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Q5VV17

- OTUD1_HUMAN

UniProt

Q5VV17 - OTUD1_HUMAN

Protein

OTU domain-containing protein 1

Gene

OTUD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (07 Dec 2004)
      Previous versions | rss
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    Functioni

    Deubiquitinating enzyme that specifically hydrolyzes 'Lys-63'-linked polyubiquitin to monoubiquitin.1 Publication

    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 sitei317 – 3171By similarity
    Active sitei320 – 3201NucleophileBy similarity
    Active sitei431 – 4311By similarity

    GO - Molecular functioni

    1. ubiquitin-specific protease activity Source: UniProtKB

    GO - Biological processi

    1. protein K63-linked deubiquitination Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Ubl conjugation pathway

    Protein family/group databases

    MEROPSiC85.004.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    OTU domain-containing protein 1 (EC:3.4.19.12)
    Alternative name(s):
    DUBA-7
    Gene namesi
    Name:OTUD1
    Synonyms:DUBA7, OTDC1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:27346. OTUD1.

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134932304.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 481481OTU domain-containing protein 1PRO_0000271018Add
    BLAST

    Proteomic databases

    PaxDbiQ5VV17.
    PRIDEiQ5VV17.

    PTM databases

    PhosphoSiteiQ5VV17.

    Expressioni

    Gene expression databases

    BgeeiQ5VV17.
    CleanExiHS_OTUD1.
    GenevestigatoriQ5VV17.

    Organism-specific databases

    HPAiHPA038504.

    Interactioni

    Protein-protein interaction databases

    BioGridi128638. 7 interactions.
    IntActiQ5VV17. 10 interactions.
    STRINGi9606.ENSP00000365678.

    Structurei

    Secondary structure

    1
    481
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi290 – 30617
    Beta strandi310 – 3123
    Helixi320 – 33011
    Helixi333 – 3353
    Helixi336 – 34914
    Helixi351 – 3544
    Helixi355 – 3573
    Helixi362 – 3698
    Helixi378 – 38811
    Beta strandi391 – 3999
    Beta strandi402 – 4109
    Beta strandi412 – 4143
    Beta strandi421 – 4277
    Turni428 – 4303
    Beta strandi431 – 4366

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4BOPX-ray2.10A/B287-437[»]
    ProteinModelPortaliQ5VV17.
    SMRiQ5VV17. Positions 288-437.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini309 – 438130OTUPROSITE-ProRule annotationAdd
    BLAST
    Repeati457 – 47620UIMAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni314 – 3207Cys-loop
    Regioni369 – 37911His-loopAdd
    BLAST
    Regioni426 – 4316Variable-loop

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi13 – 155143Ala-richAdd
    BLAST

    Domaini

    The UIM repeat increases the specificity and efficiency of the enzyme toward 'Lys-63'-linked polyubiquitin.1 Publication
    Specificity is not given by the S1' ubiquitin-binding site within the OTU domain (composed of the Cys-, His- and Variable-loops).1 Publication

    Sequence similaritiesi

    Contains 1 OTU domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG327202.
    HOGENOMiHOG000115304.
    HOVERGENiHBG080487.
    InParanoidiQ5VV17.
    KOiK13716.
    OMAiNFRLSEH.
    OrthoDBiEOG7TBC35.
    PhylomeDBiQ5VV17.
    TreeFamiTF338508.

    Family and domain databases

    InterProiIPR003323. OTU.
    [Graphical view]
    PfamiPF02338. OTU. 1 hit.
    [Graphical view]
    PROSITEiPS50802. OTU. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q5VV17-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQLYSSVCTH YPAGAPGPTA AAPAPPAAAT PFKVSLQPPG AAGAAPEPET    50
    GECQPAAAAE HREAAAVPAA KMPAFSSCFE VVSGAAAPAS AAAGPPGASC 100
    KPPLPPHYTS TAQITVRALG ADRLLLHGPD PVPGAAGSAA APRGRCLLLA 150
    PAPAAPVPPR RGSSAWLLEE LLRPDCPEPA GLDATREGPD RNFRLSEHRQ 200
    ALAAAKHRGP AATPGSPDPG PGPWGEEHLA ERGPRGWERG GDRCDAPGGD 250
    AARRPDPEAE APPAGSIEAA PSSAAEPVIV SRSDPRDEKL ALYLAEVEKQ 300
    DKYLRQRNKY RFHIIPDGNC LYRAVSKTVY GDQSLHRELR EQTVHYIADH 350
    LDHFSPLIEG DVGEFIIAAA QDGAWAGYPE LLAMGQMLNV NIHLTTGGRL 400
    ESPTVSTMIH YLGPEDSLRP SIWLSWLSNG HYDAVFDHSY PNPEYDNWCK 450
    QTQVQRKRDE ELAKSMAISL SKMYIEQNAC S 481
    Length:481
    Mass (Da):51,063
    Last modified:December 7, 2004 - v1
    Checksum:i37B3AEB0B3851982
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL512603 Genomic DNA. Translation: CAH73715.1.
    CCDSiCCDS44366.1.
    RefSeqiNP_001138845.1. NM_001145373.2.
    UniGeneiHs.499042.

    Genome annotation databases

    EnsembliENST00000376495; ENSP00000365678; ENSG00000165312.
    GeneIDi220213.
    KEGGihsa:220213.
    UCSCiuc001irr.2. human.

    Polymorphism databases

    DMDMi74747188.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL512603 Genomic DNA. Translation: CAH73715.1 .
    CCDSi CCDS44366.1.
    RefSeqi NP_001138845.1. NM_001145373.2.
    UniGenei Hs.499042.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4BOP X-ray 2.10 A/B 287-437 [» ]
    ProteinModelPortali Q5VV17.
    SMRi Q5VV17. Positions 288-437.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 128638. 7 interactions.
    IntActi Q5VV17. 10 interactions.
    STRINGi 9606.ENSP00000365678.

    Protein family/group databases

    MEROPSi C85.004.

    PTM databases

    PhosphoSitei Q5VV17.

    Polymorphism databases

    DMDMi 74747188.

    Proteomic databases

    PaxDbi Q5VV17.
    PRIDEi Q5VV17.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000376495 ; ENSP00000365678 ; ENSG00000165312 .
    GeneIDi 220213.
    KEGGi hsa:220213.
    UCSCi uc001irr.2. human.

    Organism-specific databases

    CTDi 220213.
    GeneCardsi GC10P023768.
    HGNCi HGNC:27346. OTUD1.
    HPAi HPA038504.
    MIMi 612022. gene.
    neXtProti NX_Q5VV17.
    PharmGKBi PA134932304.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG327202.
    HOGENOMi HOG000115304.
    HOVERGENi HBG080487.
    InParanoidi Q5VV17.
    KOi K13716.
    OMAi NFRLSEH.
    OrthoDBi EOG7TBC35.
    PhylomeDBi Q5VV17.
    TreeFami TF338508.

    Miscellaneous databases

    GenomeRNAii 220213.
    NextBioi 91030.
    PROi Q5VV17.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q5VV17.
    CleanExi HS_OTUD1.
    Genevestigatori Q5VV17.

    Family and domain databases

    InterProi IPR003323. OTU.
    [Graphical view ]
    Pfami PF02338. OTU. 1 hit.
    [Graphical view ]
    PROSITEi PS50802. OTU. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis."
      Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M., Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F., Freund S.M., Ovaa H., Komander D.
      Cell 154:169-184(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 287-437, FUNCTION, CATALYTIC ACTIVITY.

    Entry informationi

    Entry nameiOTUD1_HUMAN
    AccessioniPrimary (citable) accession number: Q5VV17
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2007
    Last sequence update: December 7, 2004
    Last modified: October 1, 2014
    This is version 70 of the entry and version 1 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3