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Q9C0C9

- UBE2O_HUMAN

UniProt

Q9C0C9 - UBE2O_HUMAN

Protein

E2/E3 hybrid ubiquitin-protein ligase UBE2O

Gene

UBE2O

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 3 (14 Oct 2008)
      Previous versions | rss
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    Functioni

    E2/E3 hybrid ubiquitin-protein ligase that displays both E2 and E3 ligase activities and mediates monoubiquitination of target proteins (PubMed:23455153, PubMed:24703950). Negatively regulates TRAF6-mediated NF-kappa-B activation independently of its E2 activity (PubMed:23381138). Acts as a positive regulator of BMP7 signaling by mediating monoubiquitination of SMAD6, thereby regulating adipogenesis (PubMed:23455153). Mediates monoubiquitination at different sites of the nuclear localization signal (NLS) of BAP1, leading to cytoplasmic retention of BAP1. Also able to monoubiquitinate the NLS of other chromatin-associated proteins, such as INO80 and CXXC1, affecting their subcellular location (PubMed:24703950). Acts as a regulator of retrograde transport by assisting the TRIM27:MAGEL2 E3 ubiquitin ligase complex to mediate 'Lys-63'-linked ubiquitination of WASH1, leading to promote endosomal F-actin assembly (PubMed:23452853).4 Publications

    Catalytic activityi

    ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.PROSITE-ProRule annotation

    Enzyme regulationi

    inhibited by phenylarsine oxide (PAO).1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei1040 – 10401Glycyl thioester intermediate

    GO - Molecular functioni

    1. acid-amino acid ligase activity Source: InterPro
    2. ATP binding Source: UniProtKB-KW
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: IntAct
    5. ubiquitin-protein transferase activity Source: UniProtKB

    GO - Biological processi

    1. positive regulation of BMP signaling pathway Source: UniProtKB
    2. protein K63-linked ubiquitination Source: UniProtKB
    3. protein monoubiquitination Source: UniProtKB
    4. retrograde transport, endosome to Golgi Source: UniProtKB

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Transport, Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinkiQ9C0C9.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E2/E3 hybrid ubiquitin-protein ligase UBE2O (EC:6.3.2.-, EC:6.3.2.19)
    Alternative name(s):
    Ubiquitin carrier protein O
    Ubiquitin-conjugating enzyme E2 O
    Ubiquitin-conjugating enzyme E2 of 230 kDa
    Short name:
    Ubiquitin-conjugating enzyme E2-230K
    Ubiquitin-protein ligase O
    Gene namesi
    Name:UBE2O
    Synonyms:KIAA1734
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:29554. UBE2O.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Mainly localizes to the cytoplasm.

    GO - Cellular componenti

    1. cytoplasm Source: FlyBase
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1040 – 10401C → S: Loss of function. 2 Publications

    Organism-specific databases

    PharmGKBiPA142670651.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12921292E2/E3 hybrid ubiquitin-protein ligase UBE2OPRO_0000280637Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei87 – 871Phosphoserine4 Publications
    Modified residuei89 – 891Phosphoserine4 Publications
    Modified residuei399 – 3991Phosphoserine2 Publications
    Modified residuei401 – 4011Phosphoserine2 Publications
    Modified residuei441 – 4411Phosphoserine2 Publications
    Modified residuei836 – 8361Phosphoserine3 Publications
    Modified residuei839 – 8391PhosphoserineBy similarity
    Modified residuei896 – 8961Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated. Phosphorylation affects subcellular location.5 Publications
    Ubiquitinated: autoubiquitinates, possibly affecting its subcellulat location.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9C0C9.
    PaxDbiQ9C0C9.
    PRIDEiQ9C0C9.

    PTM databases

    PhosphoSiteiQ9C0C9.

    Expressioni

    Tissue specificityi

    Predominantly expressed in skeletal muscle and heart.1 Publication

    Gene expression databases

    BgeeiQ9C0C9.
    CleanExiHS_UBE2O.
    GenevestigatoriQ9C0C9.

    Organism-specific databases

    HPAiHPA023605.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Smad6O351824EBI-2339946,EBI-4321242From a different organism.
    Smad7O352532EBI-2339946,EBI-5274835From a different organism.

