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Q96GD4

- AURKB_HUMAN

UniProt

Q96GD4 - AURKB_HUMAN

Protein

Aurora kinase B

Gene

AURKB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 3 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis. Required for central/midzone spindle assembly and cleavage furrow formation. Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: phosphorylates CHMP4C, leading to retain abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis (PubMed:22422861, PubMed:24814515). AURKB phosphorylates the CPC complex subunits BIRC5/survivin, CDCA8/borealin and INCENP. Phosphorylation of INCENP leads to increased AURKB activity. Other known AURKB substrates involved in centromeric functions and mitosis are CENPA, DES/desmin, GPAF, KIF2C, NSUN2, RACGAP1, SEPT1, VIM/vimentin, GSG2/Haspin, and histone H3. A positive feedback loop involving GSG2 and AURKB contributes to localization of CPC to centromeres. Phosphorylation of VIM controls vimentin filament segregation in cytokinetic process, whereas histone H3 is phosphorylated at 'Ser-10' and 'Ser-28' during mitosis (H3S10ph and H3S28ph, respectively). A positive feedback between GSG2 and AURKB contributes to CPC localization. AURKB is also required for kinetochore localization of BUB1 and SGOL1. Phosphorylation of p53/TP53 negatively regulates its transcriptional activity. Key regulator of active promoters in resting B- and T-lymphocytes: acts by mediating phosphorylation of H3S28ph at active promoters in resting B-cells, inhibiting RNF2/RING1B-mediated ubiquitination of histone H2A and enhancing binding and activity of the USP16 deubiquitinase at transcribed genes.19 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.

    Enzyme regulationi

    Activity is greatly increased when AURKB is within the CPC complex. In particular, AURKB-phosphorylated INCENP acts as an activator of AURKB. Positive feedback between GSG2 and AURKB contributes to CPC localization.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei106 – 1061ATPPROSITE-ProRule annotation
    Active sitei200 – 2001Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi83 – 919ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. histone serine kinase activity Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: UniProtKB
    5. protein serine/threonine/tyrosine kinase activity Source: UniProtKB
    6. protein serine/threonine kinase activity Source: FlyBase

    GO - Biological processi

    1. abscission Source: UniProtKB
    2. aging Source: Ensembl
    3. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
    4. attachment of spindle microtubules to kinetochore Source: UniProtKB
    5. cell proliferation Source: Ensembl
    6. cellular response to UV Source: UniProtKB
    7. cleavage furrow formation Source: UniProtKB
    8. cytokinesis checkpoint Source: UniProtKB
    9. histone H3-S28 phosphorylation Source: UniProtKB
    10. histone modification Source: UniProtKB
    11. mitotic cell cycle Source: Reactome
    12. negative regulation of B cell apoptotic process Source: UniProtKB
    13. negative regulation of cytokinesis Source: UniProtKB
    14. negative regulation of protein binding Source: UniProtKB
    15. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    16. positive regulation of cytokinesis Source: UniProtKB
    17. protein autophosphorylation Source: UniProtKB
    18. protein localization to kinetochore Source: UniProtKB
    19. protein phosphorylation Source: UniProtKB
    20. regulation of chromosome segregation Source: UniProtKB
    21. spindle checkpoint Source: InterPro
    22. spindle midzone assembly involved in mitosis Source: UniProtKB
    23. spindle stabilization Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_682. Mitotic Prometaphase.
    SignaLinkiQ96GD4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aurora kinase B (EC:2.7.11.1)
    Alternative name(s):
    Aurora 1
    Aurora- and IPL1-like midbody-associated protein 1
    Short name:
    AIM-1
    Aurora/IPL1-related kinase 2
    Short name:
    ARK-2
    Short name:
    Aurora-related kinase 2
    STK-1
    Serine/threonine-protein kinase 12
    Serine/threonine-protein kinase 5
    Serine/threonine-protein kinase aurora-B
    Gene namesi
    Name:AURKB
    Synonyms:AIK2, AIM1, AIRK2, ARK2, STK1, STK12, STK5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:11390. AURKB.

    Subcellular locationi

    Nucleus. Chromosome. Chromosomecentromere. Cytoplasmcytoskeletonspindle. Midbody
    Note: Localizes on chromosome arms and inner centromeres from prophase through metaphase and then transferring to the spindle midzone and midbody from anaphase through cytokinesis. Colocalized with gamma tubulin in the mid-body. Proper localization of the active, Thr-232-phosphorylated form during metaphase may be dependent upon interaction with SPDYC. Colocalized with SIRT2 during cytokinesis with the midbody.

