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Q99K46

- UBP11_MOUSE

UniProt

Q99K46 - UBP11_MOUSE

Protein

Ubiquitin carboxyl-terminal hydrolase 11

Gene

Usp11

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 4 (27 Jul 2011)
      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 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 sitei266 – 2661NucleophilePROSITE-ProRule annotation
    Active sitei847 – 8471Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. 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

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:2384312. Usp11.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 921921Ubiquitin carboxyl-terminal hydrolase 11PRO_0000080633Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei194 – 1941N6-acetyllysineBy similarity
    Modified residuei596 – 5961PhosphoserineBy similarity
    Modified residuei906 – 9061PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ99K46.
    PaxDbiQ99K46.
    PRIDEiQ99K46.

    PTM databases

    PhosphoSiteiQ99K46.

    Expressioni

    Gene expression databases

    ArrayExpressiQ99K46.
    BgeeiQ99K46.
    CleanExiMM_USP11.
    GenevestigatoriQ99K46.

    Interactioni

    Subunit structurei

    Interacts with RANBP9/RANBPM. Interacts with BRCA2, CHUK/IKKA and NFKBIA By similarity.By similarity

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000033383.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99K46.
    SMRiQ99K46. Positions 29-233, 253-447, 738-890.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 133106DUSPPROSITE-ProRule annotationAdd
    BLAST
    Domaini257 – 889633USPAdd
    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.
    GeneTreeiENSGT00670000097750.
    HOGENOMiHOG000264375.
    HOVERGENiHBG000864.
    InParanoidiB1AXB2.
    KOiK11835.
    OMAiNFRNPLG.
    OrthoDBiEOG77Q4VW.
    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.

    Q99K46-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAVAADPAA AAVPASAEDR DTQPEAMPDL DEQWRQIGNG RERPLRAGES    50
    WFLVEKHWYK QWEVYVKGGD QDASTFPGCI NNAGLFEDQI SWHLRERLLE 100
    GDDYVLLPAP AWNYMVSWYG LMDGQPPIER KVIELPGIRK VEVYPLELLL 150
    VQHSDMETAL TIQFSYTDSV ELVLQTAREQ FLVEPQEDTR LWTKNSEGSL 200
    DRLCNTQITL LDACLETGQL VIMETRNKDG TWPSAQLCGM NNIPDEDEDF 250
    QGQPGICGLT NLGNTCFMNS ALQCLSNVPQ LTEYFLNNRY LEELNFRNPL 300
    GMKGELAEAY ADLVKQTWSG YHRSIVPNVF KNKVGHFASQ FLGYQQHDSQ 350
    ELLSFLLDGL HEDLNRVKKK EYVELCNGAG RPDLEVAQEA WQNHKRRNDS 400
    VIVDTFHGLF KSTLVCPDCG NVSVTFDPFC YLSVPLPVCS RRVLEVFFVP 450
    MDPRRKPEQH RVVVPKKGNI SDLCVALSTH TSVAPDKMIV ADVFSHRFYK 500
    LYQLEDPLSG ILDRDDIFVY EVTGRIEPVE GSRDDIVVPV YLRERTPSRD 550
    YNNSYYGLIL FGHPLLVSVP RDRFSWEGLY NILMYRLSRY VTKPTSDEDD 600
    GDEKVDEDED EDVEDDSSSE EEKEEMSAPT VNDGTREAEQ EQAGTSSGVT 650
    ERCPSLLDNS LRASQWPPRR RRKQLFTLQT VNSNGTSDRT TSPEEMQTQP 700
    YIAMDWEPDM KRRYYDEVEA EGYVKHDCVG YMLKKSPVQL KECIKLFTTV 750
    ETLEKENPWY CSSCKQHQLA TKKLDLWMLP EVLIIHLKRF SFSKISREKL 800
    DTLVQFPIRD LDFSEFVIKP KNESSPDLYK YDLIAVSNHY GGMRDGHYTT 850
    FACNKDSGQW HYFDDNSVSP VNENQIESKA AYVLFYQRQD VGRRQSQTSS 900
    SDTPASPVSS STPNSDIMDI N 921
    Length:921
    Mass (Da):105,384
    Last modified:July 27, 2011 - v4
    Checksum:i269E4A3267B9EE1D
    GO

    Sequence cautioni

    The sequence AAH05470.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti863 – 8631F → L in AAH05470. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK166523 mRNA. Translation: BAE38827.1.
    AL807240 Genomic DNA. Translation: CAM23095.1.
    CH466625 Genomic DNA. Translation: EDL00740.1.
    BC005470 mRNA. Translation: AAH05470.1. Different initiation.
    CCDSiCCDS53015.1.
    RefSeqiNP_663603.3. NM_145628.4.
    UniGeneiMm.34489.

    Genome annotation databases

    EnsembliENSMUST00000033383; ENSMUSP00000033383; ENSMUSG00000031066.
    GeneIDi236733.
    KEGGimmu:236733.
    UCSCiuc009stq.3. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK166523 mRNA. Translation: BAE38827.1 .
    AL807240 Genomic DNA. Translation: CAM23095.1 .
    CH466625 Genomic DNA. Translation: EDL00740.1 .
    BC005470 mRNA. Translation: AAH05470.1 . Different initiation.
    CCDSi CCDS53015.1.
    RefSeqi NP_663603.3. NM_145628.4.
    UniGenei Mm.34489.

    3D structure databases

    ProteinModelPortali Q99K46.
    SMRi Q99K46. Positions 29-233, 253-447, 738-890.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000033383.

    Protein family/group databases

    MEROPSi C19.014.

    PTM databases

    PhosphoSitei Q99K46.

    Proteomic databases

    MaxQBi Q99K46.
    PaxDbi Q99K46.
    PRIDEi Q99K46.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033383 ; ENSMUSP00000033383 ; ENSMUSG00000031066 .
    GeneIDi 236733.
    KEGGi mmu:236733.
    UCSCi uc009stq.3. mouse.

    Organism-specific databases

    CTDi 8237.
    MGIi MGI:2384312. Usp11.

    Phylogenomic databases

    eggNOGi COG5560.
    GeneTreei ENSGT00670000097750.
    HOGENOMi HOG000264375.
    HOVERGENi HBG000864.
    InParanoidi B1AXB2.
    KOi K11835.
    OMAi NFRNPLG.
    OrthoDBi EOG77Q4VW.
    TreeFami TF106276.

    Miscellaneous databases

    NextBioi 383051.
    PROi Q99K46.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99K46.
    Bgeei Q99K46.
    CleanExi MM_USP11.
    Genevestigatori Q99K46.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] OF 1-367.
      Tissue: Mammary gland.
    4. "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] OF 125-921.

    Entry informationi

    Entry nameiUBP11_MOUSE
    AccessioniPrimary (citable) accession number: Q99K46
    Secondary accession number(s): B1AXB2, Q3TLG5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 9, 2003
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 106 of the entry and version 4 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