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P63280

- UBC9_MOUSE

UniProt

P63280 - UBC9_MOUSE

Protein

SUMO-conjugating enzyme UBC9

Gene

Ube2i

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Accepts the ubiquitin-like proteins SUMO1, SUMO2 and SUMO3 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2 or CBX4. Can catalyze the formation of poly-SUMO chains. Essential for nuclear architecture, chromosome segregation and embryonic viability. Necessary for sumoylation of FOXL2 and KAT5 By similarity. Sumoylates p53/TP53 at 'Lys-386'.By similarity3 Publications

    Catalytic activityi

    ATP + SUMO + protein lysine = AMP + diphosphate + protein N-SUMOyllysine.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei4 – 41Interaction with RANBP2By similarity
    Sitei25 – 251Interaction with RANBP2By similarity
    Sitei57 – 571Interaction with RANBP2By similarity
    Active sitei93 – 931Glycyl thioester intermediate
    Sitei100 – 1012Substrate bindingBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. HLH domain binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. SUMO ligase activity Source: Ensembl
    5. ubiquitin-protein transferase activity Source: Ensembl

    GO - Biological processi

    1. cellular protein modification process Source: ProtInc
    2. chromosome segregation Source: UniProtKB-KW
    3. mitotic nuclear division Source: UniProtKB-KW
    4. multicellular organismal development Source: UniProtKB-KW
    5. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    6. positive regulation of intracellular steroid hormone receptor signaling pathway Source: Ensembl
    7. positive regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
    8. proteasome-mediated ubiquitin-dependent protein catabolic process Source: Ensembl
    9. protein sumoylation Source: UniProtKB-UniPathway
    10. regulation of receptor activity Source: Ensembl
    11. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Developmental protein, Ligase

    Keywords - Biological processi

    Cell cycle, Cell division, Chromosome partition, Host-virus interaction, Mitosis, Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_198626. Meiotic synapsis.
    REACT_223195. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
    REACT_75800. Meiotic Synapsis.
    UniPathwayiUPA00886.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SUMO-conjugating enzyme UBC9 (EC:6.3.2.-)
    Alternative name(s):
    SUMO-protein ligase
    Ubiquitin carrier protein 9
    Short name:
    mUBC9
    Ubiquitin carrier protein I
    Ubiquitin-conjugating enzyme E2 I
    Ubiquitin-protein ligase I
    Gene namesi
    Name:Ube2i
    Synonyms:Ubc9, Ubce2i, Ubce9
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:107365. Ube2i.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Mainly nuclear. In spermatocytes, localizes in synaptonemal complexes. Recruited by BCL11A into the nuclear body.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. dendrite Source: Ensembl
    3. fibrillar center Source: Ensembl
    4. nuclear body Source: UniProtKB
    5. nucleoplasm Source: Reactome
    6. PML body Source: Ensembl
    7. synapse Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Death prior to E7.5 due to major defects in nuclear organization.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 158157SUMO-conjugating enzyme UBC9PRO_0000082456Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Cross-linki18 – 18Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei65 – 651N6-acetyllysineBy similarity
    Modified residuei71 – 711Phosphoserine; by CDK1By similarity

    Post-translational modificationi

    Phosphorylation at Ser-71 significantly enhances SUMOylation activity.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP63280.
    PaxDbiP63280.
    PRIDEiP63280.

    PTM databases

    PhosphoSiteiP63280.

    Expressioni

    Tissue specificityi

    Present in spleen, kidney, lung, brain, heart and testis (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiP63280.
    BgeeiP63280.
    CleanExiMM_UBE2I.
    GenevestigatoriP63280.

    Interactioni

    Subunit structurei

    Forms a tight complex with RANGAP1 and RANBP2. Interacts with SIAH1 and PARP. Interacts with various transcription factors such as TFAP2A, TFAP2B, TFAP2C, AR, ETS1 and SOX4. Interacts with RASD2. Interacts with RWDD3; the interaction enhances the sumoylation of a number of proteins such as HIF1A and I-kappa-B. Interacts with FOXL2. Forms a complex with SENP6 and UBE2I in response to UV irradiation. Interacts with DNM1L (via its GTPase and B domains); the interaction promotes sumoylation of DNM1L, mainly in the B domain By similarity. Interacts with HIPK1, HIPK2, PPM1J and TCF3. Interacts with Moloney murine leukemia virus CA and adenovirus type 5 and type 12 E1A. Interacts with NR2C1; the interaction promotes its sumoylation. Interacts with NFATC2IP; this inhibits formation of poly-SUMO chains. Interacts with FHIT By similarity. Interacts with PRKRA and p53/TP53. Interacts with UHRF2. Interacts with NR3C1 and this interaction is enhanced in the presence of RWDD3. Interacts with MTA1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Egr2P081522EBI-80180,EBI-7070449

    Protein-protein interaction databases

    BioGridi204408. 26 interactions.
    DIPiDIP-29276N.
    IntActiP63280. 8 interactions.
    MINTiMINT-1526807.

    Structurei

    Secondary structure

    1
    158
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 1815
    Beta strandi25 – 306
    Beta strandi36 – 4611
    Turni52 – 554
    Beta strandi57 – 637
    Turni66 – 694
    Beta strandi74 – 796
    Beta strandi90 – 923
    Helixi95 – 973
    Turni99 – 1024
    Helixi109 – 12113
    Helixi131 – 1399
    Helixi141 – 15414

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1U9AX-ray2.00A1-158[»]
    1U9BX-ray2.00A1-158[»]
    2UYZX-ray1.40A1-158[»]
    2VRRX-ray2.22A1-158[»]
    ProteinModelPortaliP63280.
    SMRiP63280. Positions 1-157.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP63280.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni13 – 186Interaction with SUMO1By similarity

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5078.
    GeneTreeiENSGT00550000075088.
    HOGENOMiHOG000233454.
    HOVERGENiHBG063308.
    InParanoidiP63280.
    KOiK10577.
    OMAiWEGGVYK.
    OrthoDBiEOG7B8S5F.
    PhylomeDBiP63280.
    TreeFamiTF101122.

    Family and domain databases

    Gene3Di3.10.110.10. 1 hit.
    InterProiIPR027230. Ubc9.
    IPR000608. UBQ-conjugat_E2.
    IPR023313. UBQ-conjugating_AS.
    IPR016135. UBQ-conjugating_enzyme/RWD.
    [Graphical view]
    PANTHERiPTHR24067:SF51. PTHR24067:SF51. 1 hit.
    PfamiPF00179. UQ_con. 1 hit.
    [Graphical view]
    SUPFAMiSSF54495. SSF54495. 1 hit.
    PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
    PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P63280-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGIALSRLA QERKAWRKDH PFGFVAVPTK NPDGTMNLMN WECAIPGKKG    50
    TPWEGGLFKL RMLFKDDYPS SPPKCKFEPP LFHPNVYPSG TVCLSILEED 100
    KDWRPAITIK QILLGIQELL NEPNIQDPAQ AEAYTIYCQN RVEYEKRVRA 150
    QAKKFAPS 158
    Length:158
    Mass (Da):18,007
    Last modified:October 11, 2004 - v1
    Checksum:iE2C826E9C8D0683D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U94402 mRNA. Translation: AAB52424.1.
    X99739 mRNA. Translation: CAA68072.1.
    U31934 mRNA. Translation: AAB02182.1.
    U76416 mRNA. Translation: AAB18790.1.
    U82627 mRNA. Translation: AAB48446.1.
    X97575 mRNA. Translation: CAA66188.1.
    AK003141 mRNA. Translation: BAB22599.1.
    AK005058 mRNA. Translation: BAB23783.1.
    AK011239 mRNA. Translation: BAB27487.1.
    AK012282 mRNA. Translation: BAB28140.1.
    AK088508 mRNA. Translation: BAC40395.1.
    AK150575 mRNA. Translation: BAE29670.1.
    AK160014 mRNA. Translation: BAE35560.1.
    AK160988 mRNA. Translation: BAE36134.1.
    AK165606 mRNA. Translation: BAE38290.1.
    AK165615 mRNA. Translation: BAE38295.1.
    AK166016 mRNA. Translation: BAE38521.1.
    AK166657 mRNA. Translation: BAE38922.1.
    AK166930 mRNA. Translation: BAE39124.1.
    AK167162 mRNA. Translation: BAE39303.1.
    AK168212 mRNA. Translation: BAE40170.1.
    AK168706 mRNA. Translation: BAE40548.1.
    AK168766 mRNA. Translation: BAE40602.1.
    AY491413 Genomic DNA. Translation: AAS21651.1.
    CCDSiCCDS28513.1.
    RefSeqiNP_001171080.1. NM_001177609.1.
    NP_001171081.1. NM_001177610.1.
    NP_035795.1. NM_011665.4.
    XP_006524111.1. XM_006524048.1.
    XP_006524112.1. XM_006524049.1.
    XP_006524113.1. XM_006524050.1.
    XP_006524114.1. XM_006524051.1.
    XP_006543476.1. XM_006543413.1.
    UniGeneiMm.240044.
    Mm.384234.
    Mm.442797.

    Genome annotation databases

    EnsembliENSMUST00000049911; ENSMUSP00000055714; ENSMUSG00000015120.
    ENSMUST00000172618; ENSMUSP00000134169; ENSMUSG00000015120.
    ENSMUST00000173084; ENSMUSP00000134261; ENSMUSG00000015120.
    ENSMUST00000173713; ENSMUSP00000134491; ENSMUSG00000015120.
    ENSMUST00000174001; ENSMUSP00000134450; ENSMUSG00000015120.
    ENSMUST00000174031; ENSMUSP00000134350; ENSMUSG00000015120.
    GeneIDi102641751.
    22196.
    KEGGimmu:102641751.
    mmu:22196.
    UCSCiuc008bai.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U94402 mRNA. Translation: AAB52424.1 .
    X99739 mRNA. Translation: CAA68072.1 .
    U31934 mRNA. Translation: AAB02182.1 .
    U76416 mRNA. Translation: AAB18790.1 .
    U82627 mRNA. Translation: AAB48446.1 .
    X97575 mRNA. Translation: CAA66188.1 .
    AK003141 mRNA. Translation: BAB22599.1 .
    AK005058 mRNA. Translation: BAB23783.1 .
    AK011239 mRNA. Translation: BAB27487.1 .
    AK012282 mRNA. Translation: BAB28140.1 .
    AK088508 mRNA. Translation: BAC40395.1 .
    AK150575 mRNA. Translation: BAE29670.1 .
    AK160014 mRNA. Translation: BAE35560.1 .
    AK160988 mRNA. Translation: BAE36134.1 .
    AK165606 mRNA. Translation: BAE38290.1 .
    AK165615 mRNA. Translation: BAE38295.1 .
    AK166016 mRNA. Translation: BAE38521.1 .
    AK166657 mRNA. Translation: BAE38922.1 .
    AK166930 mRNA. Translation: BAE39124.1 .
    AK167162 mRNA. Translation: BAE39303.1 .
    AK168212 mRNA. Translation: BAE40170.1 .
    AK168706 mRNA. Translation: BAE40548.1 .
    AK168766 mRNA. Translation: BAE40602.1 .
    AY491413 Genomic DNA. Translation: AAS21651.1 .
    CCDSi CCDS28513.1.
    RefSeqi NP_001171080.1. NM_001177609.1.
    NP_001171081.1. NM_001177610.1.
    NP_035795.1. NM_011665.4.
    XP_006524111.1. XM_006524048.1.
    XP_006524112.1. XM_006524049.1.
    XP_006524113.1. XM_006524050.1.
    XP_006524114.1. XM_006524051.1.
    XP_006543476.1. XM_006543413.1.
    UniGenei Mm.240044.
    Mm.384234.
    Mm.442797.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1U9A X-ray 2.00 A 1-158 [» ]
    1U9B X-ray 2.00 A 1-158 [» ]
    2UYZ X-ray 1.40 A 1-158 [» ]
    2VRR X-ray 2.22 A 1-158 [» ]
    ProteinModelPortali P63280.
    SMRi P63280. Positions 1-157.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204408. 26 interactions.
    DIPi DIP-29276N.
    IntActi P63280. 8 interactions.
    MINTi MINT-1526807.