    GO - Cellular componenti

    1. chromocenter Source: Ensembl
    2. chromosome passenger complex Source: UniProtKB
    3. condensed chromosome, centromeric region Source: UniProtKB
    4. condensed nuclear chromosome, centromeric region Source: BHF-UCL
    5. cytosol Source: Reactome
    6. intercellular bridge Source: HPA
    7. midbody Source: UniProtKB
    8. nucleus Source: UniProtKB
    9. spindle Source: UniProtKB

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Disruptive regulation of expression is a possible mechanism of the perturbation of chromosomal integrity in cancer cells through its dominant-negative effect on cytokinesis.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi106 – 1061K → R: Leads to loss of kinase activity and severely impairs mitotic progression. 4 Publications

    Organism-specific databases

    PharmGKBiPA36199.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 344344Aurora kinase BPRO_0000085656Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei35 – 351Phosphothreonine1 Publication
    Modified residuei62 – 621Phosphoserine1 Publication
    Modified residuei64 – 641Phosphothreonine1 Publication
    Modified residuei232 – 2321Phosphothreonine; by autocatalysis1 Publication

    Post-translational modificationi

    The phosphorylation of Thr-232 requires the binding to INCENP and occurs by means of an autophosphorylation mechanism. Thr-232 phosphorylation is indispensable for the AURKB kinase activity.3 Publications
    Ubiquitinated by different BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complexes. Ubiquitinated by the BCR(KLHL9-KLHL13) E3 ubiquitin ligase complex, ubiquitination leads to removal from mitotic chromosomes and is required for cytokinesis. During anaphase, the BCR(KLHL21) E3 ubiquitin ligase complex recruits the CPC complex from chromosomes to the spindle midzone and mediates the ubiquitination of AURKB. Ubiquitination of AURKB by BCR(KLHL21) E3 ubiquitin ligase complex may not lead to its degradation by the proteasome.2 Publications

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ96GD4.
    PaxDbiQ96GD4.
    PRIDEiQ96GD4.

    PTM databases

    PhosphoSiteiQ96GD4.

    Expressioni

    Tissue specificityi

    High level expression seen in the thymus. It is also expressed in the spleen, lung, testis, colon, placenta and fetal liver. Expressed during S and G2/M phase and expression is up-regulated in cancer cells during M phase.2 Publications

    Inductioni

    Expression is cell cycle-regulated, with a low in G1/S, an increase during G2 and M. Expression decreases again after M phase.1 Publication

    Gene expression databases

    ArrayExpressiQ96GD4.
    BgeeiQ96GD4.
    CleanExiHS_AIM1.
    HS_AURKB.
    GenevestigatoriQ96GD4.

    Organism-specific databases

    HPAiCAB005862.
    HPA037708.

    Interactioni

    Subunit structurei

    Component of the chromosomal passenger complex (CPC) composed of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB and AURKC. Associates with RACGAP1 during M phase. Interacts with CDCA1, EVI5, JTB, NDC80, PSMA3, SEPT1, SIRT2 and TACC1. Interacts with SPDYC; this interaction may be required for proper localization of active, Thr-232-phosphorylated AURKB form during prometaphase and metaphase. Interacts with p53/TP53. Interacts (via the middle kinase domain) with NOC2L (via the N- and C-terminus domains). Interacts with TTC28. Interacts with RNF2/RING1B.18 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BIRC5O153927EBI-624291,EBI-518823
    BIRC5O15392-12EBI-624291,EBI-518838
    BIRC5O15392-22EBI-624291,EBI-518842
    CDC37Q165432EBI-624291,EBI-295634
    GAS2L3Q86XJ14EBI-624291,EBI-9248152
    HSP90AB1P082382EBI-624291,EBI-352572
    INCENPQ9NQS77EBI-624291,EBI-307907
    NPM1P067485EBI-624291,EBI-78579
    SEPT1Q8WYJ66EBI-624291,EBI-693002
    TACC1O75410-62EBI-624291,EBI-624278

    Protein-protein interaction databases

    BioGridi114646. 84 interactions.
    DIPiDIP-34530N.
    IntActiQ96GD4. 35 interactions.
    MINTiMINT-1413997.
    STRINGi9606.ENSP00000313950.

    Structurei

    Secondary structure

    1
    344
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi74 – 763
    Beta strandi77 – 826
    Beta strandi89 – 968
    Turni97 – 993
    Beta strandi102 – 1098
    Helixi110 – 1167
    Helixi119 – 13012
    Beta strandi140 – 1456
    Beta strandi147 – 1559
    Helixi162 – 1698
    Helixi174 – 19320
    Helixi203 – 2053
    Beta strandi206 – 2083
    Beta strandi214 – 2163
    Helixi242 – 2454
    Helixi253 – 26816
    Helixi278 – 2869
    Helixi298 – 30710
    Helixi312 – 3143
    Helixi318 – 3225
    Helixi325 – 3306

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4AF3X-ray2.75A55-344[»]
    ProteinModelPortaliQ96GD4.
    SMRiQ96GD4. Positions 70-338.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini77 – 327251Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG108519.
    InParanoidiQ96GD4.
    KOiK11479.
    OMAiHPWVRAN.
    PhylomeDBiQ96GD4.
    TreeFamiTF351439.

    Family and domain databases

    InterProiIPR028772. AURKB.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PANTHERiPTHR24350:SF4. PTHR24350:SF4. 1 hit.
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96GD4-1) [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

    MAQKENSYPW PYGRQTAPSG LSTLPQRVLR KEPVTPSALV LMSRSNVQPT    50
    AAPGQKVMEN SSGTPDILTR HFTIDDFEIG RPLGKGKFGN VYLAREKKSH 100
    FIVALKVLFK SQIEKEGVEH QLRREIEIQA HLHHPNILRL YNYFYDRRRI 150
    YLILEYAPRG ELYKELQKSC TFDEQRTATI MEELADALMY CHGKKVIHRD 200
    IKPENLLLGL KGELKIADFG WSVHAPSLRR KTMCGTLDYL PPEMIEGRMH 250
    NEKVDLWCIG VLCYELLVGN PPFESASHNE TYRRIVKVDL KFPASVPMGA 300
    QDLISKLLRH NPSERLPLAQ VSAHPWVRAN SRRVLPPSAL QSVA 344
    Length:344
    Mass (Da):39,311
    Last modified:January 11, 2011 - v3
    Checksum:iA5ED13EF5A1FAFBF
    GO
    Isoform 2 (identifier: Q96GD4-2) [UniParc]FASTAAdd to Basket

    Also known as: aurkb-sv1

    The sequence of this isoform differs from the canonical sequence as follows:
         86-134: GKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHH → ALLCLWPEASSVSSPSH

    Show »
    Length:312
    Mass (Da):35,302
    Checksum:i9499DAE479793112
    GO
    Isoform 3 (identifier: Q96GD4-3) [UniParc]FASTAAdd to Basket

    Also known as: aurkb-sv2

    The sequence of this isoform differs from the canonical sequence as follows:
         69-69: T → TR
         133-141: HHPNILRLY → QSWRSWQML
         142-344: Missing.

    Note: Not expressed in normal liver, high expression in metastatic liver.

    Show »
    Length:142
    Mass (Da):16,211
    Checksum:iD8AB62DA2CCFA385
    GO
    Isoform 4 (identifier: Q96GD4-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-41: Missing.

    Show »
    Length:303
    Mass (Da):34,760
    Checksum:i301BAFF2494B3650
    GO
    Isoform 5 (identifier: Q96GD4-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         69-69: T → TR

    Show »
    Length:345
    Mass (Da):39,467
    Checksum:iACB05C191F35F38C
    GO

    Sequence cautioni

    The sequence AAH13300.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 152RQ → DK in AAC98891. 1 PublicationCurated
    Sequence conflicti161 – 1611E → M in AAB65786. (PubMed:11471245)Curated
    Sequence conflicti161 – 1611E → M in AAC98891. 1 PublicationCurated
    Sequence conflicti167 – 1693QKS → HKT in AAB65786. (PubMed:11471245)Curated
    Sequence conflicti179 – 1791T → TVRR in AAB65786. (PubMed:11471245)Curated
    Sequence conflicti180 – 1801I → VRAV in AAC98891. 1 PublicationCurated
    Sequence conflicti226 – 2261P → T in BAA82709. (PubMed:9858806)Curated
    Sequence conflicti249 – 2502MH → ID in BAA82709. (PubMed:9858806)Curated
    Sequence conflicti271 – 2711Missing in BAA82709. (PubMed:9858806)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti52 – 521A → V.1 Publication
    Corresponds to variant rs55878091 [ dbSNP | Ensembl ].
    VAR_040383
    Natural varianti100 – 1001H → Q.
    Corresponds to variant rs3027254 [ dbSNP | Ensembl ].
    VAR_027970
    Natural varianti179 – 1791T → M.1 Publication
    VAR_040384
    Natural varianti298 – 2981M → T.8 Publications
    Corresponds to variant rs1059476 [ dbSNP | Ensembl ].
    VAR_027971

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4141Missing in isoform 4. 1 PublicationVSP_047103Add
    BLAST
    Alternative sequencei69 – 691T → TR in isoform 3 and isoform 5. 2 PublicationsVSP_044384
    Alternative sequencei86 – 13449GKFGN…AHLHH → ALLCLWPEASSVSSPSH in isoform 2. 1 PublicationVSP_044385Add
    BLAST
    Alternative sequencei133 – 1419HHPNILRLY → QSWRSWQML in isoform 3. 1 PublicationVSP_044386
    Alternative sequencei142 – 344203Missing in isoform 3. 1 PublicationVSP_044387Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF008552 mRNA. Translation: AAC12709.1.
    AB011450 mRNA. Translation: BAA32136.1.
    AB011446 mRNA. Translation: BAA82709.1.
    AF004022 mRNA. Translation: AAB65786.1.
    AF015254 mRNA. Translation: AAC98891.1.
    AB519677 mRNA. Translation: BAI23190.1.
    AB519678 mRNA. Translation: BAI23191.1.
    AB519679 mRNA. Translation: BAI23192.1.
    BT019534 mRNA. Translation: AAV38341.1.
    AK297976 mRNA. Translation: BAG60286.1.
    AC135178 Genomic DNA. No translation available.
    CH471108 Genomic DNA. Translation: EAW90075.1.
    CH471108 Genomic DNA. Translation: EAW90077.1.
    CH471108 Genomic DNA. Translation: EAW90078.1.
    BC000442 mRNA. Translation: AAH00442.3.
    BC009751 mRNA. Translation: AAH09751.1.
    BC013300 mRNA. Translation: AAH13300.2. Different initiation.
    BC080581 mRNA. Translation: AAH80581.1.
    CCDSiCCDS11134.1. [Q96GD4-1]
    CCDS58514.1. [Q96GD4-4]
    CCDS67162.1. [Q96GD4-5]
    RefSeqiNP_001243763.1. NM_001256834.1. [Q96GD4-4]
    NP_001271455.1. NM_001284526.1. [Q96GD4-5]
    NP_004208.2. NM_004217.3. [Q96GD4-1]
    XP_005256911.1. XM_005256854.2. [Q96GD4-1]
    UniGeneiHs.442658.

    Genome annotation databases

    EnsembliENST00000316199; ENSP00000313950; ENSG00000178999. [Q96GD4-5]
    ENST00000534871; ENSP00000443869; ENSG00000178999. [Q96GD4-4]
    ENST00000578549; ENSP00000462207; ENSG00000178999. [Q96GD4-2]
    ENST00000585124; ENSP00000463999; ENSG00000178999. [Q96GD4-1]
    GeneIDi9212.
    KEGGihsa:9212.
    UCSCiuc002gkm.4. human. [Q96GD4-1]
    uc021tpy.1. human. [Q96GD4-2]

    Polymorphism databases

    DMDMi317373473.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF008552 mRNA. Translation: AAC12709.1 .
    AB011450 mRNA. Translation: BAA32136.1 .
    AB011446 mRNA. Translation: BAA82709.1 .
    AF004022 mRNA. Translation: AAB65786.1 .
    AF015254 mRNA. Translation: AAC98891.1 .
    AB519677 mRNA. Translation: BAI23190.1 .
    AB519678 mRNA. Translation: BAI23191.1 .
    AB519679 mRNA. Translation: BAI23192.1 .
    BT019534 mRNA. Translation: AAV38341.1 .
    AK297976 mRNA. Translation: BAG60286.1 .
    AC135178 Genomic DNA. No translation available.
    CH471108 Genomic DNA. Translation: EAW90075.1 .
    CH471108 Genomic DNA. Translation: EAW90077.1 .
    CH471108 Genomic DNA. Translation: EAW90078.1 .
    BC000442 mRNA. Translation: AAH00442.3 .
    BC009751 mRNA. Translation: AAH09751.1 .
    BC013300 mRNA. Translation: AAH13300.2 . Different initiation.
    BC080581 mRNA. Translation: AAH80581.1 .
    CCDSi CCDS11134.1. [Q96GD4-1 ]
    CCDS58514.1. [Q96GD4-4 ]
    CCDS67162.1. [Q96GD4-5 ]
    RefSeqi NP_001243763.1. NM_001256834.1. [Q96GD4-4 ]
    NP_001271455.1. NM_001284526.1. [Q96GD4-5 ]
    NP_004208.2. NM_004217.3. [Q96GD4-1 ]
    XP_005256911.1. XM_005256854.2. [Q96GD4-1 ]
    UniGenei Hs.442658.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4AF3 X-ray 2.75 A 55-344 [» ]
    ProteinModelPortali Q96GD4.
    SMRi Q96GD4. Positions 70-338.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114646. 84 interactions.
    DIPi DIP-34530N.
    IntActi Q96GD4. 35 interactions.
    MINTi MINT-1413997.
    STRINGi 9606.ENSP00000313950.

