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Q5VVQ6

- OTU1_HUMAN

UniProt

Q5VVQ6 - OTU1_HUMAN

Protein

Ubiquitin thioesterase OTU1

Gene

YOD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (07 Dec 2004)
      Previous versions | rss
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    Functioni

    Hydrolase that can remove conjugated ubiquitin from proteins and participates in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by triming the ubiquitin chain on the associated substrate to facilitate their threading through the VCP/p97 pore. Ubiquitin moieties on substrates may present a steric impediment to the threading process when the substrate is transferred to the VCP pore and threaded through VCP's axial channel. Mediates deubiquitination of 'Lys-27'-, 'Lys-29'- and 'Lys-33'-linked polyubiquitin chains. Also able to hydrolyze 'Lys-11'-linked ubiquitin chains. Cleaves both polyubiquitin and di-ubiquitin.2 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).2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei157 – 1571By similarity
    Active sitei160 – 1601NucleophileCurated
    Binding sitei266 – 2661Substrate; via carbonyl oxygen
    Active sitei267 – 2671By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri318 – 34225C2H2-typeAdd
    BLAST

    GO - Molecular functioni

    1. Lys48-specific deubiquitinase activity Source: ParkinsonsUK-UCL
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. ubiquitin-specific protease activity Source: UniProtKB

    GO - Biological processi

    1. cellular amino acid metabolic process Source: UniProtKB
    2. endoplasmic reticulum unfolded protein response Source: UniProtKB
    3. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
    4. protein K11-linked deubiquitination Source: UniProtKB
    5. protein K27-linked deubiquitination Source: UniProtKB
    6. protein K29-linked deubiquitination Source: UniProtKB
    7. protein K33-linked deubiquitination Source: UniProtKB
    8. protein K48-linked deubiquitination Source: UniProtKB
    9. protein K63-linked deubiquitination Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Ubl conjugation pathway, Unfolded protein response

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiC85.007.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin thioesterase OTU1 (EC:3.4.19.12)
    Alternative name(s):
    DUBA-8
    HIV-1-induced protease 7
    Short name:
    HIN-7
    Short name:
    HsHIN7
    OTU domain-containing protein 2
    Gene namesi
    Name:YOD1
    Synonyms:DUBA8, HIN7, OTUD2
    ORF Names:PRO0907
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:25035. YOD1.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi160 – 1601C → S: Abolishes deubiquitinase activity without affecting interaction with VCP. Specifically blocks a step in the course of dislocation and/or degradation of endoplasmic reticulum-resident proteins destined for proteasomal degradation. 1 Publication
    Mutagenesisi292 – 2921I → Q: Does not affect activity or specificity. Impairs ability to cleave longer 'Lys-11'-linked ubiquitin chains; when associated with Q-295. 1 Publication
    Mutagenesisi295 – 2951V → Q: Does not affect activity or specificity. Impairs ability to cleave longer 'Lys-11'-linked ubiquitin chains; when associated with Q-292. 1 Publication
    Mutagenesisi336 – 3361H → A: Reduced activity toward 'Lys-27'-, 'Lys-29'- and 'Lys-33'-linked ubiquitin without affecting activity toward 'Lys-11'-linked ubiquitin; when associated with A-342. 1 Publication
    Mutagenesisi342 – 3421H → A: Reduced activity toward 'Lys-27'-, 'Lys-29'- and 'Lys-33'-linked ubiquitin without affecting activity toward 'Lys-11'-linked ubiquitin; when associated with A-336. 1 Publication

    Organism-specific databases

    PharmGKBiPA142670552.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 348348Ubiquitin thioesterase OTU1PRO_0000282356Add
    BLAST

    Proteomic databases

    MaxQBiQ5VVQ6.
    PaxDbiQ5VVQ6.
    PRIDEiQ5VVQ6.

    PTM databases

    PhosphoSiteiQ5VVQ6.

    Expressioni

    Gene expression databases

    BgeeiQ5VVQ6.
    CleanExiHS_YOD1.
    GenevestigatoriQ5VVQ6.

    Organism-specific databases

    HPAiHPA028400.
    HPA028439.

    Interactioni

    Subunit structurei

    Interacts with VCP; the interaction is direct. Interacts with FAF2/UBXD8. Interacts with DERL1; however interaction is dependent on the UBAX-like region, suggesting that it may be indirect.2 Publications

    Protein-protein interaction databases

    BioGridi120666. 18 interactions.
    IntActiQ5VVQ6. 2 interactions.
    STRINGi9606.ENSP00000326813.

