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Q7TQI3

- OTUB1_MOUSE

UniProt

Q7TQI3 - OTUB1_MOUSE

Protein

Ubiquitin thioesterase OTUB1

Gene

Otub1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 2 (01 Mar 2004)
      Previous versions | rss
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    Functioni

    Hydrolase that can specifically remove compared to 'Lys-48'-linked conjugated ubiquitin from proteins and plays an important regulatory role at the level of protein turnover by preventing degradation. Regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered unresponsive to antigen rechallenge and no longer respond to their cognate antigen. Acts via its interaction with RNF128/GRAIL. Surprisingly, it regulates RNF128-mediated ubiquitination, but does not deubiquitinate polyubiquitinated RNF128. Deubiquitinates estrogen receptor alpha (ESR1). Mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains, but not 'Lys-63'-linked polyubiquitin chains. Not able to cleave di-ubiquitin. Also capable of removing NEDD8 from NEDD8 conjugates, but with a much lower preference compared to 'Lys-48'-linked ubiquitin.1 Publication
    Plays a key non-catalytic role in DNA repair regulation by inhibiting activity of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites. Inhibits RNF168 independently of ubiquitin thioesterase activity by binding and inhibiting UBE2N/UBC13, the E2 partner of RNF168, thereby limiting spreading of 'Lys-63'-linked histone H2A and H2AX marks. Inhibition occurs by binding to free ubiquitin: free ubiquitin acts as an allosteric regulator that increases affinity for UBE2N/UBC13 and disrupts interaction with UBE2V1. The OTUB1-UBE2N/UBC13-free ubiquitin complex adopts a configuration that mimics a cleaved 'Lys48'-linked di-ubiquitin chain 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).

    Enzyme regulationi

    By free ubiquitin: binding of free ubiquitin triggers conformational changes in the OTU domain and formation of a ubiquitin-binding helix in the N-terminus, promoting binding of the conjugated donor ubiquitin in UBE2N/UBC13 to OTUB1.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei88 – 881By similarity
    Active sitei91 – 911NucleophileBy similarity
    Binding sitei221 – 2211Free ubiquitinBy similarity
    Binding sitei235 – 2351Free ubiquitinBy similarity
    Binding sitei237 – 2371Free ubiquitinBy similarity
    Binding sitei261 – 2611Free ubiquitinBy similarity
    Active sitei265 – 2651By similarity
    Binding sitei266 – 2661Free ubiquitinBy similarity

    GO - Molecular functioni

    1. NEDD8-specific protease activity Source: UniProtKB
    2. omega peptidase activity Source: InterPro
    3. ubiquitin binding Source: UniProtKB
    4. ubiquitin-specific protease activity Source: UniProtKB

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: UniProtKB
    2. DNA repair Source: UniProtKB-KW
    3. immune system process Source: UniProtKB-KW
    4. negative regulation of double-strand break repair Source: UniProtKB
    5. negative regulation of histone H2A K63-linked ubiquitination Source: UniProtKB
    6. protein K48-linked deubiquitination Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Adaptive immunity, DNA damage, DNA repair, Immunity, Ubl conjugation pathway

    Protein family/group databases

    MEROPSiC65.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin thioesterase OTUB1 (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme OTUB1
    OTU domain-containing ubiquitin aldehyde-binding protein 1
    Otubain-1
    Ubiquitin-specific-processing protease OTUB1
    Gene namesi
    Name:Otub1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:2147616. Otub1.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 271270Ubiquitin thioesterase OTUB1PRO_0000221009Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei16 – 161PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ7TQI3.
    PaxDbiQ7TQI3.
    PRIDEiQ7TQI3.

    2D gel databases

    REPRODUCTION-2DPAGEQ7TQI3.

    PTM databases

    PhosphoSiteiQ7TQI3.

    Expressioni

    Gene expression databases

    ArrayExpressiQ7TQI3.
    BgeeiQ7TQI3.
    CleanExiMM_OTUB1.
    GenevestigatoriQ7TQI3.

    Interactioni

    Subunit structurei

    Interacts with RNF128. Forms a ternary complex with RNF128 and USP8. Interacts with FUS, ESR1 and GNB2L1/RACK1. Interacts with UBE2N/UBC13 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi223228. 4 interactions.
    IntActiQ7TQI3. 3 interactions.
    MINTiMINT-1854563.
    STRINGi10090.ENSMUSP00000025679.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7TQI3.
    SMRiQ7TQI3. Positions 25-271.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini80 – 271192OTUPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni130 – 1389Ubiquitin-conjugating enzyme E2 bindingBy similarity
    Regioni169 – 1779Ubiquitin-conjugating enzyme E2 bindingBy similarity
    Regioni189 – 1957Free ubiquitin bindingBy similarity
    Regioni206 – 2138Ubiquitin-conjugating enzyme E2 bindingBy similarity
    Regioni214 – 2218Free ubiquitin bindingBy similarity
    Regioni245 – 2517Free ubiquitin bindingBy similarity

    Sequence similaritiesi

    Belongs to the peptidase C65 family.Curated
    Contains 1 OTU domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG267426.
    GeneTreeiENSGT00390000006979.
    HOGENOMiHOG000019496.
    HOVERGENiHBG053383.
    InParanoidiQ7TQI3.
    KOiK09602.
    OMAiVEPMYKE.
    OrthoDBiEOG71K64D.
    PhylomeDBiQ7TQI3.
    TreeFamiTF314145.

    Family and domain databases

    InterProiIPR003323. OTU.
    IPR019400. Peptidase_C65_otubain.
    IPR016615. Ubiquitin_thioesterase_Otubain.
    [Graphical view]
    PfamiPF10275. Peptidase_C65. 1 hit.
    [Graphical view]
    PIRSFiPIRSF013503. Ubiquitin_thioesterase_Otubain. 1 hit.
    PROSITEiPS50802. OTU. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q7TQI3-1 [UniParc]FASTAAdd to Basket

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    MAAEEPQQQK QEPLGSDSEG VNCLAYDEAI MAQQDRIQQE IAVQNPLVSE    50
    RLELSVLYKE YAEDDNIYQQ KIKDLHKKYS YIRKTRPDGN CFYRAFGFSH 100
    LEALLDDSKE LQRFKAVSAK SKEDLVSQGF TEFTIEDFHN TFMDLIEQVE 150
    KQTSVADLLA SFNDQSTSDY LVVYLRLLTS GYLQRESKFF EHFIEGGRTV 200
    KEFCQQEVEP MCKESDHIHI IALAQALSVS IQVEYMDRGE GGTTNPHVFP 250
    EGSEPKVYLL YRPGHYDILY K 271
    Length:271
    Mass (Da):31,270
    Last modified:March 1, 2004 - v2
    Checksum:i32F78EE1DC5FD679
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti186 – 1861E → D in BAE20433. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK027996 mRNA. Translation: BAE20433.1.
    AK140070 mRNA. Translation: BAE24227.1.
    AK145273 mRNA. Translation: BAE26339.1.
    AK145970 mRNA. Translation: BAE26795.1.
    BC022575 mRNA. Translation: AAH22575.1.
    BC054410 mRNA. Translation: AAH54410.1.
    CCDSiCCDS29520.1.
    RefSeqiNP_598911.1. NM_134150.2.
    UniGeneiMm.203921.

    Genome annotation databases

    EnsembliENSMUST00000025679; ENSMUSP00000025679; ENSMUSG00000024767.
    GeneIDi107260.
    KEGGimmu:107260.
    UCSCiuc008gki.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK027996 mRNA. Translation: BAE20433.1 .
    AK140070 mRNA. Translation: BAE24227.1 .
    AK145273 mRNA. Translation: BAE26339.1 .
    AK145970 mRNA. Translation: BAE26795.1 .
    BC022575 mRNA. Translation: AAH22575.1 .
    BC054410 mRNA. Translation: AAH54410.1 .
    CCDSi CCDS29520.1.
    RefSeqi NP_598911.1. NM_134150.2.
    UniGenei Mm.203921.

    3D structure databases

    ProteinModelPortali Q7TQI3.
    SMRi Q7TQI3. Positions 25-271.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 223228. 4 interactions.
    IntActi Q7TQI3. 3 interactions.
    MINTi MINT-1854563.
    STRINGi 10090.ENSMUSP00000025679.

    Protein family/group databases

    MEROPSi C65.001.

    PTM databases

    PhosphoSitei Q7TQI3.

    2D gel databases

    REPRODUCTION-2DPAGE Q7TQI3.

    Proteomic databases

    MaxQBi Q7TQI3.
    PaxDbi Q7TQI3.
    PRIDEi Q7TQI3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025679 ; ENSMUSP00000025679 ; ENSMUSG00000024767 .
    GeneIDi 107260.
    KEGGi mmu:107260.
    UCSCi uc008gki.1. mouse.

    Organism-specific databases

    CTDi 55611.
    MGIi MGI:2147616. Otub1.

    Phylogenomic databases

    eggNOGi NOG267426.
    GeneTreei ENSGT00390000006979.
    HOGENOMi HOG000019496.
    HOVERGENi HBG053383.
    InParanoidi Q7TQI3.
    KOi K09602.
    OMAi VEPMYKE.
    OrthoDBi EOG71K64D.
    PhylomeDBi Q7TQI3.
    TreeFami TF314145.

    Miscellaneous databases

    ChiTaRSi OTUB1. mouse.
    NextBioi 358648.
    PROi Q7TQI3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7TQI3.
    Bgeei Q7TQI3.
    CleanExi MM_OTUB1.
    Genevestigatori Q7TQI3.

    Family and domain databases

    InterProi IPR003323. OTU.
    IPR019400. Peptidase_C65_otubain.
    IPR016615. Ubiquitin_thioesterase_Otubain.
    [Graphical view ]
    Pfami PF10275. Peptidase_C65. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF013503. Ubiquitin_thioesterase_Otubain. 1 hit.
    PROSITEi PS50802. OTU. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: Corpora quadrigemina, Embryo, Mammary gland and Placenta.
    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].
      Strain: FVB/N.
      Tissue: Colon and Mammary tumor.
    3. Lubec G., Klug S.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 189-198, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hippocampus.
    4. Cited for: FUNCTION.
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiOTUB1_MOUSE
    AccessioniPrimary (citable) accession number: Q7TQI3
    Secondary accession number(s): Q3ULV9
    , Q3V408, Q8C326, Q8R5F2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2004
    Last sequence update: March 1, 2004
    Last modified: October 1, 2014
    This is version 103 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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