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Q8C6M1

- UBP20_MOUSE

UniProt

Q8C6M1 - UBP20_MOUSE

Protein

Ubiquitin carboxyl-terminal hydrolase 20

Gene

Usp20

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    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. 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.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 sitei154 – 1541NucleophilePROSITE-ProRule annotation
    Active sitei645 – 6451Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri28 – 9265UBP-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Endocytosis, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiC19.025.

    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
    VHL-interacting deubiquitinating enzyme 2
    Gene namesi
    Name:Usp20
    Synonyms:Kiaa1003, Vdu2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:1921520. Usp20.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 916916Ubiquitin carboxyl-terminal hydrolase 20PRO_0000390418Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei132 – 1321Phosphoserine1 Publication
    Modified residuei134 – 1341Phosphoserine1 Publication
    Modified residuei259 – 2591PhosphothreonineBy similarity
    Modified residuei369 – 3691Phosphoserine1 Publication
    Modified residuei378 – 3781Phosphothreonine1 Publication
    Modified residuei415 – 4151PhosphoserineBy similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ8C6M1.
    PaxDbiQ8C6M1.
    PRIDEiQ8C6M1.

    PTM databases

    PhosphoSiteiQ8C6M1.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8C6M1.
    BgeeiQ8C6M1.
    GenevestigatoriQ8C6M1.

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliQ8C6M1.
    SMRiQ8C6M1. Positions 5-99, 143-247, 437-688.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini145 – 687543USPAdd
    BLAST
    Domaini689 – 78294DUSP 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini791 – 894104DUSP 2PROSITE-ProRule annotationAdd
    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.By similarity

    Sequence similaritiesi

    Contains 2 DUSP domains.PROSITE-ProRule annotation
    Contains 1 UBP-type zinc finger.PROSITE-ProRule annotation
    Contains 1 USP domain.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri28 – 9265UBP-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5560.
    GeneTreeiENSGT00750000117701.
    HOGENOMiHOG000286031.
    HOVERGENiHBG054196.
    InParanoidiQ8C6M1.
    KOiK11848.
    OMAiADYGQIS.
    OrthoDBiEOG7CRTP2.
    PhylomeDBiQ8C6M1.
    TreeFamiTF352179.

    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. 1 hit.
    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.

    Q8C6M1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGDARDLCPH LDCIGEVTKE DLLLKSKGTC QSCGVAGPNL WACLQVTCPY    50
    VGCGESFADH SSIHAQVKKH NLTVNLTTFR VWCYACEREV FLEQRLAVHL 100
    ASSSARLSEQ DSPPPSHPLK AVPIAVADEG ESESEDDDLK PRGLTGMKNL 150
    GNSCYMNAAL QALSNCPPLT QFFLECGGLV RTDKKPALCK SYQKLISEVW 200
    HKKRPSYVVP TSLSHGIKLV NPMFRGYAQQ DTQEFLRCLM DQLHEELKEP 250
    MVAAVAALTD ARDSDSSDTD ERRDGDRSPS EDEFLSCDSS SDRGEGDGQG 300
    RGGGSSKAEM ELLISDEAGR AISEKERMKD RKFSWGQQRT NSEQVDEDAD 350
    VDTAMASLDE QSREAQPPSP RSTSPCQTPE PDNEAHIRSS SRPCSPVHHH 400
    HEGHSKLSSS PPRASPVRMG PSYVLKKAQV PSTGGRRRKE QSYRSVISDV 450
    FNGSVLSLVQ CLTCDRVSTT VETFQDLSLP IPGKEDLAKL HSAIYQNVPA 500
    KPGACGDSYS SQGWLAFIVE YIRRFVVSCT PSWFWGPVVT LEDCLAAFFA 550
    ADELKGDNMY SCERCKKLRN GVKYCKVLCL PEILCVHLKR FRHEVMYSFK 600
    VSSHVSFPLE GLDLRPFLAK ECTSQVTTYD LLSVICHHGT AGSGHYIAYC 650
    QNVINGQWYE FDDQYVTEVH ETVVQNVEAY VLFYRKSSEE AMRERQQVVS 700
    LAAMREPSLL RFYVSREWLN KFNTFAEPGP ITNHTFLCSH GGIPPNKYHY 750
    IDDLVVILPQ SVWEHLYSRF GGGPAVNHLY VCSICQVEIE ALAKRRRVEI 800
    DTFIKLNKAF QAEESPAVIY CISMHWFREW EAFVKGKDSE PPGPIDNSRI 850
    AQVKGSGHIQ LKQGADCGQI SEETWTYLSS LYGGGPEIAI RQSVAQLPDP 900
    ESLHGEQKIE AETRAL 916
    Length:916
    Mass (Da):102,140
    Last modified:March 1, 2003 - v1
    Checksum:iE104BD489E7ED49F
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti117 – 1171H → T in AAN15803. (PubMed:12056827)Curated
    Sequence conflicti380 – 3801E → D in AAN15803. (PubMed:12056827)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS15893.1.
    RefSeqiNP_083122.1. NM_028846.5.
    XP_006498455.1. XM_006498392.1.
    UniGeneiMm.346654.

    Genome annotation databases

    EnsembliENSMUST00000102849; ENSMUSP00000099913; ENSMUSG00000026854.
    ENSMUST00000170476; ENSMUSP00000127388; ENSMUSG00000026854.
    GeneIDi74270.
    KEGGimmu:74270.
    UCSCiuc008jde.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS15893.1.
    RefSeqi NP_083122.1. NM_028846.5.
    XP_006498455.1. XM_006498392.1.
    UniGenei Mm.346654.

    3D structure databases

    ProteinModelPortali Q8C6M1.
    SMRi Q8C6M1. Positions 5-99, 143-247, 437-688.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C19.025.

    PTM databases

    PhosphoSitei Q8C6M1.

    Proteomic databases

    MaxQBi Q8C6M1.
    PaxDbi Q8C6M1.
    PRIDEi Q8C6M1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000102849 ; ENSMUSP00000099913 ; ENSMUSG00000026854 .
    ENSMUST00000170476 ; ENSMUSP00000127388 ; ENSMUSG00000026854 .
    GeneIDi 74270.
    KEGGi mmu:74270.
    UCSCi uc008jde.2. mouse.

    Organism-specific databases

    CTDi 10868.
    MGIi MGI:1921520. Usp20.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG5560.
    GeneTreei ENSGT00750000117701.
    HOGENOMi HOG000286031.
    HOVERGENi HBG054196.
    InParanoidi Q8C6M1.
    KOi K11848.
    OMAi ADYGQIS.
    OrthoDBi EOG7CRTP2.
    PhylomeDBi Q8C6M1.
    TreeFami TF352179.

    Miscellaneous databases

    NextBioi 340299.
    PROi Q8C6M1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8C6M1.
    Bgeei Q8C6M1.
    Genevestigatori Q8C6M1.

    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. 1 hit.
    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. "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.
      , 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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-134 AND THR-378, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiUBP20_MOUSE
    AccessioniPrimary (citable) accession number: Q8C6M1
    Secondary accession number(s): Q69ZT5, Q8CJ72
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2009
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 102 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3