    Structurei

    Secondary structure

    1
    348
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi138 – 1403
    Beta strandi148 – 1514
    Helixi160 – 16910
    Helixi176 – 1783
    Helixi179 – 19214
    Turni194 – 1963
    Helixi199 – 2024
    Helixi206 – 2138
    Beta strandi215 – 2173
    Helixi222 – 23211
    Beta strandi234 – 2407
    Turni241 – 2444
    Beta strandi245 – 2495
    Turni250 – 2523
    Beta strandi256 – 2638
    Beta strandi268 – 2747
    Beta strandi276 – 2805
    Beta strandi285 – 2873
    Helixi292 – 30817

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4BOQX-ray1.47A132-314[»]
    4BOSX-ray2.35A/B147-314[»]
    4BOZX-ray3.03A/D132-314[»]
    ProteinModelPortaliQ5VVQ6.
    SMRiQ5VVQ6. Positions 47-132, 135-309.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini149 – 274126OTUPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni50 – 12879UBX-likeAdd
    BLAST
    Regioni154 – 1607Cys-loopBy similarity
    Regioni213 – 22311Variable-loopBy similarityAdd
    BLAST
    Regioni263 – 2675His-loopBy similarity
    Regioni291 – 2966S2 site

    Domaini

    The UBAX-like region mediates the interaction with VCP. According to PubMed:19818707, it corresponds to a UBX domain, which is a hallmark for VCP-associated proteins. However, no canonical UBX is detected by prediction tools such as Pfam or PROSITE.
    The C2H2-type zinc finger mediates specificity for 'Lys-27'-, 'Lys-29'- and 'Lys-33'-linked polyubiquitin chains but not for 'Lys-11'-linked ubiquitin chains. Selectivity for 'Lys-11'-linked ubiquitin chains is provided by recognition of the sequence surrounding 'Lys-11' in ubiquitin. The S2 site region provides specificity for longer 'Lys-11'-linked ubiquitin chains (PubMed:23827681).1 Publication

    Sequence similaritiesi

    Contains 1 C2H2-type zinc finger.Curated
    Contains 1 OTU domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri318 – 34225C2H2-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5539.
    HOGENOMiHOG000193461.
    HOVERGENiHBG097006.
    InParanoidiQ5VVQ6.
    KOiK13719.
    OMAiKSSRQFT.
    OrthoDBiEOG7J1808.
    PhylomeDBiQ5VVQ6.
    TreeFamiTF323700.

    Family and domain databases

    InterProiIPR003323. OTU.
    IPR029071. Ubiquitin-rel_dom.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    [Graphical view]
    PfamiPF02338. OTU. 1 hit.
    [Graphical view]
    SMARTiSM00355. ZnF_C2H2. 1 hit.
    [Graphical view]
    SUPFAMiSSF54236. SSF54236. 1 hit.
    PROSITEiPS50802. OTU. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q5VVQ6-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MFGPAKGRHF GVHPAPGFPG GVSQQAAGTK AGPAGAWPVG SRTDTMWRLR    50
    CKAKDGTHVL QGLSSRTRVR ELQGQIAAIT GIAPGGQRIL VGYPPECLDL 100
    SNGDTILEDL PIQSGDMLII EEDQTRPRSS PAFTKRGASS YVRETLPVLT 150
    RTVVPADNSC LFTSVYYVVE GGVLNPACAP EMRRLIAQIV ASDPDFYSEA 200
    ILGKTNQEYC DWIKRDDTWG GAIEISILSK FYQCEICVVD TQTVRIDRFG 250
    EDAGYTKRVL LIYDGIHYDP LQRNFPDPDT PPLTIFSSND DIVLVQALEL 300
    ADEARRRRQF TDVNRFTLRC MVCQKGLTGQ AEAREHAKET GHTNFGEV 348
    Length:348
    Mass (Da):38,322
    Last modified:December 7, 2004 - v1
    Checksum:i91DBD25BE85B1CCC
    GO
    Isoform 2 (identifier: Q5VVQ6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-61: MFGPAKGRHF...KAKDGTHVLQ → METLHIIYSEAKSFTVE

    Note: No experimental confirmation available.

    Show »
    Length:304
    Mass (Da):33,979
    Checksum:i8055467E0FD819CA
    GO

    Sequence cautioni

    The sequence EAW93510.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81R → G in CAD89975. (PubMed:17974005)Curated
    Sequence conflicti90 – 901L → F in BAC87233. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6161MFGPA…THVLQ → METLHIIYSEAKSFTVE in isoform 2. 1 PublicationVSP_024122Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK128014 mRNA. Translation: BAC87233.1.
    AL445493 Genomic DNA. Translation: CAH70775.1.
    AL445493 Genomic DNA. Translation: CAH70776.1.
    CH471100 Genomic DNA. Translation: EAW93509.1.
    CH471100 Genomic DNA. Translation: EAW93510.1. Sequence problems.
    BC137166 mRNA. Translation: AAI37167.1.
    BC137167 mRNA. Translation: AAI37168.1.
    AL833081 mRNA. Translation: CAD89975.1.
    AF116608 mRNA. Translation: AAF71033.1. Sequence problems.
    CCDSiCCDS31002.1. [Q5VVQ6-1]
    CCDS60402.1. [Q5VVQ6-2]
    RefSeqiNP_001263249.1. NM_001276320.1. [Q5VVQ6-2]
    NP_061036.3. NM_018566.3. [Q5VVQ6-1]
    UniGeneiHs.567533.
    Hs.745490.

