Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q6GQQ9

- OTU7B_HUMAN

UniProt

Q6GQQ9 - OTU7B_HUMAN

Protein

OTU domain-containing protein 7B

Gene

OTUD7B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (19 Jul 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Negative regulator of the non-canonical NF-kappa-B pathway that acts by mediating deubiquitination of TRAF3, an inhibitor of the NF-kappa-B pathway, thereby acting as a negative regulator of B-cell responses. In response to non-canonical NF-kappa-B stimuli, deubiquitinates 'Lys-48'-linked polyubiquitin chains of TRAF3, preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappa-B. Negatively regulates mucosal immunity against infections. Mediates deubiquitination of EGFR. Has deubiquitinating activity toward 'Lys-11', 'Lys-48' or 'Lys-63'-linked polyubiquitin chains. In vitro, has preference for 'Lys-11'-linked polyubiquitin chains; however such data are unsure in vivo. Hydrolyzes both linear and branched forms of polyubiquitin.6 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

    Enzyme regulationi

    Deubiquitinase activity is inhibited following interactin with PARK7.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei191 – 1911By similarity
    Active sitei194 – 1941NucleophileCurated
    Active sitei358 – 3581Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri796 – 83136A20-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. cysteine-type peptidase activity Source: UniProtKB
    2. DNA binding Source: InterPro
    3. Lys48-specific deubiquitinase activity Source: ParkinsonsUK-UCL
    4. protein binding Source: IntAct
    5. ubiquitin-specific protease activity Source: UniProtKB
    6. ubiquitin thiolesterase activity Source: UniProtKB
    7. zinc ion binding Source: InterPro

    GO - Biological processi

    1. mucosal immune response Source: UniProtKB
    2. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: HGNC
    3. negative regulation of interleukin-8 production Source: ParkinsonsUK-UCL
    4. negative regulation of protein localization to nucleus Source: ParkinsonsUK-UCL
    5. negative regulation of transcription from RNA polymerase II promoter Source: ParkinsonsUK-UCL
    6. protein K11-linked deubiquitination Source: UniProtKB
    7. protein K48-linked deubiquitination Source: UniProtKB
    8. protein K63-linked deubiquitination Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Immunity, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiQ6GQQ9.

    Protein family/group databases

    MEROPSiC64.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    OTU domain-containing protein 7B (EC:3.4.19.12)
    Alternative name(s):
    Cellular zinc finger anti-NF-kappa-B protein
    Zinc finger A20 domain-containing protein 1
    Zinc finger protein Cezanne
    Gene namesi
    Name:OTUD7B
    Synonyms:ZA20D1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:16683. OTUD7B.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Shuttles be cytoplasm and the nucleus in a XPO1/CRM1-dependent manner.

    GO - Cellular componenti

    1. cytoplasm Source: HGNC
    2. nucleus Source: HGNC

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi194 – 1941C → A: Increased ability to interact with polyubiquitin. 3 Publications
    Mutagenesisi194 – 1941C → S: Loss of deubiquitinating activity. 3 Publications
    Mutagenesisi809 – 8091F → A: Does not affect interaction with EGFR. 1 Publication
    Mutagenesisi810 – 8101Y → A: Impairs interaction with EGFR. 1 Publication

    Organism-specific databases

    PharmGKBiPA134873802.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 843843OTU domain-containing protein 7BPRO_0000188788Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei100 – 1001Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylated by EGFR.3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ6GQQ9.
    PaxDbiQ6GQQ9.
    PRIDEiQ6GQQ9.

    PTM databases

    PhosphoSiteiQ6GQQ9.

    Expressioni

    Tissue specificityi

    Widely expressed. Abundant in kidney, heart and fetal liver. Expressed differentially among B-cells at distinct developmental stages. Higher expression seen in primary immature B-cells as compared to the mature cells.2 Publications

    Inductioni

    By TNF-alpha.1 Publication

    Gene expression databases

    ArrayExpressiQ6GQQ9.
    BgeeiQ6GQQ9.
    CleanExiHS_OTUD7B.
    GenevestigatoriQ6GQQ9.