    Protein-protein interaction databases

    BioGridi121973. 26 interactions.
    IntActiQ9C0C9. 25 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9C0C9.
    SMRiQ9C0C9. Positions 936-1150.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili812 – 88271Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi512 – 53625Nuclear localization signal1 PublicationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi2 – 4342Ala-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5078.
    HOVERGENiHBG080116.
    InParanoidiQ9C0C9.
    KOiK10581.
    OMAiCAQGEGS.
    OrthoDBiEOG7GN2KX.
    PhylomeDBiQ9C0C9.
    TreeFamiTF325556.

    Family and domain databases

    Gene3Di3.10.110.10. 1 hit.
    InterProiIPR000608. UBQ-conjugat_E2.
    IPR016135. UBQ-conjugating_enzyme/RWD.
    [Graphical view]
    PfamiPF00179. UQ_con. 1 hit.
    [Graphical view]
    SUPFAMiSSF54495. SSF54495. 1 hit.
    PROSITEiPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9C0C9-1 [UniParc]FASTAAdd to Basket

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    MADPAAPTPA APAPAQAPAP APEAVPAPAA APVPAPAPAS DSASGPSSDS     50
    GPEAGSQRLL FSHDLVSGRY RGSVHFGLVR LIHGEDSDSE GEEEGRGSSG 100
    CSEAGGAGHE EGRASPLRRG YVRVQWYPEG VKQHVKETKL KLEDRSVVPR 150
    DVVRHMRSTD SQCGTVIDVN IDCAVKLIGT NCIIYPVNSK DLQHIWPFMY 200
    GDYIAYDCWL GKVYDLKNQI ILKLSNGARC SMNTEDGAKL YDVCPHVSDS 250
    GLFFDDSYGF YPGQVLIGPA KIFSSVQWLS GVKPVLSTKS KFRVVVEEVQ 300
    VVELKVTWIT KSFCPGGTDS VSPPPSVITQ ENLGRVKRLG CFDHAQRQLG 350
    ERCLYVFPAK VEPAKIAWEC PEKNCAQGEG SMAKKVKRLL KKQVVRIMSC 400
    SPDTQCSRDH SMEDPDKKGE SKTKSEAESA SPEETPDGSA SPVEMQDEGA 450
    EEPHEAGEQL PPFLLKEGRD DRLHSAEQDA DDEAADDTDD TSSVTSSASS 500
    TTSSQSGSGT SRKKSIPLSI KNLKRKHKRK KNKITRDFKP GDRVAVEVVT 550
    TMTSADVMWQ DGSVECNIRS NDLFPVHHLD NNEFCPGDFV VDKRVQSCPD 600
    PAVYGVVQSG DHIGRTCMVK WFKLRPSGDD VELIGEEEDV SVYDIADHPD 650
    FRFRTTDIVI RIGNTEDGAP HKEDEPSVGQ VARVDVSSKV EVVWADNSKT 700
    IILPQHLYNI ESEIEESDYD SVEGSTSGAS SDEWEDDSDS WETDNGLVED 750
    EHPKIEEPPI PPLEQPVAPE DKGVVISEEA ATAAVQGAVA MAAPMAGLME 800
    KAGKDGPPKS FRELKEAIKI LESLKNMTVE QLLTGSPTSP TVEPEKPTRE 850
    KKFLDDIKKL QENLKKTLDN VAIVEEEKME AVPDVERKED KPEGQSPVKA 900
    EWPSETPVLC QQCGGKPGVT FTSAKGEVFS VLEFAPSNHS FKKIEFQPPE 950
    AKKFFSTVRK EMALLATSLP EGIMVKTFED RMDLFSALIK GPTRTPYEDG 1000
    LYLFDIQLPN IYPAVPPHFC YLSQCSGRLN PNLYDNGKVC VSLLGTWIGK 1050
    GTERWTSKSS LLQVLISIQG LILVNEPYYN EAGFDSDRGL QEGYENSRCY 1100
    NEMALIRVVQ SMTQLVRRPP EVFEQEIRQH FSTGGWRLVN RIESWLETHA 1150
    LLEKAQALPN GVPKASSSPE PPAVAELSDS GQQEPEDGGP APGEASQGSD 1200
    SEGGAQGLAS ASRDHTDQTS ETAPDASVPP SVKPKKRRKS YRSFLPEKSG 1250
    YPDIGFPLFP LSKGFIKSIR GVLTQFRAAL LEAGMPECTE DK 1292
    Length:1,292
    Mass (Da):141,293
    Last modified:October 14, 2008 - v3
    Checksum:iC9DF6395A32E9AB0
    GO

