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A5PN09

- UBP20_DANRE

UniProt

A5PN09 - UBP20_DANRE

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Protein
Ubiquitin carboxyl-terminal hydrolase 20
Gene
usp20, dkey-125i20.3
Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

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 activityi

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).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei157 – 1571Nucleophile By similarity
Active sitei643 – 6431Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri28 – 9265UBP-type
Add
BLAST

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: UniProtKB
  2. ubiquitin thiolesterase activity Source: UniProtKB
  3. ubiquitin-specific protease activity Source: InterPro
  4. zinc ion binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. endocytosis Source: UniProtKB-KW
  2. protein K48-linked deubiquitination Source: UniProtKB
  3. protein K63-linked deubiquitination Source: UniProtKB
  4. protein deubiquitination Source: UniProtKB
  5. regulation of G-protein coupled receptor protein signaling pathway Source: UniProtKB
  6. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Endocytosis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:usp20
ORF Names:dkey-125i20.3
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
ProteomesiUP000000437: Unplaced

Organism-specific databases

ZFINiZDB-GENE-040426-1219. usp20.

Subcellular locationi

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. perinuclear region of cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 911911Ubiquitin carboxyl-terminal hydrolase 20
PRO_0000390420Add
BLAST

Expressioni

Gene expression databases

BgeeiA5PN09.

Structurei

3D structure databases

ProteinModelPortaliA5PN09.
SMRiA5PN09. Positions 8-95.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini148 – 685538USP
Add
BLAST
Domaini687 – 78094DUSP 1
Add
BLAST
Domaini789 – 891103DUSP 2
Add
BLAST

Domaini

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 similaritiesi

Contains 2 DUSP domains.
Contains 1 USP domain.

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5560.
HOGENOMiHOG000286031.
HOVERGENiHBG054196.
KOiK11848.
PhylomeDBiA5PN09.

Family and domain databases

Gene3Di3.30.2230.10. 2 hits.
3.30.40.10. 1 hit.
InterProiIPR006615. 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]
PfamiPF06337. DUSP. 2 hits.
PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
SMARTiSM00695. DUSP. 2 hits.
[Graphical view]
SUPFAMiSSF143791. SSF143791. 2 hits.
PROSITEiPS51283. 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]

Sequencei

Sequence statusi: Complete.

A5PN09-1 [UniParc]FASTAAdd to Basket

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MTDSGDLCPH LDSIGEVTKE ELIQKSKGTC QSCGVGGPNL WACLQCDCPY    50
VGCGESYSDH STIHAQAKKH NLTVNLTTFR VWCYVCEREV FLEPKPVTPV 100
SSAHRCKPHD QDPVSQTTCY PLKAVPIAVA DEEGSESEED ELKPRGLTGM 150
KNIGNSCYMN AALQALSNCP PLTQFFQDCS GLVRTDKKPA LCKSYQKLIS 200
ELWHKKRPSY VVPTTLFHGI KLVNPMFRGY AQQDTQEFLR CLMDQLHEEL 250
KEPLFDCSGG ISEVEPDLSL DSCNLVDGDR SPSEDEFLSC DSGSGSERGD 300
GERAGGEAEL LIQDECVAVR GTGGISEKER LKERRGEERT REMDEDADVD 350
TAAQDGQAER ETETATPATA VPAPGNTEPD NEASMHCPSS RPCSPAHSVQ 400
ELHSRLSSNP PRSSPLRTGP TYTFKKAQML LSTKKKKQSR FRSVISDIFD 450
GSILSLVQCL TCDRVSTTVE TFQDLSLPIP GKEDLAKLHS SIHQSAPVKA 500
GVCTDGYAAQ GWISYIMDSI RRFVVSCIPS WFWGPMVTLE DCLAAFFAAD 550
ELKGDNMYSC ERCKKLRNGV KYCKVLRLPE ILCIHLKRFR HEVMYSFKIN 600
SHVSFPLEGL DLKPFLAKES PSQITTYDLL SVICHHGTAG SGHYIAYCQN 650
VINGQWYEFD DQYVTEVHET VVQNAEAYVL FYRKSSEESV RERQRVVALA 700
NLKEPSLLQF YISREWLNKF NTFTEPGPIT NHTFLCQHGG IPPTKYHYVD 750
DLVVILPQNV WEYLYNRFGG GPAVNHLYVC AICQVEIETL AKRRKLEIDT 800
FIKLNKEFQA EEAPTVILCI SMQWFREWEN FVKGKDNEPP GPIDNSKIAV 850
MKGGHIQLKQ GADYGQISEE TWQYLLSIYG GGPEIAVRQT ISPPDTDTHG 900
ERKIEAETRA L 911
Length:911
Mass (Da):101,984
Last modified:July 10, 2007 - v1
Checksum:iEB98B978FAE7FA4D
GO

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti115 – 1151S → L in CAN88765. 1 Publication
Sequence conflicti115 – 1151S → L in CAN88088. 1 Publication
Sequence conflicti429 – 4291M → I in CAN88765. 1 Publication
Sequence conflicti429 – 4291M → I in CAN88088. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX927184 Genomic DNA. Translation: CAN88489.1.
BX005029, CR382323 Genomic DNA. Translation: CAN88088.1.
CR382323, BX005029 Genomic DNA. Translation: CAN88765.1. Sequence problems.
RefSeqiNP_957281.2. NM_200987.2.
UniGeneiDr.161818.

Genome annotation databases

GeneIDi393962.
KEGGidre:393962.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX927184 Genomic DNA. Translation: CAN88489.1 .
BX005029 , CR382323 Genomic DNA. Translation: CAN88088.1 .
CR382323 , BX005029 Genomic DNA. Translation: CAN88765.1 . Sequence problems.
RefSeqi NP_957281.2. NM_200987.2.
UniGenei Dr.161818.

3D structure databases

ProteinModelPortali A5PN09.
SMRi A5PN09. Positions 8-95.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 393962.
KEGGi dre:393962.

Organism-specific databases

CTDi 10868.
ZFINi ZDB-GENE-040426-1219. usp20.

Phylogenomic databases

eggNOGi COG5560.
HOGENOMi HOG000286031.
HOVERGENi HBG054196.
KOi K11848.
PhylomeDBi A5PN09.

Miscellaneous databases

NextBioi 20814933.
PROi A5PN09.

Gene expression databases

Bgeei A5PN09.

Family and domain databases

Gene3Di 3.30.2230.10. 2 hits.
3.30.40.10. 1 hit.
InterProi IPR006615. 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 ]
Pfami PF06337. DUSP. 2 hits.
PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view ]
SMARTi SM00695. DUSP. 2 hits.
[Graphical view ]
SUPFAMi SSF143791. SSF143791. 2 hits.
PROSITEi PS51283. 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 ]
ProtoNeti Search...

Publicationsi

  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.
    , 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.

Entry informationi

Entry nameiUBP20_DANRE
AccessioniPrimary (citable) accession number: A5PN09
Secondary accession number(s): A5PM59
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi