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A5PN09 (UBP20_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 52. 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
ORF Names:dkey-125i20.3
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length911 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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. 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).

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.

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.

Sequence caution

The sequence CAN88765.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processEndocytosis
Ubl conjugation pathway
   Cellular componentCytoplasm
Cytoskeleton
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Protease
Thiol protease
   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 – 911911Ubiquitin carboxyl-terminal hydrolase 20
PRO_0000390420

Regions

Domain148 – 685538USP
Domain687 – 78094DUSP 1
Domain789 – 891103DUSP 2
Zinc finger28 – 9265UBP-type

Sites

Active site1571Nucleophile By similarity
Active site6431Proton acceptor By similarity

Experimental info

Sequence conflict1151S → L in CAN88765. Ref.1
Sequence conflict1151S → L in CAN88088. Ref.1
Sequence conflict4291M → I in CAN88765. Ref.1
Sequence conflict4291M → I in CAN88088. Ref.1

Sequences

Sequence LengthMass (Da)Tools
A5PN09 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: EB98B978FAE7FA4D

FASTA911101,984
        10         20         30         40         50         60 
MTDSGDLCPH LDSIGEVTKE ELIQKSKGTC QSCGVGGPNL WACLQCDCPY VGCGESYSDH 

        70         80         90        100        110        120 
STIHAQAKKH NLTVNLTTFR VWCYVCEREV FLEPKPVTPV SSAHRCKPHD QDPVSQTTCY 

       130        140        150        160        170        180 
PLKAVPIAVA DEEGSESEED ELKPRGLTGM KNIGNSCYMN AALQALSNCP PLTQFFQDCS 

       190        200        210        220        230        240 
GLVRTDKKPA LCKSYQKLIS ELWHKKRPSY VVPTTLFHGI KLVNPMFRGY AQQDTQEFLR 

       250        260        270        280        290        300 
CLMDQLHEEL KEPLFDCSGG ISEVEPDLSL DSCNLVDGDR SPSEDEFLSC DSGSGSERGD 

       310        320        330        340        350        360 
GERAGGEAEL LIQDECVAVR GTGGISEKER LKERRGEERT REMDEDADVD TAAQDGQAER 

       370        380        390        400        410        420 
ETETATPATA VPAPGNTEPD NEASMHCPSS RPCSPAHSVQ ELHSRLSSNP PRSSPLRTGP 

       430        440        450        460        470        480 
TYTFKKAQML LSTKKKKQSR FRSVISDIFD GSILSLVQCL TCDRVSTTVE TFQDLSLPIP 

       490        500        510        520        530        540 
GKEDLAKLHS SIHQSAPVKA GVCTDGYAAQ GWISYIMDSI RRFVVSCIPS WFWGPMVTLE 

       550        560        570        580        590        600 
DCLAAFFAAD ELKGDNMYSC ERCKKLRNGV KYCKVLRLPE ILCIHLKRFR HEVMYSFKIN 

       610        620        630        640        650        660 
SHVSFPLEGL DLKPFLAKES PSQITTYDLL SVICHHGTAG SGHYIAYCQN VINGQWYEFD 

       670        680        690        700        710        720 
DQYVTEVHET VVQNAEAYVL FYRKSSEESV RERQRVVALA NLKEPSLLQF YISREWLNKF 

       730        740        750        760        770        780 
NTFTEPGPIT NHTFLCQHGG IPPTKYHYVD DLVVILPQNV WEYLYNRFGG GPAVNHLYVC 

       790        800        810        820        830        840 
AICQVEIETL AKRRKLEIDT FIKLNKEFQA EEAPTVILCI SMQWFREWEN FVKGKDNEPP 

       850        860        870        880        890        900 
GPIDNSKIAV MKGGHIQLKQ GADYGQISEE TWQYLLSIYG GGPEIAVRQT ISPPDTDTHG 

       910 
ERKIEAETRA L 

« Hide

References

[1]"The zebrafish reference genome sequence and its relationship to the human genome."
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J. expand/collapse author list , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tuebingen.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX927184 Genomic DNA. Translation: CAN88489.1.
BX005029, CR382323 Genomic DNA. Translation: CAN88088.1.
CR382323, BX005029 Genomic DNA. Translation: CAN88765.1. Sequence problems.
RefSeqNP_957281.2. NM_200987.2.
UniGeneDr.161818.

3D structure databases

ProteinModelPortalA5PN09.
SMRA5PN09. Positions 8-95.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID393962.
KEGGdre:393962.

Organism-specific databases

CTD10868.
ZFINZDB-GENE-040426-1219. usp20.

Phylogenomic databases

eggNOGCOG5560.
HOGENOMHOG000286031.
HOVERGENHBG054196.
KOK11848.
PhylomeDBA5PN09.

Gene expression databases

BgeeA5PN09.

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. 2 hits.
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...

Other

NextBio20814933.
PROA5PN09.

Entry information

Entry nameUBP20_DANRE
AccessionPrimary (citable) accession number: A5PN09
Secondary accession number(s): A5PM59
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: July 10, 2007
Last modified: April 16, 2014
This is version 52 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