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P51784

- UBP11_HUMAN

UniProt

P51784 - UBP11_HUMAN

Protein

Ubiquitin carboxyl-terminal hydrolase 11

Gene

USP11

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 3 (07 Jul 2009)
      Previous versions | rss
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    Functioni

    Protease that can remove conjugated ubiquitin from target proteins and polyubiquitin chains. Inhibits the degradation of target proteins by the proteasome. Plays a role in the regulation of pathways leading to NF-kappa-B activation. Plays a role in the regulation of DNA repair after double-stranded DNA breaks.5 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).1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei318 – 3181Nucleophile
    Active sitei888 – 8881Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: ProtInc
    2. protein binding Source: UniProtKB
    3. ubiquitin-specific protease activity Source: UniProtKB

    GO - Biological processi

    1. protein deubiquitination Source: UniProtKB
    2. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_16907. Association of TriC/CCT with target proteins during biosynthesis.

    Protein family/group databases

    MEROPSiC19.014.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 11 (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme 11
    Ubiquitin thioesterase 11
    Ubiquitin-specific-processing protease 11
    Gene namesi
    Name:USP11
    Synonyms:UHX1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:12609. USP11.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Predominantly nuclear. Associates with chromatin.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi318 – 3181C → S: Loss of deubiquitinase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA37235.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 963963Ubiquitin carboxyl-terminal hydrolase 11PRO_0000080632Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei245 – 2451N6-acetyllysine1 Publication
    Modified residuei648 – 6481Phosphoserine2 Publications
    Modified residuei948 – 9481Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP51784.
    PaxDbiP51784.
    PRIDEiP51784.

    PTM databases

    PhosphoSiteiP51784.

    Expressioni

    Gene expression databases

    ArrayExpressiP51784.
    BgeeiP51784.
    CleanExiHS_USP11.
    GenevestigatoriP51784.

    Organism-specific databases

    HPAiHPA003103.
    HPA037536.

    Interactioni

    Subunit structurei

    Interacts with RANBP9/RANBPM. Interacts with BRCA2, CHUK/IKKA and NFKBIA. Interacts with papilloma virus protein 16E7.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BMI1P352267EBI-306876,EBI-2341576
    CBX8Q9HC525EBI-306876,EBI-712912
    E7P031296EBI-306876,EBI-866453From a different organism.
    NPQ9DLK63EBI-306876,EBI-8433218From a different organism.
    PAP156592EBI-306876,EBI-8431752From a different organism.
    PCGF2P352275EBI-306876,EBI-2129767
    RING1Q065874EBI-306876,EBI-752313
    RNF2Q994964EBI-306876,EBI-722416
    tatP046083EBI-306876,EBI-6164389From a different organism.

    Protein-protein interaction databases

    BioGridi113866. 98 interactions.
    DIPiDIP-27567N.
    IntActiP51784. 80 interactions.
    MINTiMINT-1147600.
    STRINGi9606.ENSP00000218348.

    Structurei

    Secondary structure

    1
    963
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi78 – 869
    Beta strandi87 – 915
    Beta strandi101 – 1066
    Helixi107 – 11711
    Turni118 – 1203
    Helixi134 – 1363
    Beta strandi140 – 1423
    Turni152 – 1543
    Beta strandi155 – 1595
    Helixi160 – 16910
    Beta strandi180 – 1856
    Beta strandi190 – 1956
    Beta strandi197 – 2059
    Beta strandi207 – 2159
    Helixi221 – 23111
    Beta strandi240 – 2456
    Turni247 – 2493
    Beta strandi252 – 2543
    Beta strandi257 – 2615
    Helixi262 – 2643
    Beta strandi271 – 2766

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4MELX-ray2.90A/B67-288[»]
    ProteinModelPortaliP51784.
    SMRiP51784. Positions 96-284, 305-491, 779-931.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini76 – 184109DUSPPROSITE-ProRule annotationAdd
    BLAST
    Domaini309 – 930622USPAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase C19 family.Curated
    Contains 1 DUSP domain.PROSITE-ProRule annotation
    Contains 1 USP domain.Curated

    Phylogenomic databases

    eggNOGiCOG5560.
    HOGENOMiHOG000264375.
    HOVERGENiHBG000864.
    InParanoidiP51784.
    KOiK11835.
    OMAiNFRNPLG.
    PhylomeDBiP51784.
    TreeFamiTF106276.

    Family and domain databases

    Gene3Di3.30.2230.10. 1 hit.
    InterProiIPR006615. Pept_C19_DUSP.
    IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028135. Ub_USP-typ.
    IPR028889. UCH/PAN2.
    [Graphical view]
    PfamiPF06337. DUSP. 1 hit.
    PF14836. Ubiquitin_3. 1 hit.
    PF00443. UCH. 1 hit.
    [Graphical view]
    SMARTiSM00695. DUSP. 1 hit.
    [Graphical view]
    SUPFAMiSSF143791. SSF143791. 1 hit.
    PROSITEiPS51283. DUSP. 1 hit.
    PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P51784-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVAPRLFGG LCFRFRDQNP EVAVEGRLPI SHSCVGCRRE RTAMATVAAN    50
    PAAAAAAVAA AAAVTEDREP QHEELPGLDS QWRQIENGES GRERPLRAGE 100
    SWFLVEKHWY KQWEAYVQGG DQDSSTFPGC INNATLFQDE INWRLKEGLV 150
    EGEDYVLLPA AAWHYLVSWY GLEHGQPPIE RKVIELPNIQ KVEVYPVELL 200
    LVRHNDLGKS HTVQFSHTDS IGLVLRTARE RFLVEPQEDT RLWAKNSEGS 250
    LDRLYDTHIT VLDAALETGQ LIIMETRKKD GTWPSAQLHV MNNNMSEEDE 300
    DFKGQPGICG LTNLGNTCFM NSALQCLSNV PQLTEYFLNN CYLEELNFRN 350
    PLGMKGEIAE AYADLVKQAW SGHHRSIVPH VFKNKVGHFA SQFLGYQQHD 400
    SQELLSFLLD GLHEDLNRVK KKEYVELCDA AGRPDQEVAQ EAWQNHKRRN 450
    DSVIVDTFHG LFKSTLVCPD CGNVSVTFDP FCYLSVPLPI SHKRVLEVFF 500
    IPMDPRRKPE QHRLVVPKKG KISDLCVALS KHTGISPERM MVADVFSHRF 550
    YKLYQLEEPL SSILDRDDIF VYEVSGRIEA IEGSREDIVV PVYLRERTPA 600
    RDYNNSYYGL MLFGHPLLVS VPRDRFTWEG LYNVLMYRLS RYVTKPNSDD 650
    EDDGDEKEDD EEDKDDVPGP STGGSLRDPE PEQAGPSSGV TNRCPFLLDN 700
    CLGTSQWPPR RRRKQLFTLQ TVNSNGTSDR TTSPEEVHAQ PYIAIDWEPE 750
    MKKRYYDEVE AEGYVKHDCV GYVMKKAPVR LQECIELFTT VETLEKENPW 800
    YCPSCKQHQL ATKKLDLWML PEILIIHLKR FSYTKFSREK LDTLVEFPIR 850
    DLDFSEFVIQ PQNESNPELY KYDLIAVSNH YGGMRDGHYT TFACNKDSGQ 900
    WHYFDDNSVS PVNENQIESK AAYVLFYQRQ DVARRLLSPA GSSGAPASPA 950
    CSSPPSSEFM DVN 963
    Length:963
    Mass (Da):109,817
    Last modified:July 7, 2009 - v3
    Checksum:i876FDC41945AFD9B
    GO

    Sequence cautioni

    The sequence AAC50450.1 differs from that shown. Reason: Frameshift at positions 65, 117, 134 and 146.
    The sequence AAC50450.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAC20463.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAD20056.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti52 – 521A → AT in BAC20463. (PubMed:12084015)Curated
    Sequence conflicti58 – 581V → M in AAC50450. (PubMed:8845848)Curated
    Sequence conflicti62 – 621A → R in AAC50450. (PubMed:8845848)Curated
    Sequence conflicti82 – 832WR → CG in AAC50450. (PubMed:8845848)Curated
    Sequence conflicti160 – 1601A → R in BAC20463. (PubMed:12084015)Curated
    Sequence conflicti161 – 1611A → R in BAC20463. (PubMed:12084015)Curated
    Sequence conflicti161 – 1611A → R in AAC50450. (PubMed:8845848)Curated
    Sequence conflicti489 – 4891P → L in AAH00350. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL096791 Genomic DNA. Translation: CAD20056.1. Sequence problems.
    BC140849 mRNA. Translation: AAI40850.1.
    BC000350 mRNA. Translation: AAH00350.4.
    AB073597 mRNA. Translation: BAC20463.1. Different initiation.
    U44839 mRNA. Translation: AAC50450.1. Sequence problems.
    CCDSiCCDS14277.1.
    RefSeqiNP_004642.2. NM_004651.3.
    XP_005272731.1. XM_005272674.2.
    UniGeneiHs.171501.

    Genome annotation databases

    EnsembliENST00000218348; ENSP00000218348; ENSG00000102226.
    GeneIDi8237.
    KEGGihsa:8237.
    UCSCiuc004dhp.3. human.

    Polymorphism databases

    DMDMi251757432.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL096791 Genomic DNA. Translation: CAD20056.1 . Sequence problems.
    BC140849 mRNA. Translation: AAI40850.1 .
    BC000350 mRNA. Translation: AAH00350.4 .
    AB073597 mRNA. Translation: BAC20463.1 . Different initiation.
    U44839 mRNA. Translation: AAC50450.1 . Sequence problems.
    CCDSi CCDS14277.1.
    RefSeqi NP_004642.2. NM_004651.3.
    XP_005272731.1. XM_005272674.2.
    UniGenei Hs.171501.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4MEL X-ray 2.90 A/B 67-288 [» ]
    ProteinModelPortali P51784.
    SMRi P51784. Positions 96-284, 305-491, 779-931.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113866. 98 interactions.
    DIPi DIP-27567N.
    IntActi P51784. 80 interactions.
    MINTi MINT-1147600.
    STRINGi 9606.ENSP00000218348.

    Protein family/group databases

    MEROPSi C19.014.

    PTM databases

    PhosphoSitei P51784.

    Polymorphism databases

    DMDMi 251757432.

    Proteomic databases

    MaxQBi P51784.
    PaxDbi P51784.
    PRIDEi P51784.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000218348 ; ENSP00000218348 ; ENSG00000102226 .
    GeneIDi 8237.
    KEGGi hsa:8237.
    UCSCi uc004dhp.3. human.

    Organism-specific databases

    CTDi 8237.
    GeneCardsi GC0XP047093.
    HGNCi HGNC:12609. USP11.
    HPAi HPA003103.
    HPA037536.
    MIMi 300050. gene.
    neXtProti NX_P51784.
    PharmGKBi PA37235.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5560.
    HOGENOMi HOG000264375.
    HOVERGENi HBG000864.
    InParanoidi P51784.
    KOi K11835.
    OMAi NFRNPLG.
    PhylomeDBi P51784.
    TreeFami TF106276.

    Enzyme and pathway databases

    Reactomei REACT_16907. Association of TriC/CCT with target proteins during biosynthesis.

    Miscellaneous databases

    ChiTaRSi USP11. human.
    GeneWikii USP11.
    GenomeRNAii 8237.
    NextBioi 30985.
    PROi P51784.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51784.
    Bgeei P51784.
    CleanExi HS_USP11.
    Genevestigatori P51784.

    Family and domain databases

    Gene3Di 3.30.2230.10. 1 hit.
    InterProi IPR006615. Pept_C19_DUSP.
    IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028135. Ub_USP-typ.
    IPR028889. UCH/PAN2.
    [Graphical view ]
    Pfami PF06337. DUSP. 1 hit.
    PF14836. Ubiquitin_3. 1 hit.
    PF00443. UCH. 1 hit.
    [Graphical view ]
    SMARTi SM00695. DUSP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF143791. SSF143791. 1 hit.
    PROSITEi PS51283. DUSP. 1 hit.
    PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "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: Muscle.
    3. "Structural and functional characterization of the USP11 deubiquitinating enzyme, which interacts with the RanGTP-associated protein RanBPM."
      Ideguchi H., Ueda A., Tanaka M., Yang J., Tsuji T., Ohno S., Hagiwara E., Aoki A., Ishigatsubo Y.
      Biochem. J. 367:87-95(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 41-963, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH RANBP9.
      Tissue: Fetal brain.
    4. "A ubiquitin C-terminal hydrolase gene on the proximal short arm of the X chromosome: implications for X-linked retinal disorders."
      Swanson D.A., Freund C.L., Ploder L., McInnes R.R., Valle D.
      Hum. Mol. Genet. 5:533-538(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 52-963.
      Tissue: Retina.
    5. "BRCA2 is ubiquitinated in vivo and interacts with USP11, a deubiquitinating enzyme that exhibits prosurvival function in the cellular response to DNA damage."
      Schoenfeld A.R., Apgar S., Dolios G., Wang R., Aaronson S.A.
      Mol. Cell. Biol. 24:7444-7455(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BRCA2, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-318, IDENTIFICATION BY MASS SPECTROMETRY.
    6. "The deubiquitinating enzyme USP11 controls an IkappaB kinase alpha (IKKalpha)-p53 signaling pathway in response to tumor necrosis factor alpha (TNFalpha)."
      Yamaguchi T., Kimura J., Miki Y., Yoshida K.
      J. Biol. Chem. 282:33943-33948(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CHUK.
    7. "USP11 stabilizes HPV-16E7 and further modulates the E7 biological activity."
      Lin C.H., Chang H.S., Yu W.C.
      J. Biol. Chem. 283:15681-15688(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HUMAN PAPILLOMA VIRUS 16E7.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-948, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "USP11 negatively regulates TNFalpha-induced NF-kappaB activation by targeting on IkappaBalpha."
      Sun W., Tan X., Shi Y., Xu G., Mao R., Gu X., Fan Y., Yu Y., Burlingame S., Zhang H., Rednam S.P., Lu X., Zhang T., Fu S., Cao G., Qin J., Yang J.
      Cell. Signal. 22:386-394(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NFKBIA, IDENTIFICATION BY MASS SPECTROMETRY.
    12. "Sensitivity to poly(ADP-ribose) polymerase (PARP) inhibition identifies ubiquitin-specific peptidase 11 (USP11) as a regulator of DNA double-strand break repair."
      Wiltshire T.D., Lovejoy C.A., Wang T., Xia F., O'Connor M.J., Cortez D.
      J. Biol. Chem. 285:14565-14571(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-648, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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-648, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiUBP11_HUMAN
    AccessioniPrimary (citable) accession number: P51784
    Secondary accession number(s): B2RTX1, Q8IUG6, Q9BWE1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: July 7, 2009
    Last modified: October 1, 2014
    This is version 144 of the entry and version 3 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

    Caution

    It is uncertain whether Met-1 or Met-44 is the initiator.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Peptidase families
      Classification of peptidase families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3