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Q6ZPJ3

- UBE2O_MOUSE

UniProt

Q6ZPJ3 - UBE2O_MOUSE

Protein

E2/E3 hybrid ubiquitin-protein ligase UBE2O

Gene

Ube2o

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      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. Negatively regulates TRAF6-mediated NF-kappa-B activation independently of its E2 activity. Acts as a positive regulator of BMP7 signaling by mediating monoubiquitination of SMAD6, thereby regulating adipogenesis. 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. 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 By similarity.By similarity

    Catalytic activityi

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

    Enzyme regulationi

    Inhibited by inorganic arsenite such as phenylarsenoxides.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei1037 – 10371Glycyl thioester intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. acid-amino acid ligase activity Source: InterPro
    2. ATP binding Source: UniProtKB-KW
    3. 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

    Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    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 (EC:6.3.2.19)
    Ubiquitin-conjugating enzyme E2 of 230 kDa
    Short name:
    Ubiquitin-conjugating enzyme E2-230K
    Ubiquitin-protein ligase O
    Gene namesi
    Name:Ube2o
    Synonyms:Kiaa1734
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:2444266. Ube2o.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity
    Note: Mainly localizes to the cytoplasm.By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12881288E2/E3 hybrid ubiquitin-protein ligase UBE2OPRO_0000280638Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei82 – 821Phosphoserine1 Publication
    Modified residuei84 – 841Phosphoserine1 Publication
    Modified residuei394 – 3941PhosphoserineBy similarity
    Modified residuei436 – 4361PhosphoserineBy similarity
    Modified residuei833 – 8331Phosphoserine1 Publication
    Modified residuei836 – 8361Phosphoserine1 Publication
    Modified residuei893 – 8931PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated. Phosphorylation affects subcellular location By similarity.By similarity
    Ubiquitinated: autoubiquitinates, possibly affecting its subcellulat location.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ6ZPJ3.
    PaxDbiQ6ZPJ3.
    PRIDEiQ6ZPJ3.

    PTM databases

    PhosphoSiteiQ6ZPJ3.

    Expressioni

    Tissue specificityi

    Highly expressed in reticulocytes.1 Publication

    Inductioni

    By EPO/Erythropoietin which induces erythroid differentiation.1 Publication

    Gene expression databases

    BgeeiQ6ZPJ3.
    CleanExiMM_UBE2O.
    GenevestigatoriQ6ZPJ3.

    Interactioni

    Protein-protein interaction databases

    BioGridi229895. 4 interactions.
    IntActiQ6ZPJ3. 1 interaction.
    MINTiMINT-7034165.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6ZPJ3.
    SMRiQ6ZPJ3. Positions 932-1161.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili809 – 87971Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi2 – 3837Ala-richAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5078.
    GeneTreeiENSGT00730000110680.
    HOGENOMiHOG000231096.
    HOVERGENiHBG080116.
    InParanoidiA2A7X3.
    KOiK10581.
    OMAiCAQGEGS.
    OrthoDBiEOG7GN2KX.
    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.

    Q6ZPJ3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADPAAPAPA QAQAAAAPTP AAAPAAAAPP PAPATDSASG PSSDSGPEAG     50
    SQRLLFSHDL VSGRYRGSVH FGLVRLIHGE DSDSEGDDDG RGSSGCSEAG 100
    GAGHEEGRAS PLRRGYVRVQ WYPEGVKQHV KETKLKLEDR SVVPRDVVRH 150
    MRSTDSQCGT VIDVNIDCAV KLIGTNCIIY PVNSKDLQHI WPFMYGDYIA 200
    YDCWLGKVYD LKNQIILKLS NGARCSMNTE DGAKLYDVCP HVSDSGLFFD 250
    DSYGFYPGQV LIGPAKIFSS VQWLSGVKPV LSTKSKFRVV VEEVQVVELK 300
    VTWITKSFCP GGTDSVSPPP SIITQENLGR VKRLGCFDHA QRQLGERCLY 350
    VFPAKVEPAK IAWECPEKNC AQGEGSMAKK VKRLLKKQVV RIMSCTPDTQ 400
    CPRDHSMEDP DKKGEARAGS EIGSASPEEQ PDGSASPVEM QDEGSEELQE 450
    TCEPLPPFLL KEGGDDGLHS AEQDADDEAA DDTDDTSSVT SSASSTTSSQ 500
    SGSGTGRKKS IPLSIKNLKR KHKRKKNKVT RDFKPGDRVA VEVVTTMTSA 550
    DVMWQDGSVE CNIRSNDLFP VHHLDNNEFC PGDFVVDKRV QSCPDPAVYG 600
    VVQSGDHVGR TCMVKWFKLR PSGDDVELIG EEEDVSVYDI ADHPDFRFRT 650
    TDIVIRIGNT EDGALPKEDE PSVGQVARVD VSSKVEVVWA DNSKTIILPQ 700
    HLYNIESEIE ESDYDSVEGS SSGASSDEWE DDSDSWETDN GLVDDEHPKI 750
    EELAAILPAE QPTAPEEDKG VVISEEAATA AIQGAVAMAA PVAGLMEKAG 800
    KDGPPKSFRE LKEAIKILES LKNMTVEQLL TGSPTSPTVE PEKPTREKKF 850
    LDDIKKLQEN LKKTLDNVAI AEEEKMEAVP DTERKEEKPE VQSPVKAEWP 900
    SETPVLCQQC GGRPGVTFTS AKGEVFSVLE FAPSNHSFKK IEFQPPEAKK 950
    FFSTVRKEMA LLATSLPDGI MVKTFEDRMD LFSALIKGPT RTPYEDGLYL 1000
    FDIQLPNIYP AVPPHFCYLS QCSGRLNPNL YDNGKVCVSL LGTWIGKGTE 1050
    RWTSKSSLLQ VLISIQGLIL VNEPYYNEAG FDSDRGLQEG YENSRCYNEM 1100
    ALIRVVQSMT QLVRRPPEVF EQEIRQHFSV GGWRLVNRIE SWLETHAMQE 1150
    RAQVMPNGAL KDSSSLEPMA AAELSDSGRE EPEDVGMAPG EASQGSDSEG 1200
    GAQGPASASR DHTEQTETAP DASAPPSVRP KRRRKSYRSF LPEKSGYPDI 1250
    GFPLFPLSKG FIKSIRGVLT QFRAALLEAG MPESTEDK 1288
    Length:1,288
    Mass (Da):140,834
    Last modified:July 27, 2011 - v3
    Checksum:iD2BCE5F36A687CE1
    GO

    Sequence cautioni

    The sequence AAA69916.1 differs from that shown. Reason: Frameshift at positions 344, 367, 374 and 411.
    The sequence AAH59193.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAC32345.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAC98241.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti309 – 3091C → S in AAA69916. (PubMed:7761435)Curated
    Sequence conflicti317 – 3193SPP → CPR in AAA69916. (PubMed:7761435)Curated
    Sequence conflicti343 – 3431Q → H in AAA69916. (PubMed:7761435)Curated
    Sequence conflicti871 – 8711A → G in BAC32345. (PubMed:15489334)Curated
    Sequence conflicti1160 – 11601L → P in BAC98241. (PubMed:14621295)Curated
    Sequence conflicti1160 – 11601L → P in AAH59193. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK129431 mRNA. Translation: BAC98241.1. Different initiation.
    AL645851, AL607039 Genomic DNA. Translation: CAM17106.1.
    AL607039, AL645851 Genomic DNA. Translation: CAM20507.1.
    U20780 mRNA. Translation: AAA69916.1. Frameshift.
    BC059193 mRNA. Translation: AAH59193.1. Different initiation.
    AK045398 mRNA. Translation: BAC32345.1. Different initiation.
    CCDSiCCDS25670.1.
    PIRiI49264.
    RefSeqiNP_776116.2. NM_173755.3.
    UniGeneiMm.243950.

    Genome annotation databases

    EnsembliENSMUST00000082152; ENSMUSP00000080791; ENSMUSG00000020802.
    GeneIDi217342.
    KEGGimmu:217342.
    UCSCiuc007mlm.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK129431 mRNA. Translation: BAC98241.1 . Different initiation.
    AL645851 , AL607039 Genomic DNA. Translation: CAM17106.1 .
    AL607039 , AL645851 Genomic DNA. Translation: CAM20507.1 .
    U20780 mRNA. Translation: AAA69916.1 . Frameshift.
    BC059193 mRNA. Translation: AAH59193.1 . Different initiation.
    AK045398 mRNA. Translation: BAC32345.1 . Different initiation.
    CCDSi CCDS25670.1.
    PIRi I49264.
    RefSeqi NP_776116.2. NM_173755.3.
    UniGenei Mm.243950.

    3D structure databases

    ProteinModelPortali Q6ZPJ3.
    SMRi Q6ZPJ3. Positions 932-1161.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 229895. 4 interactions.
    IntActi Q6ZPJ3. 1 interaction.
    MINTi MINT-7034165.

    PTM databases

    PhosphoSitei Q6ZPJ3.

    Proteomic databases

    MaxQBi Q6ZPJ3.
    PaxDbi Q6ZPJ3.
    PRIDEi Q6ZPJ3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000082152 ; ENSMUSP00000080791 ; ENSMUSG00000020802 .
    GeneIDi 217342.
    KEGGi mmu:217342.
    UCSCi uc007mlm.1. mouse.

    Organism-specific databases

    CTDi 63893.
    MGIi MGI:2444266. Ube2o.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG5078.
    GeneTreei ENSGT00730000110680.
    HOGENOMi HOG000231096.
    HOVERGENi HBG080116.
    InParanoidi A2A7X3.
    KOi K10581.
    OMAi CAQGEGS.
    OrthoDBi EOG7GN2KX.
    TreeFami TF325556.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    ChiTaRSi UBE2O. mouse.
    NextBioi 375789.
    PROi Q6ZPJ3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q6ZPJ3.
    CleanExi MM_UBE2O.
    Genevestigatori Q6ZPJ3.

    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 mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
      DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Embryonic tail.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "Induction of ubiquitin-conjugating enzymes during terminal erythroid differentiation."
      Wefes I., Mastrandrea L.D., Haldeman M., Koury S.T., Tamburlin J., Pickart C.M., Finley D.
      Proc. Natl. Acad. Sci. U.S.A. 92:4982-4986(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 103-628, TISSUE SPECIFICITY, INDUCTION.
      Tissue: Reticulocyte.
    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 123-1288.
      Strain: FVB/N.
      Tissue: Liver.
    5. "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] OF 867-1288.
      Strain: C57BL/6J.
      Tissue: Corpora quadrigemina.
    6. "Mechanism of ubiquitin conjugating enzyme E2-230K: catalysis involving a thiol relay?"
      Berleth E.S., Pickart C.M.
      Biochemistry 35:1664-1671(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-84; SER-833 AND SER-836, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    8. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiUBE2O_MOUSE
    AccessioniPrimary (citable) accession number: Q6ZPJ3
    Secondary accession number(s): A2A7X3
    , Q60800, Q6PCR9, Q7TPN2, Q8BLE8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 2007
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 88 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3