    Chemistry

    BindingDBi P63280.

    PTM databases

    PhosphoSitei P63280.

    Proteomic databases

    MaxQBi P63280.
    PaxDbi P63280.
    PRIDEi P63280.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000049911 ; ENSMUSP00000055714 ; ENSMUSG00000015120 .
    ENSMUST00000172618 ; ENSMUSP00000134169 ; ENSMUSG00000015120 .
    ENSMUST00000173084 ; ENSMUSP00000134261 ; ENSMUSG00000015120 .
    ENSMUST00000173713 ; ENSMUSP00000134491 ; ENSMUSG00000015120 .
    ENSMUST00000174001 ; ENSMUSP00000134450 ; ENSMUSG00000015120 .
    ENSMUST00000174031 ; ENSMUSP00000134350 ; ENSMUSG00000015120 .
    GeneIDi 102641751.
    22196.
    KEGGi mmu:102641751.
    mmu:22196.
    UCSCi uc008bai.2. mouse.

    Organism-specific databases

    CTDi 7329.
    MGIi MGI:107365. Ube2i.

    Phylogenomic databases

    eggNOGi COG5078.
    GeneTreei ENSGT00550000075088.
    HOGENOMi HOG000233454.
    HOVERGENi HBG063308.
    InParanoidi P63280.
    KOi K10577.
    OMAi WEGGVYK.
    OrthoDBi EOG7B8S5F.
    PhylomeDBi P63280.
    TreeFami TF101122.

    Enzyme and pathway databases

    UniPathwayi UPA00886 .
    Reactomei REACT_198626. Meiotic synapsis.
    REACT_223195. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
    REACT_75800. Meiotic Synapsis.

    Miscellaneous databases

    ChiTaRSi UBE2I. mouse.
    EvolutionaryTracei P63280.
    NextBioi 302181.
    PROi P63280.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P63280.
    Bgeei P63280.
    CleanExi MM_UBE2I.
    Genevestigatori P63280.

    Family and domain databases

    Gene3Di 3.10.110.10. 1 hit.
    InterProi IPR027230. Ubc9.
    IPR000608. UBQ-conjugat_E2.
    IPR023313. UBQ-conjugating_AS.
    IPR016135. UBQ-conjugating_enzyme/RWD.
    [Graphical view ]
    PANTHERi PTHR24067:SF51. PTHR24067:SF51. 1 hit.
    Pfami PF00179. UQ_con. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54495. SSF54495. 1 hit.
    PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
    PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "E3, a hematopoietic-specific transcript directly regulated by the retinoic acid receptor alpha."
      Scott L.M., Mueller L., Collins S.J.
      Blood 88:2517-2530(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: MDF1.
      Tissue: Promyelocytic leukemia.
    2. "mUBC9, a novel adenovirus E1A-interacting protein that complements a yeast cell cycle defect."
      Hateboer G., Hijmans E.M., Nooij J.B.D., Schlenker S., Jentsch S., Bernards R.
      J. Biol. Chem. 271:25906-25911(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ADENOVIRUS TYPE 5 AND TYPE 12 E1A.
    3. "Mammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51 recombination protein and localizes in synaptonemal complexes."
      Kovalenko O.V., Plug A.W., Haaf T., Gonda D.K., Ashley T., Ward D.C., Radding C.M., Golub E.I.
      Proc. Natl. Acad. Sci. U.S.A. 93:2958-2963(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
    4. "The mUBC9 murine ubiquitin conjugating enzyme interacts with the E2A transcription factors."
      Loveys D.A., Streiff M.B., Schaefer T.S., Kato G.J.
      Gene 201:169-177(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH TCF3.
      Strain: BALB/c.
      Tissue: Fibroblast.
    5. "Direct involvement of the ubiquitin-conjugating enzyme Ubc9/Hus5 in the degradation of IkappaBalpha."
      Tashiro K., Pando M.P., Kanegae Y., Wamsley P.M., Inoue S., Verma I.M.
      Proc. Natl. Acad. Sci. U.S.A. 94:7862-7867(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
      Tissue: B-cell lymphoma.
    6. Weber B.
      Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: PJS1.
    7. "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].
      Strain: BALB/c, C57BL/6J and NOD.
      Tissue: Bone marrow, Head, Heart, Kidney, Liver, Lung and Thymus.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    9. "Covalent modification of the homeodomain-interacting protein kinase 2 (HIPK2) by the ubiquitin-like protein SUMO-1."
      Kim Y.H., Choi C.Y., Kim Y.
      Proc. Natl. Acad. Sci. U.S.A. 96:12350-12355(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIPK1 AND HIPK2.
    10. "The SUMO pathway is essential for nuclear integrity and chromosome segregation in mice."
      Nacerddine K., Lehembre F., Bhaumik M., Artus J., Cohen-Tannoudji M., Babinet C., Pandolfi P.P., Dejean A.
      Dev. Cell 9:769-779(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    11. "A novel protein phosphatase 2C family member (PP2Czeta) is able to associate with ubiquitin conjugating enzyme 9."
      Kashiwaba M., Katsura K., Ohnishi M., Sasaki M., Tanaka H., Nishimune Y., Kobayashi T., Tamura S.
      FEBS Lett. 538:197-202(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPM1J.
    12. "Interaction of moloney murine leukemia virus capsid with Ubc9 and PIASy mediates SUMO-1 addition required early in infection."
      Yueh A., Leung J., Bhattacharyya S., Perrone L.A., de los Santos K., Pu S.-Y., Goff S.P.
      J. Virol. 80:342-352(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MOMLV CA.
    13. "SUMOylation of Tr2 orphan receptor involves Pml and fine-tunes Oct4 expression in stem cells."
      Park S.W., Hu X., Gupta P., Lin Y.P., Ha S.G., Wei L.N.
      Nat. Struct. Mol. Biol. 14:68-75(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NR2C1, FUNCTION IN NR2C1 SUMOYLATION.
    14. "BCL11A is a SUMOylated protein and recruits SUMO-conjugation enzymes in its nuclear body."
      Kuwata T., Nakamura T.
      Genes Cells 13:931-940(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    15. "The RAX/PACT-PKR stress response pathway promotes p53 sumoylation and activation, leading to G(1) arrest."
      Bennett R.L., Pan Y., Christian J., Hui T., May W.S. Jr.
      Cell Cycle 11:407-417(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PRKRA AND TP53.
    16. "Crystal structure of murine/human Ubc9 provides insight into the variability of the ubiquitin-conjugating system."
      Tong H., Hateboer G., Perrakis A., Bernards R., Sixma T.K.
      J. Biol. Chem. 272:21381-21387(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

    Entry informationi

    Entry nameiUBC9_MOUSE
    AccessioniPrimary (citable) accession number: P63280
    Secondary accession number(s): P50550
    , Q15698, Q6RUT3, Q86VB3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 112 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3