    Organism-specific databases

    HPAiHPA027045.

    Interactioni

    Subunit structurei

    Interacts with TRAF3 and TRAF6. Interacts with PARK7, leading to inhibit deubiquitinase activity. Interacts with EGFR, ITCH and NEDD4.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CCDC50Q8IVM05EBI-527784,EBI-723996
    PARK7Q994973EBI-527784,EBI-1164361

    Protein-protein interaction databases

    BioGridi121281. 13 interactions.
    DIPiDIP-33805N.
    IntActiQ6GQQ9. 13 interactions.
    STRINGi9606.ENSP00000358131.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6GQQ9.
    SMRiQ6GQQ9. Positions 1-61, 147-395.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini183 – 365183OTUPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni152 – 401250TRAF-bindingAdd
    BLAST
    Regioni167 – 440274CatalyticAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi483 – 49816Nuclear localization signalSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase C64 family.Curated
    Contains 1 A20-type zinc finger.PROSITE-ProRule annotation
    Contains 1 OTU domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri796 – 83136A20-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG282016.
    HOGENOMiHOG000048103.
    HOVERGENiHBG050904.
    InParanoidiQ6GQQ9.
    KOiK11860.
    OMAiYATFPRQ.
    OrthoDBiEOG7JHM57.
    PhylomeDBiQ6GQQ9.
    TreeFamiTF323312.

    Family and domain databases

    InterProiIPR003323. OTU.
    IPR002653. Znf_A20.
    [Graphical view]
    PfamiPF02338. OTU. 1 hit.
    [Graphical view]
    PROSITEiPS50802. OTU. 1 hit.
    PS51036. ZF_A20. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6GQQ9-1) [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

    MTLDMDAVLS DFVRSTGAEP GLARDLLEGK NWDVNAALSD FEQLRQVHAG    50
    NLPPSFSEGS GGSRTPEKGF SDREPTRPPR PILQRQDDIV QEKRLSRGIS 100
    HASSSIVSLA RSHVSSNGGG GGSNEHPLEM PICAFQLPDL TVYNEDFRSF 150
    IERDLIEQSM LVALEQAGRL NWWVSVDPTS QRLLPLATTG DGNCLLHAAS 200
    LGMWGFHDRD LMLRKALYAL MEKGVEKEAL KRRWRWQQTQ QNKESGLVYT 250
    EDEWQKEWNE LIKLASSEPR MHLGTNGANC GGVESSEEPV YESLEEFHVF 300
    VLAHVLRRPI VVVADTMLRD SGGEAFAPIP FGGIYLPLEV PASQCHRSPL 350
    VLAYDQAHFS ALVSMEQKEN TKEQAVIPLT DSEYKLLPLH FAVDPGKGWE 400
    WGKDDSDNVR LASVILSLEV KLHLLHSYMN VKWIPLSSDA QAPLAQPESP 450
    TASAGDEPRS TPESGDSDKE SVGSSSTSNE GGRRKEKSKR DREKDKKRAD 500
    SVANKLGSFG KTLGSKLKKN MGGLMHSKGS KPGGVGTGLG GSSGTETLEK 550
    KKKNSLKSWK GGKEEAAGDG PVSEKPPAES VGNGGSKYSQ EVMQSLSILR 600
    TAMQGEGKFI FVGTLKMGHR HQYQEEMIQR YLSDAEERFL AEQKQKEAER 650
    KIMNGGIGGG PPPAKKPEPD AREEQPTGPP AESRAMAFST GYPGDFTIPR 700
    PSGGGVHCQE PRRQLAGGPC VGGLPPYATF PRQCPPGRPY PHQDSIPSLE 750
    PGSHSKDGLH RGALLPPPYR VADSYSNGYR EPPEPDGWAG GLRGLPPTQT 800
    KCKQPNCSFY GHPETNNFCS CCYREELRRR EREPDGELLV HRF 843
    Length:843
    Mass (Da):92,526
    Last modified:July 19, 2004 - v1
    Checksum:i6D386C864B12EE57
    GO
    Isoform 2 (identifier: Q6GQQ9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         805-833: Missing.

