R5Z6

Proteomes

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00003904191-913Ubiquitin carboxyl-terminal hydrolase 20
Modified residue111Phosphoserine
Modified residue131Phosphoserine
Modified residue133Phosphoserine
Modified residue257Phosphothreonine
Modified residue304Phosphoserine
Modified residue367Phosphoserine
Modified residue376Phosphothreonine
Modified residue407Phosphoserine
Modified residue412Phosphoserine

Post-translational modification

Ubiquitinated via a VHL-dependent pathway for proteasomal degradation.

Keywords

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

Family & Domains

Features

Showing features for zinc finger, domain, region, compositional bias.

TypeIDPosition(s)Description
Zinc finger6-111UBP-type
Domain144-684USP
Region256-414Disordered
Compositional bias261-288Basic and acidic residues
Compositional bias316-334Basic and acidic residues
Compositional bias374-388Polar residues
Domain686-779DUSP 1
Domain788-891DUSP 2

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

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    913
  • Mass (Da)
    101,851
  • Last updated
    2004-12-21 v1
  • Checksum
    54CA311FD1D3E626
MGDSRDLCPHLDSIGEVTKEDLLLKSMGTCQSCGVTGPNLWACLQVACPYVGCGESFADHSTIHAQAKKHNLTVNLTTFRLWCYACEKEVFLEQRLAAPLLGSSKFSEQDSPPPSHPLKAVPIAVADEGESESEDDDLKPRGLTGMKNLGNSCYMNAALQALSNCPPLTQFFLECGGLVRTDKKPALCKSYQKLVSEVWHKKRPSYVVPTSLSHGIKLVNPMFRGYAQQDTQEFLRCLMDQLHEELKEPVVATVALTEARDSDSSDTDEKREGDRSPSEDEFLSCDSSSDRGEGDGQGRGGGSSQAETELLIPDEASRAISEKERMKDRKFSWGQQRTNSEQVDEDADVDTTMAALDDQPAEAQPPSPRSSSPCRTPEPDNDAHLCSSSRPCSPVHHHEGHAKLSSSPPRASPVRMAPSYVLKKAQVLSAGSRRRKEQRYRSVISDIFDGSILSLVQCLTCDRVSATVETFQDLSLPIPGKEDLAKLHSAIYQNVPAKPGTCGDSYAAQGWLAFIVEYIRRFVVSCTPSWFWGPVVTLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLRLPEILCIHLKRFRHEVMYSFKINSHVSFPLEGLDLRPFLAKECTSQITTYDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEVHETVVQNAEGYVLFYRKSSEEAVRERQQVVSLAAMREPSLLRFYVSREWLNKFNTFAEPGPITNQTFLCSHGGIPPHKYHYIDDLVVILPQNVWEHLYNRFGGGPAVNHLYVCSICQVEIEALAKRRRIEIDTFIKLNKAFQAEESPGIIYCISMQWFREWEAFVKGKDNEPPGPIDNSRIAQVKGSGHVQLKQGADYGQISEETWTYLNSLYGGGPEIAIRQSVAQPLGPESLHGEQKIEAEARAV

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias261-288Basic and acidic residues
Compositional bias316-334Basic and acidic residues
Compositional bias374-388Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CR860704
EMBL· GenBank· DDBJ
CAH92820.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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