    Genome annotation databases

    EnsembliENST00000315927; ENSP00000326813; ENSG00000180667. [Q5VVQ6-1]
    ENST00000367084; ENSP00000356051; ENSG00000180667. [Q5VVQ6-2]
    GeneIDi55432.
    KEGGihsa:55432.
    UCSCiuc001hfe.1. human. [Q5VVQ6-1]
    uc001hff.1. human. [Q5VVQ6-2]

    Polymorphism databases

    DMDMi74747276.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK128014 mRNA. Translation: BAC87233.1 .
    AL445493 Genomic DNA. Translation: CAH70775.1 .
    AL445493 Genomic DNA. Translation: CAH70776.1 .
    CH471100 Genomic DNA. Translation: EAW93509.1 .
    CH471100 Genomic DNA. Translation: EAW93510.1 . Sequence problems.
    BC137166 mRNA. Translation: AAI37167.1 .
    BC137167 mRNA. Translation: AAI37168.1 .
    AL833081 mRNA. Translation: CAD89975.1 .
    AF116608 mRNA. Translation: AAF71033.1 . Sequence problems.
    CCDSi CCDS31002.1. [Q5VVQ6-1 ]
    CCDS60402.1. [Q5VVQ6-2 ]
    RefSeqi NP_001263249.1. NM_001276320.1. [Q5VVQ6-2 ]
    NP_061036.3. NM_018566.3. [Q5VVQ6-1 ]
    UniGenei Hs.567533.
    Hs.745490.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4BOQ X-ray 1.47 A 132-314 [» ]
    4BOS X-ray 2.35 A/B 147-314 [» ]
    4BOZ X-ray 3.03 A/D 132-314 [» ]
    ProteinModelPortali Q5VVQ6.
    SMRi Q5VVQ6. Positions 47-132, 135-309.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120666. 18 interactions.
    IntActi Q5VVQ6. 2 interactions.
    STRINGi 9606.ENSP00000326813.

    Protein family/group databases

    MEROPSi C85.007.

    PTM databases

    PhosphoSitei Q5VVQ6.

    Polymorphism databases

    DMDMi 74747276.

    Proteomic databases

    MaxQBi Q5VVQ6.
    PaxDbi Q5VVQ6.
    PRIDEi Q5VVQ6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000315927 ; ENSP00000326813 ; ENSG00000180667 . [Q5VVQ6-1 ]
    ENST00000367084 ; ENSP00000356051 ; ENSG00000180667 . [Q5VVQ6-2 ]
    GeneIDi 55432.
    KEGGi hsa:55432.
    UCSCi uc001hfe.1. human. [Q5VVQ6-1 ]
    uc001hff.1. human. [Q5VVQ6-2 ]

    Organism-specific databases

    CTDi 55432.
    GeneCardsi GC01M207217.
    HGNCi HGNC:25035. YOD1.
    HPAi HPA028400.
    HPA028439.
    MIMi 612023. gene.
    neXtProti NX_Q5VVQ6.
    PharmGKBi PA142670552.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5539.
    HOGENOMi HOG000193461.
    HOVERGENi HBG097006.
    InParanoidi Q5VVQ6.
    KOi K13719.
    OMAi KSSRQFT.
    OrthoDBi EOG7J1808.
    PhylomeDBi Q5VVQ6.
    TreeFami TF323700.

    Miscellaneous databases

    GenomeRNAii 55432.
    NextBioi 59830.
    PROi Q5VVQ6.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q5VVQ6.
    CleanExi HS_YOD1.
    Genevestigatori Q5VVQ6.

    Family and domain databases

    InterProi IPR003323. OTU.
    IPR029071. Ubiquitin-rel_dom.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    [Graphical view ]
    Pfami PF02338. OTU. 1 hit.
    [Graphical view ]
    SMARTi SM00355. ZnF_C2H2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54236. SSF54236. 1 hit.
    PROSITEi PS50802. OTU. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Testis.
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 1).
      Tissue: Brain and Testis.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-348.
      Tissue: Spinal cord.
    6. "Gene expression profiling in human fetal liver and identification of tissue- and developmental-stage-specific genes through compiled expression profiles and efficient cloning of full-length cDNAs."
      Yu Y., Zhang C., Zhou G., Wu S., Qu X., Wei H., Xing G., Dong C., Zhai Y., Wan J., Ouyang S., Li L., Zhang S., Zhou K., Zhang Y., Wu C., He F.
      Genome Res. 11:1392-1403(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 267-348.
      Tissue: Fetal liver.
    7. "The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER."
      Ernst R., Mueller B., Ploegh H.L., Schlieker C.
      Mol. Cell 36:28-38(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME ACTIVITY, INTERACTION WITH FAF2; DERL1 AND VCP, MUTAGENESIS OF CYS-160.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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 (1.47 ANGSTROMS) OF 132-314 IN COMPLEX WITH UBIQUITINATED SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ILE-292; VAL-295; HIS-336 AND HIS-342.

    Entry informationi

    Entry nameiOTU1_HUMAN
    AccessioniPrimary (citable) accession number: Q5VVQ6
    Secondary accession number(s): B2RNX3
    , Q5VVQ5, Q6ZRS6, Q86T63, Q9P1L8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2007
    Last sequence update: December 7, 2004
    Last modified: October 1, 2014
    This is version 86 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 1
      Human chromosome 1: 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