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Q8C6M1 (UBP20_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
VHL-interacting deubiquitinating enzyme 2
Gene names
Name:Usp20
Synonyms:Kiaa1003, Vdu2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length916 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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.

Sequence caution

The sequence BAD32361.1 differs from that shown. Reason: Erroneous initiation.

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 – 916916Ubiquitin carboxyl-terminal hydrolase 20
PRO_0000390418

Regions

Domain145 – 687543USP
Domain689 – 78294DUSP 1
Domain791 – 894104DUSP 2
Zinc finger28 – 9265UBP-type

Sites

Active site1541Nucleophile By similarity
Active site6451Proton acceptor By similarity

Amino acid modifications

Modified residue1321Phosphoserine Ref.8
Modified residue1341Phosphoserine Ref.8
Modified residue2591Phosphothreonine By similarity
Modified residue3691Phosphoserine Ref.7
Modified residue3781Phosphothreonine Ref.8
Modified residue4151Phosphoserine By similarity

Experimental info

Sequence conflict1171H → T in AAN15803. Ref.1
Sequence conflict3801E → D in AAN15803. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8C6M1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: E104BD489E7ED49F

FASTA916102,140
        10         20         30         40         50         60 
MGDARDLCPH LDCIGEVTKE DLLLKSKGTC QSCGVAGPNL WACLQVTCPY VGCGESFADH 

        70         80         90        100        110        120 
SSIHAQVKKH NLTVNLTTFR VWCYACEREV FLEQRLAVHL ASSSARLSEQ DSPPPSHPLK 

       130        140        150        160        170        180 
AVPIAVADEG ESESEDDDLK PRGLTGMKNL GNSCYMNAAL QALSNCPPLT QFFLECGGLV 

       190        200        210        220        230        240 
RTDKKPALCK SYQKLISEVW HKKRPSYVVP TSLSHGIKLV NPMFRGYAQQ DTQEFLRCLM 

       250        260        270        280        290        300 
DQLHEELKEP MVAAVAALTD ARDSDSSDTD ERRDGDRSPS EDEFLSCDSS SDRGEGDGQG 

       310        320        330        340        350        360 
RGGGSSKAEM ELLISDEAGR AISEKERMKD RKFSWGQQRT NSEQVDEDAD VDTAMASLDE 

       370        380        390        400        410        420 
QSREAQPPSP RSTSPCQTPE PDNEAHIRSS SRPCSPVHHH HEGHSKLSSS PPRASPVRMG 

       430        440        450        460        470        480 
PSYVLKKAQV PSTGGRRRKE QSYRSVISDV FNGSVLSLVQ CLTCDRVSTT VETFQDLSLP 

       490        500        510        520        530        540 
IPGKEDLAKL HSAIYQNVPA KPGACGDSYS SQGWLAFIVE YIRRFVVSCT PSWFWGPVVT 

       550        560        570        580        590        600 
LEDCLAAFFA ADELKGDNMY SCERCKKLRN GVKYCKVLCL PEILCVHLKR FRHEVMYSFK 

       610        620        630        640        650        660 
VSSHVSFPLE GLDLRPFLAK ECTSQVTTYD LLSVICHHGT AGSGHYIAYC QNVINGQWYE 

       670        680        690        700        710        720 
FDDQYVTEVH ETVVQNVEAY VLFYRKSSEE AMRERQQVVS LAAMREPSLL RFYVSREWLN 

       730        740        750        760        770        780 
KFNTFAEPGP ITNHTFLCSH GGIPPNKYHY IDDLVVILPQ SVWEHLYSRF GGGPAVNHLY 

       790        800        810        820        830        840 
VCSICQVEIE ALAKRRRVEI DTFIKLNKAF QAEESPAVIY CISMHWFREW EAFVKGKDSE 

       850        860        870        880        890        900 
PPGPIDNSRI AQVKGSGHIQ LKQGADCGQI SEETWTYLSS LYGGGPEIAI RQSVAQLPDP 

       910 
ESLHGEQKIE AETRAL 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a deubiquitinating enzyme subfamily as substrates of the von Hippel-Lindau tumor suppressor."
Li Z., Wang D., Na X., Schoen S.R., Messing E.M., Wu G.
Biochem. Biophys. Res. Commun. 294:700-709(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Fetal brain.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Medulla oblongata and Ovary.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[7]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[8]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-134 AND THR-378, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF449715 mRNA. Translation: AAN15803.1.
AK173083 mRNA. Translation: BAD32361.1. Different initiation.
AK054279 mRNA. Translation: BAC35715.1.
AK163663 mRNA. Translation: BAE37447.1.
AL844546 Genomic DNA. Translation: CAM18433.1.
CH466542 Genomic DNA. Translation: EDL08500.1.
BC079674 mRNA. Translation: AAH79674.1.
CCDSCCDS15893.1.
RefSeqNP_083122.1. NM_028846.5.
XP_006498455.1. XM_006498392.1.
UniGeneMm.346654.

3D structure databases

ProteinModelPortalQ8C6M1.
SMRQ8C6M1. Positions 5-99, 143-247, 437-688.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC19.025.

PTM databases

PhosphoSiteQ8C6M1.

Proteomic databases

MaxQBQ8C6M1.
PaxDbQ8C6M1.
PRIDEQ8C6M1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000102849; ENSMUSP00000099913; ENSMUSG00000026854.
ENSMUST00000170476; ENSMUSP00000127388; ENSMUSG00000026854.
GeneID74270.
KEGGmmu:74270.
UCSCuc008jde.2. mouse.

Organism-specific databases

CTD10868.
MGIMGI:1921520. Usp20.
RougeSearch...

Phylogenomic databases

eggNOGCOG5560.
GeneTreeENSGT00750000117701.
HOGENOMHOG000286031.
HOVERGENHBG054196.
InParanoidQ8C6M1.
KOK11848.
OMAADYGQIS.
OrthoDBEOG7CRTP2.
PhylomeDBQ8C6M1.
TreeFamTF352179.

Gene expression databases

ArrayExpressQ8C6M1.
BgeeQ8C6M1.
GenevestigatorQ8C6M1.

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...

Other

NextBio340299.
PROQ8C6M1.
SOURCESearch...

Entry information

Entry nameUBP20_MOUSE
AccessionPrimary (citable) accession number: Q8C6M1
Secondary accession number(s): Q69ZT5, Q8CJ72
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 101 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot