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Q9Y2K6

- UBP20_HUMAN

UniProt

Q9Y2K6 - UBP20_HUMAN

Protein

Ubiquitin carboxyl-terminal hydrolase 20

Gene

USP20

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      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.4 Publications

    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 – 1541Nucleophile
    Active sitei643 – 6431Proton 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. G-protein coupled receptor binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. ubiquitin-specific protease activity Source: InterPro
    5. ubiquitin thiolesterase activity Source: UniProtKB
    6. 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
    Short name:
    hVDU2
    Gene namesi
    Name:USP20
    Synonyms:KIAA1003, LSFR3A, VDU2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:12619. USP20.

    Subcellular locationi

    Cytoplasmperinuclear region By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication
    Note: According to PubMed:12865408, it localizes in the endoplasmic reticulum; however the relevance of such result is unclear.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi154 – 1541C → S: Abolishes deubiquitinating activity. Does not inhibit lysosomal trafficking of ADRB2; when associated with Q-643. 1 Publication
    Mutagenesisi643 – 6431H → Q: Abolishes deubiquitinating activity. Does not inhibit lysosomal trafficking of ADRB2; when associated with S-154. 1 Publication

    Organism-specific databases

    PharmGKBiPA37245.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 914914Ubiquitin carboxyl-terminal hydrolase 20PRO_0000080647Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei132 – 1321Phosphoserine2 Publications
    Modified residuei134 – 1341Phosphoserine2 Publications
    Modified residuei258 – 2581Phosphothreonine1 Publication
    Modified residuei368 – 3681PhosphoserineBy similarity
    Modified residuei377 – 3771Phosphothreonine1 Publication
    Modified residuei413 – 4131Phosphoserine1 Publication

    Post-translational modificationi

    Ubiquitinated via a VHL-dependent pathway for proteasomal degradation.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9Y2K6.
    PaxDbiQ9Y2K6.
    PRIDEiQ9Y2K6.

    PTM databases

    PhosphoSiteiQ9Y2K6.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y2K6.
    BgeeiQ9Y2K6.
    CleanExiHS_USP20.
    GenevestigatoriQ9Y2K6.

    Organism-specific databases

    HPAiHPA006287.

    Interactioni

    Subunit structurei

    Interacts with VHL, leading to its ubiquitination and subsequent degradation. Interacts with CCP110, DIO2 and HIF1A.5 Publications

    Protein-protein interaction databases

    BioGridi116077. 51 interactions.
    IntActiQ9Y2K6. 40 interactions.
    MINTiMINT-4658328.
    STRINGi9606.ENSP00000313811.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y2K6.
    SMRiQ9Y2K6. Positions 5-97, 143-280, 435-686.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini145 – 685541USPAdd
    BLAST
    Domaini687 – 78094DUSP 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini789 – 892104DUSP 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.
    HOGENOMiHOG000286031.
    HOVERGENiHBG054196.
    InParanoidiQ9Y2K6.
    KOiK11848.
    OMAiADYGQIS.
    OrthoDBiEOG7CRTP2.
    PhylomeDBiQ9Y2K6.
    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.

    Q9Y2K6-1 [UniParc]FASTAAdd to Basket

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    MGDSRDLCPH LDSIGEVTKE DLLLKSKGTC QSCGVTGPNL WACLQVACPY    50
    VGCGESFADH STIHAQAKKH NLTVNLTTFR LWCYACEKEV FLEQRLAAPL 100
    LGSSSKFSEQ DSPPPSHPLK AVPIAVADEG ESESEDDDLK PRGLTGMKNL 150
    GNSCYMNAAL QALSNCPPLT QFFLECGGLV RTDKKPALCK SYQKLVSEVW 200
    HKKRPSYVVP TSLSHGIKLV NPMFRGYAQQ DTQEFLRCLM DQLHEELKEP 250
    VVATVALTEA RDSDSSDTDE KREGDRSPSE DEFLSCDSSS DRGEGDGQGR 300
    GGGSSQAETE LLIPDEAGRA ISEKERMKDR KFSWGQQRTN SEQVDEDADV 350
    DTAMAALDDQ PAEAQPPSPR SSSPCRTPEP DNDAHLRSSS RPCSPVHHHE 400
    GHAKLSSSPP RASPVRMAPS YVLKKAQVLS AGSRRRKEQR YRSVISDIFD 450
    GSILSLVQCL TCDRVSTTVE TFQDLSLPIP GKEDLAKLHS AIYQNVPAKP 500
    GACGDSYAAQ GWLAFIVEYI RRFVVSCTPS WFWGPVVTLE DCLAAFFAAD 550
    ELKGDNMYSC ERCKKLRNGV KYCKVLRLPE ILCIHLKRFR HEVMYSFKIN 600
    SHVSFPLEGL DLRPFLAKEC TSQITTYDLL SVICHHGTAG SGHYIAYCQN 650
    VINGQWYEFD DQYVTEVHET VVQNAEGYVL FYRKSSEEAM RERQQVVSLA 700
    AMREPSLLRF YVSREWLNKF NTFAEPGPIT NQTFLCSHGG IPPHKYHYID 750
    DLVVILPQNV WEHLYNRFGG GPAVNHLYVC SICQVEIEAL AKRRRIEIDT 800
    FIKLNKAFQA EESPGVIYCI SMQWFREWEA FVKGKDNEPP GPIDNSRIAQ 850
    VKGSGHVQLK QGADYGQISE ETWTYLNSLY GGGPEIAIRQ SVAQPLGPEN 900
    LHGEQKIEAE TRAV 914
    Length:914
    Mass (Da):102,003
    Last modified:October 17, 2006 - v2
    Checksum:iDC094570A396D20E
    GO

    Sequence cautioni

    The sequence BAA76847.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti320 – 3201A → V in AAL79676. (PubMed:12056827)Curated
    Sequence conflicti320 – 3201A → V in BAA76847. (PubMed:10231032)Curated
    Sequence conflicti359 – 3591Missing in AAL79676. (PubMed:12056827)Curated
    Sequence conflicti359 – 3591Missing in BAA76847. (PubMed:10231032)Curated
    Sequence conflicti359 – 3591Missing in EAW87914. 1 PublicationCurated
    Sequence conflicti359 – 3591Missing in AAH39593. (PubMed:15489334)Curated
    Sequence conflicti776 – 7761H → Q in CAB44350. (PubMed:10369878)Curated
    Sequence conflicti794 – 7941R → M in CAB44350. (PubMed:10369878)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti103 – 1031S → Y.
    Corresponds to variant rs36086252 [ dbSNP | Ensembl ].
    VAR_051529
    Natural varianti444 – 4441V → I.
    Corresponds to variant rs36055332 [ dbSNP | Ensembl ].
    VAR_051530

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY074877 mRNA. Translation: AAL79676.1.
    AB023220 mRNA. Translation: BAA76847.2. Different initiation.
    AL158207 Genomic DNA. Translation: CAC88170.1.
    CH471090 Genomic DNA. Translation: EAW87914.1.
    BC039593 mRNA. Translation: AAH39593.1.
    Y17457 Genomic DNA. Translation: CAB44350.1.
    Y17459 Genomic DNA. Translation: CAB44352.1.
    CCDSiCCDS43892.1.
    RefSeqiNP_001008563.2. NM_001008563.4.
    NP_001103773.2. NM_001110303.3.
    NP_006667.3. NM_006676.7.
    XP_005251722.1. XM_005251665.1.
    XP_006717001.1. XM_006716938.1.
    UniGeneiHs.5452.

    Genome annotation databases

    EnsembliENST00000315480; ENSP00000313811; ENSG00000136878.
    ENST00000358355; ENSP00000351122; ENSG00000136878.
    ENST00000372429; ENSP00000361506; ENSG00000136878.
    GeneIDi10868.
    KEGGihsa:10868.
    UCSCiuc004byr.3. human.

    Polymorphism databases

    DMDMi116242837.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY074877 mRNA. Translation: AAL79676.1 .
    AB023220 mRNA. Translation: BAA76847.2 . Different initiation.
    AL158207 Genomic DNA. Translation: CAC88170.1 .
    CH471090 Genomic DNA. Translation: EAW87914.1 .
    BC039593 mRNA. Translation: AAH39593.1 .
    Y17457 Genomic DNA. Translation: CAB44350.1 .
    Y17459 Genomic DNA. Translation: CAB44352.1 .
    CCDSi CCDS43892.1.
    RefSeqi NP_001008563.2. NM_001008563.4.
    NP_001103773.2. NM_001110303.3.
    NP_006667.3. NM_006676.7.
    XP_005251722.1. XM_005251665.1.
    XP_006717001.1. XM_006716938.1.
    UniGenei Hs.5452.

    3D structure databases

    ProteinModelPortali Q9Y2K6.
    SMRi Q9Y2K6. Positions 5-97, 143-280, 435-686.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116077. 51 interactions.
    IntActi Q9Y2K6. 40 interactions.
    MINTi MINT-4658328.
    STRINGi 9606.ENSP00000313811.

    Protein family/group databases

    MEROPSi C19.025.

    PTM databases

    PhosphoSitei Q9Y2K6.

    Polymorphism databases

    DMDMi 116242837.

    Proteomic databases

    MaxQBi Q9Y2K6.
    PaxDbi Q9Y2K6.
    PRIDEi Q9Y2K6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000315480 ; ENSP00000313811 ; ENSG00000136878 .
    ENST00000358355 ; ENSP00000351122 ; ENSG00000136878 .
    ENST00000372429 ; ENSP00000361506 ; ENSG00000136878 .
    GeneIDi 10868.
    KEGGi hsa:10868.
    UCSCi uc004byr.3. human.

    Organism-specific databases

    CTDi 10868.
    GeneCardsi GC09P132596.
    H-InvDB HIX0008459.
    HGNCi HGNC:12619. USP20.
    HPAi HPA006287.
    MIMi 615143. gene.
    neXtProti NX_Q9Y2K6.
    PharmGKBi PA37245.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5560.
    HOGENOMi HOG000286031.
    HOVERGENi HBG054196.
    InParanoidi Q9Y2K6.
    KOi K11848.
    OMAi ADYGQIS.
    OrthoDBi EOG7CRTP2.
    PhylomeDBi Q9Y2K6.
    TreeFami TF352179.

    Miscellaneous databases

    ChiTaRSi USP20. human.
    GeneWikii USP20.
    GenomeRNAii 10868.
    NextBioi 41265.
    PROi Q9Y2K6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y2K6.
    Bgeei Q9Y2K6.
    CleanExi HS_USP20.
    Genevestigatori Q9Y2K6.

    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], FUNCTION, UBIQUITINATION, INTERACTION WITH VHL.
    2. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    3. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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].
      Tissue: Ovary.
    6. "Extensive gene order differences within regions of conserved synteny between the Fugu and human genomes: implications for chromosomal evolution and the cloning of disease genes."
      Gilley J., Fried M.
      Hum. Mol. Genet. 8:1313-1320(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 581-803 AND 839-914.
    7. "Deubiquitination of type 2 iodothyronine deiodinase by von Hippel-Lindau protein-interacting deubiquitinating enzymes regulates thyroid hormone activation."
      Curcio-Morelli C., Zavacki A.M., Christofollete M., Gereben B., de Freitas B.C., Harney J.W., Li Z., Wu G., Bianco A.C.
      J. Clin. Invest. 112:189-196(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DIO2.
    8. "VHL protein-interacting deubiquitinating enzyme 2 deubiquitinates and stabilizes HIF-1alpha."
      Li Z., Wang D., Messing E.M., Wu G.
      EMBO Rep. 6:373-378(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HIF1A.
    9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-258, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-134, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-377 AND SER-413, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "The deubiquitinases USP33 and USP20 coordinate beta2 adrenergic receptor recycling and resensitization."
      Berthouze M., Venkataramanan V., Li Y., Shenoy S.K.
      EMBO J. 28:1684-1696(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ADRB2, MUTAGENESIS OF CYS-154 AND HIS-643.
    13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-134, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "USP33 regulates centrosome biogenesis via deubiquitination of the centriolar protein CP110."
      Li J., D'Angiolella V., Seeley E.S., Kim S., Kobayashi T., Fu W., Campos E.I., Pagano M., Dynlacht B.D.
      Nature 495:255-259(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CCP110.

    Entry informationi

    Entry nameiUBP20_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y2K6
    Secondary accession number(s): Q541F1
    , Q8IXQ1, Q96LG5, Q9UQN8, Q9UQP0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 133 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3