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Q5R5Z6 (UBP20_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase 20

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 20
Ubiquitin thioesterase 20
Ubiquitin-specific-processing protease 20
Gene names
Name:USP20
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length913 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Deubiquitinating enzyme involved in beta-2 adrenergic receptor (ADRB2) recycling. 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. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains By similarity.

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 structure

Interacts with VHL, leading to its ubiquitination and subsequent degradation. Interacts with CCP110, DIO2 and HIF1A By similarity.

Subcellular location

Cytoplasmperinuclear region By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity.

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.

Post-translational modification

Ubiquitinated via a VHL-dependent pathway for proteasomal degradation By similarity.

Sequence similarities

Belongs to the peptidase C19 family. USP20/USP33 subfamily.

Contains 2 DUSP domains.

Contains 1 UBP-type zinc finger.

Contains 1 USP domain.

Ontologies

Keywords
   Biological processEndocytosis
Ubl conjugation pathway
   Cellular componentCytoplasm
Cytoskeleton
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Protease
Thiol protease
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processendocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

protein K48-linked deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein K63-linked deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of G-protein coupled receptor protein signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcentrosome

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncysteine-type endopeptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin thiolesterase activity

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin-specific protease activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 913913Ubiquitin carboxyl-terminal hydrolase 20
PRO_0000390419

Regions

Domain144 – 684541USP
Domain686 – 77994DUSP 1
Domain788 – 891104DUSP 2
Zinc finger28 – 9265UBP-type

Sites

Active site1531Nucleophile By similarity
Active site6421Proton acceptor By similarity

Amino acid modifications

Modified residue1311Phosphoserine By similarity
Modified residue1331Phosphoserine By similarity
Modified residue2571Phosphothreonine By similarity
Modified residue3671Phosphoserine By similarity
Modified residue3761Phosphothreonine By similarity
Modified residue4121Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5R5Z6 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 54CA311FD1D3E626

FASTA913101,851
        10         20         30         40         50         60 
MGDSRDLCPH LDSIGEVTKE DLLLKSMGTC QSCGVTGPNL WACLQVACPY VGCGESFADH 

        70         80         90        100        110        120 
STIHAQAKKH NLTVNLTTFR LWCYACEKEV FLEQRLAAPL LGSSKFSEQD SPPPSHPLKA 

       130        140        150        160        170        180 
VPIAVADEGE SESEDDDLKP RGLTGMKNLG NSCYMNAALQ ALSNCPPLTQ FFLECGGLVR 

       190        200        210        220        230        240 
TDKKPALCKS YQKLVSEVWH KKRPSYVVPT SLSHGIKLVN PMFRGYAQQD TQEFLRCLMD 

       250        260        270        280        290        300 
QLHEELKEPV VATVALTEAR DSDSSDTDEK REGDRSPSED EFLSCDSSSD RGEGDGQGRG 

       310        320        330        340        350        360 
GGSSQAETEL LIPDEASRAI SEKERMKDRK FSWGQQRTNS EQVDEDADVD TTMAALDDQP 

       370        380        390        400        410        420 
AEAQPPSPRS SSPCRTPEPD NDAHLCSSSR PCSPVHHHEG HAKLSSSPPR ASPVRMAPSY 

       430        440        450        460        470        480 
VLKKAQVLSA GSRRRKEQRY RSVISDIFDG SILSLVQCLT CDRVSATVET FQDLSLPIPG 

       490        500        510        520        530        540 
KEDLAKLHSA IYQNVPAKPG TCGDSYAAQG WLAFIVEYIR RFVVSCTPSW FWGPVVTLED 

       550        560        570        580        590        600 
CLAAFFAADE LKGDNMYSCE RCKKLRNGVK YCKVLRLPEI LCIHLKRFRH EVMYSFKINS 

       610        620        630        640        650        660 
HVSFPLEGLD LRPFLAKECT SQITTYDLLS VICHHGTAGS GHYIAYCQNV INGQWYEFDD 

       670        680        690        700        710        720 
QYVTEVHETV VQNAEGYVLF YRKSSEEAVR ERQQVVSLAA MREPSLLRFY VSREWLNKFN 

       730        740        750        760        770        780 
TFAEPGPITN QTFLCSHGGI PPHKYHYIDD LVVILPQNVW EHLYNRFGGG PAVNHLYVCS 

       790        800        810        820        830        840 
ICQVEIEALA KRRRIEIDTF IKLNKAFQAE ESPGIIYCIS MQWFREWEAF VKGKDNEPPG 

       850        860        870        880        890        900 
PIDNSRIAQV KGSGHVQLKQ GADYGQISEE TWTYLNSLYG GGPEIAIRQS VAQPLGPESL 

       910 
HGEQKIEAEA RAV 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR860704 mRNA. Translation: CAH92820.1.
RefSeqNP_001126647.1. NM_001133175.1.

3D structure databases

ProteinModelPortalQ5R5Z6.
SMRQ5R5Z6. Positions 5-97.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100173645.
KEGGpon:100173645.

Organism-specific databases

CTD10868.

Phylogenomic databases

HOGENOMHOG000286031.
HOVERGENHBG054196.
InParanoidQ5R5Z6.
KOK11848.

Family and domain databases

Gene3D3.30.2230.10. 2 hits.
3.30.40.10. 1 hit.
InterProIPR006615. Pept_C19_DUSP.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamPF06337. DUSP. 1 hit.
PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
SMARTSM00695. DUSP. 2 hits.
[Graphical view]
SUPFAMSSF143791. SSF143791. 2 hits.
PROSITEPS51283. DUSP. 2 hits.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameUBP20_PONAB
AccessionPrimary (citable) accession number: Q5R5Z6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries