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O43684

- BUB3_HUMAN

UniProt

O43684 - BUB3_HUMAN

Protein

Mitotic checkpoint protein BUB3

Gene

BUB3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    Functioni

    Has a dual function in spindle-assembly checkpoint signaling and in promoting the establishment of correct kinetochore-microtubule (K-MT) attachments. Promotes the formation of stable end-on bipolar attachments. Necessary for kinetochore localization of BUB1. Regulates chromosome segregation during oocyte meiosis. The BUB1/BUB3 complex plays a role in the inhibition of anaphase-promoting complex or cyclosome (APC/C) when spindle-assembly checkpoint is activated and inhibits the ubiquitin ligase activity of APC/C by phosphorylating its activator CDC20. This complex can also phosphorylate MAD1L1.3 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
    2. attachment of spindle microtubules to kinetochore Source: UniProtKB
    3. meiotic nuclear division Source: UniProtKB-KW
    4. mitotic cell cycle Source: Reactome
    5. mitotic sister chromatid segregation Source: Ensembl
    6. mitotic spindle assembly checkpoint Source: Reactome
    7. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    8. regulation of chromosome segregation Source: Ensembl
    9. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    10. spindle assembly checkpoint Source: UniProtKB

    Keywords - Biological processi

    Cell cycle, Cell division, Chromosome partition, Meiosis, Mitosis

    Enzyme and pathway databases

    ReactomeiREACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
    REACT_682. Mitotic Prometaphase.
    SignaLinkiO43684.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitotic checkpoint protein BUB3
    Gene namesi
    Name:BUB3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:1151. BUB3.

    Subcellular locationi

    Nucleus. Chromosomecentromerekinetochore By similarity
    Note: Starts to localize at kinetochores in prometaphase I (Pro-MI) stage and maintains the localization until the metaphase I-anaphase I (MI-AI) transition.By similarity

    GO - Cellular componenti

    1. condensed chromosome kinetochore Source: UniProtKB-SubCell
    2. cytosol Source: Reactome
    3. kinetochore Source: UniProtKB
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Centromere, Chromosome, Kinetochore, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti1052. Mosaic variegated aneuploidy syndrome.
    PharmGKBiPA25467.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 328328Mitotic checkpoint protein BUB3PRO_0000050891Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei179 – 1791N6-acetyllysine1 Publication
    Modified residuei211 – 2111Phosphoserine1 Publication
    Cross-linki216 – 216Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

    Post-translational modificationi

    Poly-ADP-ribosylated by PARP1.By similarity

    Keywords - PTMi

    Acetylation, ADP-ribosylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO43684.
    PaxDbiO43684.
    PRIDEiO43684.

    PTM databases

    PhosphoSiteiO43684.

    Expressioni

    Gene expression databases

    ArrayExpressiO43684.
    BgeeiO43684.
    CleanExiHS_BUB3.
    GenevestigatoriO43684.

    Organism-specific databases

    HPAiCAB037075.
    HPA003601.

    Interactioni

    Subunit structurei

    Interacts with BUB1 and BUBR1. The BUB1/BUB3 complex interacts with MAD1L1. Interacts with ZNF207/BuGZ; leading to promote stability and kinetochore loading of BUB3.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BUB1BO605662EBI-1050987,EBI-1001438
    Dynlt3Q5XI902EBI-1050987,EBI-1781818From a different organism.

    Protein-protein interaction databases

    BioGridi114621. 44 interactions.
    DIPiDIP-24205N.
    IntActiO43684. 33 interactions.
    MINTiMINT-5005850.
    STRINGi9606.ENSP00000357858.

    Structurei

    3D structure databases

    ProteinModelPortaliO43684.
    SMRiO43684. Positions 6-324.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati5 – 4339WD 1Add
    BLAST
    Repeati46 – 8338WD 2Add
    BLAST
    Repeati86 – 12439WD 3Add
    BLAST
    Repeati128 – 16336WD 4Add
    BLAST
    Repeati223 – 26240WD 5Add
    BLAST

    Sequence similaritiesi

    Belongs to the WD repeat BUB3 family.Curated
    Contains 5 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    HOGENOMiHOG000208822.
    HOVERGENiHBG002942.
    InParanoidiO43684.
    KOiK02180.
    OMAiKCHRQTI.
    OrthoDBiEOG7J4472.
    PhylomeDBiO43684.
    TreeFamiTF105454.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    InterProiIPR020472. G-protein_beta_WD-40_rep.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PfamiPF00400. WD40. 3 hits.
    [Graphical view]
    PRINTSiPR00320. GPROTEINBRPT.
    SMARTiSM00320. WD40. 6 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 1 hit.
    PROSITEiPS50082. WD_REPEATS_2. 2 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O43684-1) [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

    MTGSNEFKLN QPPEDGISSV KFSPNTSQFL LVSSWDTSVR LYDVPANSMR    50
    LKYQHTGAVL DCAFYDPTHA WSGGLDHQLK MHDLNTDQEN LVGTHDAPIR 100
    CVEYCPEVNV MVTGSWDQTV KLWDPRTPCN AGTFSQPEKV YTLSVSGDRL 150
    IVGTAGRRVL VWDLRNMGYV QQRRESSLKY QTRCIRAFPN KQGYVLSSIE 200
    GRVAVEYLDP SPEVQKKKYA FKCHRLKENN IEQIYPVNAI SFHNIHNTFA 250
    TGGSDGFVNI WDPFNKKRLC QFHRYPTSIA SLAFSNDGTT LAIASSYMYE 300
    MDDTEHPEDG IFIRQVTDAE TKPKSPCT 328
    Length:328
    Mass (Da):37,155
    Last modified:June 1, 1998 - v1
    Checksum:i2915572A57368E5A
    GO
    Isoform 2 (identifier: O43684-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         326-328: PCT → T

    Show »
    Length:326
    Mass (Da):36,955
    Checksum:iF1EA57368E5A6345
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei326 – 3283PCT → T in isoform 2. 1 PublicationVSP_038655

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF047472 mRNA. Translation: AAC28438.1.
    AF047473 mRNA. Translation: AAC28439.1.
    AF053304 mRNA. Translation: AAC06258.1.
    AF081496 mRNA. Translation: AAC36307.1.
    AK312546 mRNA. Translation: BAG35444.1.
    AC012391 Genomic DNA. No translation available.
    CH471066 Genomic DNA. Translation: EAW49284.1.
    CH471066 Genomic DNA. Translation: EAW49285.1.
    CH471066 Genomic DNA. Translation: EAW49286.1.
    BC005138 mRNA. Translation: AAH05138.1.
    BC022438 mRNA. Translation: AAH22438.1.
    CCDSiCCDS31306.1. [O43684-2]
    CCDS7635.1. [O43684-1]
    RefSeqiNP_001007794.1. NM_001007793.2. [O43684-2]
    NP_004716.1. NM_004725.3. [O43684-1]
    UniGeneiHs.418533.

    Genome annotation databases

    EnsembliENST00000368858; ENSP00000357851; ENSG00000154473. [O43684-2]
    ENST00000368865; ENSP00000357858; ENSG00000154473. [O43684-1]
    GeneIDi9184.
    KEGGihsa:9184.
    UCSCiuc001lhd.2. human. [O43684-2]
    uc001lhe.2. human. [O43684-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF047472 mRNA. Translation: AAC28438.1 .
    AF047473 mRNA. Translation: AAC28439.1 .
    AF053304 mRNA. Translation: AAC06258.1 .
    AF081496 mRNA. Translation: AAC36307.1 .
    AK312546 mRNA. Translation: BAG35444.1 .
    AC012391 Genomic DNA. No translation available.
    CH471066 Genomic DNA. Translation: EAW49284.1 .
    CH471066 Genomic DNA. Translation: EAW49285.1 .
    CH471066 Genomic DNA. Translation: EAW49286.1 .
    BC005138 mRNA. Translation: AAH05138.1 .
    BC022438 mRNA. Translation: AAH22438.1 .
    CCDSi CCDS31306.1. [O43684-2 ]
    CCDS7635.1. [O43684-1 ]
    RefSeqi NP_001007794.1. NM_001007793.2. [O43684-2 ]
    NP_004716.1. NM_004725.3. [O43684-1 ]
    UniGenei Hs.418533.

    3D structure databases

    ProteinModelPortali O43684.
    SMRi O43684. Positions 6-324.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114621. 44 interactions.
    DIPi DIP-24205N.
    IntActi O43684. 33 interactions.
    MINTi MINT-5005850.
    STRINGi 9606.ENSP00000357858.

    PTM databases

    PhosphoSitei O43684.

    Proteomic databases

    MaxQBi O43684.
    PaxDbi O43684.
    PRIDEi O43684.

    Protocols and materials databases

    DNASUi 9184.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368858 ; ENSP00000357851 ; ENSG00000154473 . [O43684-2 ]
    ENST00000368865 ; ENSP00000357858 ; ENSG00000154473 . [O43684-1 ]
    GeneIDi 9184.
    KEGGi hsa:9184.
    UCSCi uc001lhd.2. human. [O43684-2 ]
    uc001lhe.2. human. [O43684-1 ]

    Organism-specific databases

    CTDi 9184.
    GeneCardsi GC10P124903.
    HGNCi HGNC:1151. BUB3.
    HPAi CAB037075.
    HPA003601.
    MIMi 603719. gene.
    neXtProti NX_O43684.
    Orphaneti 1052. Mosaic variegated aneuploidy syndrome.
    PharmGKBi PA25467.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2319.
    HOGENOMi HOG000208822.
    HOVERGENi HBG002942.
    InParanoidi O43684.
    KOi K02180.
    OMAi KCHRQTI.
    OrthoDBi EOG7J4472.
    PhylomeDBi O43684.
    TreeFami TF105454.

    Enzyme and pathway databases

    Reactomei REACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
    REACT_682. Mitotic Prometaphase.
    SignaLinki O43684.

    Miscellaneous databases

    ChiTaRSi Bub3. human.
    GeneWikii BUB3.
    GenomeRNAii 9184.
    NextBioi 34433.
    PROi O43684.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43684.
    Bgeei O43684.
    CleanExi HS_BUB3.
    Genevestigatori O43684.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    InterProi IPR020472. G-protein_beta_WD-40_rep.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    Pfami PF00400. WD40. 3 hits.
    [Graphical view ]
    PRINTSi PR00320. GPROTEINBRPT.
    SMARTi SM00320. WD40. 6 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 1 hit.
    PROSITEi PS50082. WD_REPEATS_2. 2 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Phosphorylation of human MAD1 by the BUB1 kinase in vitro."
      Seeley T.W., Wang L., Zhen J.Y.
      Biochem. Biophys. Res. Commun. 257:589-595(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH BUB1 AND MAD1L1.
      Tissue: Spleen and Testis.
    2. "The human homologue of Bub3 is required for kinetochore localization of Bub1 and a Mad3/Bub1-related protein kinase."
      Taylor S.S., Ha E., McKeon F.
      J. Cell Biol. 142:1-11(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Human BUB3 is a kinetochore protein that interacts with hBUB1 and hBUBR1."
      Chan G.K.T., Yen T.J.
      Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "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 1).
      Tissue: Tongue.
    5. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 Placenta.
    8. "Phosphorylation of Cdc20 by Bub1 provides a catalytic mechanism for APC/C inhibition by the spindle checkpoint."
      Tang Z., Shu H., Oncel D., Chen S., Yu H.
      Mol. Cell 16:387-397(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BUB1.
    9. "The human spindle assembly checkpoint protein Bub3 is required for the establishment of efficient kinetochore-microtubule attachments."
      Logarinho E., Resende T., Torres C., Bousbaa H.
      Mol. Biol. Cell 19:1798-1813(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "A microtubule-associated zinc finger protein, BuGZ, regulates mitotic chromosome alignment by ensuring Bub3 stability and kinetochore targeting."
      Jiang H., He X., Wang S., Jia J., Wan Y., Wang Y., Zeng R., Yates J. III, Zhu X., Zheng Y.
      Dev. Cell 28:268-281(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZNF207.
    14. "BuGZ is required for Bub3 stability, Bub1 kinetochore function, and chromosome alignment."
      Toledo C.M., Herman J.A., Olsen J.B., Ding Y., Corrin P., Girard E.J., Olson J.M., Emili A., Deluca J.G., Paddison P.J.
      Dev. Cell 28:282-294(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZNF207.

    Entry informationi

    Entry nameiBUB3_HUMAN
    AccessioniPrimary (citable) accession number: O43684
    Secondary accession number(s): A6NJ42
    , B2R6E7, D3DRE9, O43685
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 136 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 10
      Human chromosome 10: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3