    Sequence cautioni

    The sequence AAH22237.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH25977.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH36820.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH51868.2 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB14320.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB14948.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB15313.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB21825.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti50 – 501S → F in BAB21825. (PubMed:11214970)Curated
    Sequence conflicti675 – 6751E → EQ in BAB15313. (PubMed:14702039)Curated
    Sequence conflicti1047 – 10471W → C in AAH22237. (PubMed:15489334)Curated
    Sequence conflicti1143 – 11431E → D in AAH25977. (PubMed:15489334)Curated
    Sequence conflicti1150 – 11501A → T in BAB14320. (PubMed:14702039)Curated
    Sequence conflicti1261 – 12611L → P in BAB14320. (PubMed:14702039)Curated
    Sequence conflicti1290 – 12901E → G in BAB14948. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1207 – 12071G → S.4 Publications
    Corresponds to variant rs3803739 [ dbSNP | Ensembl ].
    VAR_031184

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB051521 mRNA. Translation: BAB21825.1. Different initiation.
    AC090699 Genomic DNA. No translation available.
    CH471099 Genomic DNA. Translation: EAW89396.1.
    BC004525 mRNA. Translation: AAH04525.2.
    BC022237 mRNA. Translation: AAH22237.1. Different initiation.
    BC025977 mRNA. Translation: AAH25977.1. Different initiation.
    BC036820 mRNA. Translation: AAH36820.1. Different initiation.
    BC051868 mRNA. Translation: AAH51868.2. Different initiation.
    AL832432 mRNA. Translation: CAH10644.1.
    AK022940 mRNA. Translation: BAB14320.1. Different initiation.
    AK024657 mRNA. Translation: BAB14948.1. Different initiation.
    AK025999 mRNA. Translation: BAB15313.1. Different initiation.
    CCDSiCCDS32742.1.
    RefSeqiNP_071349.3. NM_022066.3.
    UniGeneiHs.16130.

    Genome annotation databases

    EnsembliENST00000319380; ENSP00000323687; ENSG00000175931.
    GeneIDi63893.
    KEGGihsa:63893.
    UCSCiuc002jrl.4. human.

    Polymorphism databases

    DMDMi209572710.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB051521 mRNA. Translation: BAB21825.1 . Different initiation.
    AC090699 Genomic DNA. No translation available.
    CH471099 Genomic DNA. Translation: EAW89396.1 .
    BC004525 mRNA. Translation: AAH04525.2 .
    BC022237 mRNA. Translation: AAH22237.1 . Different initiation.
    BC025977 mRNA. Translation: AAH25977.1 . Different initiation.
    BC036820 mRNA. Translation: AAH36820.1 . Different initiation.
    BC051868 mRNA. Translation: AAH51868.2 . Different initiation.
    AL832432 mRNA. Translation: CAH10644.1 .
    AK022940 mRNA. Translation: BAB14320.1 . Different initiation.
    AK024657 mRNA. Translation: BAB14948.1 . Different initiation.
    AK025999 mRNA. Translation: BAB15313.1 . Different initiation.
    CCDSi CCDS32742.1.
    RefSeqi NP_071349.3. NM_022066.3.
    UniGenei Hs.16130.

    3D structure databases

    ProteinModelPortali Q9C0C9.
    SMRi Q9C0C9. Positions 936-1150.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121973. 26 interactions.
    IntActi Q9C0C9. 25 interactions.

    PTM databases

    PhosphoSitei Q9C0C9.

    Polymorphism databases

    DMDMi 209572710.