    Show »
    Length:814
    Mass (Da):88,947
    Checksum:i26C3BFE215BEC0D3
    GO

    Sequence cautioni

    The sequence CAB97494.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti243 – 2431K → E in AAH20622. (PubMed:15489334)Curated
    Sequence conflicti421 – 4211K → R in AAH20622. (PubMed:15489334)Curated
    Sequence conflicti791 – 7911G → S in BAH13129. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei805 – 83329Missing in isoform 2. 1 PublicationVSP_046015Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ293573 mRNA. Translation: CAB97494.1. Different initiation.
    AK299790 mRNA. Translation: BAH13129.1.
    AL590487 Genomic DNA. Translation: CAI12651.1.
    CH471121 Genomic DNA. Translation: EAW53586.1.
    CH471121 Genomic DNA. Translation: EAW53587.1.
    BC020622 mRNA. Translation: AAH20622.1.
    BC072681 mRNA. Translation: AAH72681.1.
    AL122102 mRNA. Translation: CAB59268.1.
    CCDSiCCDS41389.1. [Q6GQQ9-1]
    PIRiT34535.
    RefSeqiNP_064590.2. NM_020205.3. [Q6GQQ9-1]
    XP_006711524.1. XM_006711461.1. [Q6GQQ9-1]
    XP_006711525.1. XM_006711462.1. [Q6GQQ9-1]
    XP_006711526.1. XM_006711463.1. [Q6GQQ9-1]
    UniGeneiHs.98322.

    Genome annotation databases

    EnsembliENST00000581312; ENSP00000462729; ENSG00000264522. [Q6GQQ9-1]
    GeneIDi56957.
    KEGGihsa:56957.
    UCSCiuc001etn.3. human. [Q6GQQ9-1]

    Polymorphism databases

    DMDMi51701318.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ293573 mRNA. Translation: CAB97494.1 . Different initiation.
    AK299790 mRNA. Translation: BAH13129.1 .
    AL590487 Genomic DNA. Translation: CAI12651.1 .
    CH471121 Genomic DNA. Translation: EAW53586.1 .
    CH471121 Genomic DNA. Translation: EAW53587.1 .
    BC020622 mRNA. Translation: AAH20622.1 .
    BC072681 mRNA. Translation: AAH72681.1 .
    AL122102 mRNA. Translation: CAB59268.1 .
    CCDSi CCDS41389.1. [Q6GQQ9-1 ]
    PIRi T34535.
    RefSeqi NP_064590.2. NM_020205.3. [Q6GQQ9-1 ]
    XP_006711524.1. XM_006711461.1. [Q6GQQ9-1 ]
    XP_006711525.1. XM_006711462.1. [Q6GQQ9-1 ]
    XP_006711526.1. XM_006711463.1. [Q6GQQ9-1 ]
    UniGenei Hs.98322.

    3D structure databases

    ProteinModelPortali Q6GQQ9.
    SMRi Q6GQQ9. Positions 1-61, 147-395.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121281. 13 interactions.
    DIPi DIP-33805N.
    IntActi Q6GQQ9. 13 interactions.
    STRINGi 9606.ENSP00000358131.

    Protein family/group databases

    MEROPSi C64.001.

    PTM databases

    PhosphoSitei Q6GQQ9.

    Polymorphism databases

    DMDMi 51701318.

    Proteomic databases

    MaxQBi Q6GQQ9.
    PaxDbi Q6GQQ9.
    PRIDEi Q6GQQ9.

    Protocols and materials databases

    DNASUi 56957.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000581312 ; ENSP00000462729 ; ENSG00000264522 . [Q6GQQ9-1 ]
    GeneIDi 56957.
    KEGGi hsa:56957.
    UCSCi uc001etn.3. human. [Q6GQQ9-1 ]

    Organism-specific databases

    CTDi 56957.
    GeneCardsi GC01M149912.
    HGNCi HGNC:16683. OTUD7B.
    HPAi HPA027045.
    MIMi 611748. gene.
    neXtProti NX_Q6GQQ9.
    PharmGKBi PA134873802.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG282016.
    HOGENOMi HOG000048103.
    HOVERGENi HBG050904.
    InParanoidi Q6GQQ9.
    KOi K11860.
    OMAi YATFPRQ.
    OrthoDBi EOG7JHM57.
    PhylomeDBi Q6GQQ9.
    TreeFami TF323312.

    Enzyme and pathway databases

    SignaLinki Q6GQQ9.

    Miscellaneous databases

    ChiTaRSi OTUD7B. human.
    GeneWikii OTUD7B.
    GenomeRNAii 56957.
    NextBioi 35479876.
    PROi Q6GQQ9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6GQQ9.
    Bgeei Q6GQQ9.
    CleanExi HS_OTUD7B.
    Genevestigatori Q6GQQ9.

    Family and domain databases

    InterProi IPR003323. OTU.
    IPR002653. Znf_A20.
    [Graphical view ]
    Pfami PF02338. OTU. 1 hit.
    [Graphical view ]
    PROSITEi PS50802. OTU. 1 hit.
    PS51036. ZF_A20. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of two novel A20-like proteins."
      Evans P.C., Taylor E.R., Coadwell J., Heyninck K., Beyaert R., Kilshaw P.J.
      Biochem. J. 357:617-623(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH TRAF6.
      Tissue: Lymphocyte.
    2. "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: Brain.
    3. "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].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Eye and Prostate.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 437-843.
      Tissue: Testis.
    7. Cited for: FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-194.
    8. "Zinc-finger protein A20, a regulator of inflammation and cell survival, has de-ubiquitinating activity."
      Evans P.C., Ovaa H., Hamon M., Kilshaw P.J., Hamm S., Bauer S., Ploegh H.L., Smith T.S.
      Biochem. J. 378:727-734(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-194.
    9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "NF-kappaB suppression by the deubiquitinating enzyme Cezanne: a novel negative feedback loop in pro-inflammatory signaling."
      Enesa K., Zakkar M., Chaudhury H., Luong le A., Rawlinson L., Mason J.C., Haskard D.O., Dean J.L., Evans P.C.
      J. Biol. Chem. 283:7036-7045(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    11. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne."
      Bremm A., Freund S.M., Komander D.
      Nat. Struct. Mol. Biol. 17:939-947(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "DJ-1 enhances cell survival through the binding of cezanne, a negative regulator of NF-{kappa}B."
      McNally R.S., Davis B.K., Clements C.M., Accavitti-Loper M.A., Mak T.W., Ting J.P.
      J. Biol. Chem. 286:4098-4106(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, INTERACTION WITH PARK7.
    18. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "A global survey of CRM1-dependent nuclear export sequences in the human deubiquitinase family."
      Garcia-Santisteban I., Banuelos S., Rodriguez J.A.
      Biochem. J. 441:209-217(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    20. Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH EGFR; ITCH AND NEDD4, MUTAGENESIS OF CYS-194; PHE-809 AND TYR-810.
    21. "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: FUNCTION, CATALYTIC ACTIVITY.

    Entry informationi

    Entry nameiOTU7B_HUMAN
    AccessioniPrimary (citable) accession number: Q6GQQ9
    Secondary accession number(s): B7Z643
    , D3DUZ8, Q5SZ60, Q8WWA7, Q9NQ53, Q9UFF4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 31, 2004
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 113 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

    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. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3