    Proteomic databases

    MaxQBi Q9C0C9.
    PaxDbi Q9C0C9.
    PRIDEi Q9C0C9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000319380 ; ENSP00000323687 ; ENSG00000175931 .
    GeneIDi 63893.
    KEGGi hsa:63893.
    UCSCi uc002jrl.4. human.

    Organism-specific databases

    CTDi 63893.
    GeneCardsi GC17M074385.
    H-InvDB HIX0020035.
    HGNCi HGNC:29554. UBE2O.
    HPAi HPA023605.
    neXtProti NX_Q9C0C9.
    PharmGKBi PA142670651.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5078.
    HOVERGENi HBG080116.
    InParanoidi Q9C0C9.
    KOi K10581.
    OMAi CAQGEGS.
    OrthoDBi EOG7GN2KX.
    PhylomeDBi Q9C0C9.
    TreeFami TF325556.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki Q9C0C9.

    Miscellaneous databases

    ChiTaRSi UBE2O. human.
    GeneWikii UBE2O.
    GenomeRNAii 63893.
    NextBioi 65578.
    PROi Q9C0C9.

    Gene expression databases

    Bgeei Q9C0C9.
    CleanExi HS_UBE2O.
    Genevestigatori Q9C0C9.

    Family and domain databases

    Gene3Di 3.10.110.10. 1 hit.
    InterProi IPR000608. UBQ-conjugat_E2.
    IPR016135. UBQ-conjugating_enzyme/RWD.
    [Graphical view ]
    Pfami PF00179. UQ_con. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54495. SSF54495. 1 hit.
    PROSITEi PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
      DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-1207.
      Tissue: Brain.
    2. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(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] OF 270-1292, VARIANT SER-1207.
      Tissue: Brain and Skin.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 338-1292, VARIANT SER-1207.
      Tissue: Melanoma.
    6. "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] OF 448-1292, VARIANT SER-1207.
    7. "Identification, tissue expression, and chromosomal position of a novel gene encoding human ubiquitin-conjugating enzyme E2-230k."
      Yokota T., Nagai H., Harada H., Mine N., Terada Y., Fujiwara H., Yabe A., Miyazaki K., Emi M.
      Gene 267:95-100(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION, TISSUE SPECIFICITY.
    8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399; SER-401; SER-441 AND SER-836, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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].
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-89 AND SER-836, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87 AND SER-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-89 AND SER-896, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Regulation of WASH-dependent actin polymerization and protein trafficking by ubiquitination."
      Hao Y.H., Doyle J.M., Ramanathan S., Gomez T.S., Jia D., Xu M., Chen Z.J., Billadeau D.D., Rosen M.K., Potts P.R.
      Cell 152:1051-1064(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "UBE2O negatively regulates TRAF6-mediated NF-kappaB activation by inhibiting TRAF6 polyubiquitination."
      Zhang X., Zhang J., Zhang L., van Dam H., ten Dijke P.
      Cell Res. 23:366-377(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "Fine-tuning BMP7 signalling in adipogenesis by UBE2O/E2-230K-mediated monoubiquitination of SMAD6."
      Zhang X., Zhang J., Bauer A., Zhang L., Selinger D.W., Lu C.X., Ten Dijke P.
      EMBO J. 32:996-1007(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-1040.
    18. "Autodeubiquitination protects the tumor suppressor BAP1 from cytoplasmic sequestration mediated by the atypical ubiquitin ligase UBE2O."
      Mashtalir N., Daou S., Barbour H., Sen N.N., Gagnon J., Hammond-Martel I., Dar H.H., Therrien M., Affar E.B.
      Mol. Cell 54:392-406(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION, PHOSPHORYLATION, UBIQUITINATION, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF CYS-1040.

    Entry informationi

    Entry nameiUBE2O_HUMAN
    AccessioniPrimary (citable) accession number: Q9C0C9
    Secondary accession number(s): A6NDU5
    , Q69YP4, Q6PIZ2, Q86UA4, Q8N425, Q8TBN1, Q9BSW1, Q9H6E6, Q9H7E4, Q9H9B2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 2007
    Last sequence update: October 14, 2008
    Last modified: October 1, 2014
    This is version 108 of the entry and version 3 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 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3