    Chemistry

    BindingDBi Q96GD4.
    ChEMBLi CHEMBL2185.
    GuidetoPHARMACOLOGYi 1937.

    PTM databases

    PhosphoSitei Q96GD4.

    Polymorphism databases

    DMDMi 317373473.

    Proteomic databases

    MaxQBi Q96GD4.
    PaxDbi Q96GD4.
    PRIDEi Q96GD4.

    Protocols and materials databases

    DNASUi 9212.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000316199 ; ENSP00000313950 ; ENSG00000178999 . [Q96GD4-5 ]
    ENST00000534871 ; ENSP00000443869 ; ENSG00000178999 . [Q96GD4-4 ]
    ENST00000578549 ; ENSP00000462207 ; ENSG00000178999 . [Q96GD4-2 ]
    ENST00000585124 ; ENSP00000463999 ; ENSG00000178999 . [Q96GD4-1 ]
    GeneIDi 9212.
    KEGGi hsa:9212.
    UCSCi uc002gkm.4. human. [Q96GD4-1 ]
    uc021tpy.1. human. [Q96GD4-2 ]

    Organism-specific databases

    CTDi 9212.
    GeneCardsi GC17M008108.
    H-InvDB HIX0019005.
    HGNCi HGNC:11390. AURKB.
    HPAi CAB005862.
    HPA037708.
    MIMi 604970. gene.
    neXtProti NX_Q96GD4.
    PharmGKBi PA36199.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG108519.
    InParanoidi Q96GD4.
    KOi K11479.
    OMAi HPWVRAN.
    PhylomeDBi Q96GD4.
    TreeFami TF351439.

    Enzyme and pathway databases

    Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_682. Mitotic Prometaphase.
    SignaLinki Q96GD4.

    Miscellaneous databases

    GeneWikii Aurora_B_kinase.
    GenomeRNAii 9212.
    NextBioi 34535.
    PROi Q96GD4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96GD4.
    Bgeei Q96GD4.
    CleanExi HS_AIM1.
    HS_AURKB.
    Genevestigatori Q96GD4.

    Family and domain databases

    InterProi IPR028772. AURKB.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    PANTHERi PTHR24350:SF4. PTHR24350:SF4. 1 hit.
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning, expression, subcellular localization, and chromosomal assignment of mammalian aurora homologues, aurora-related kinase (ARK) 1 and 2."
      Shindo M., Nakano H., Kuroyanagi H., Shirasawa T., Mihara M., Gilbert D.J., Jenkins N.A., Copeland N.G., Yagita H., Okumura K.
      Biochem. Biophys. Res. Commun. 244:285-292(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-298.
    2. "Multinuclearity and increased ploidy caused by overexpression of the aurora- and Ipl1-like midbody-associated protein mitotic kinase in human cancer cells."
      Tatsuka M., Katayama H., Ota T., Tanaka T., Odashima S., Suzuki F., Terada Y.
      Cancer Res. 58:4811-4816(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT THR-298.
    3. "Identification and characterization of STK12/Aik2: a human gene related to aurora of Drosophila and yeast IPL1."
      Kimura M., Matsuda Y., Yoshioka T., Sumi N., Okano Y.
      Cytogenet. Cell Genet. 82:147-152(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT THR-298.
      Tissue: Liver and Spleen.
    4. "In silico cloning of a new protein kinase, Aik2, related to Drosophila aurora using the new tool: EST Blast."
      Prigent C., Gill R., Trower M., Sanseau P.
      In Silico Biol. 1:123-128(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-298.
    5. "Cloning of a novel human gene homologous to mouse STK-1."
      Zhang Q., Yu L., Bi A.
      Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-298.
    6. "Expression of Aurora B and alternative variant forms in hepatocellular carcinoma and adjacent tissue."
      Yasen M., Mizushima H., Mogushi K., Obulhasim G., Miyaguchi K., Inoue K., Nakahara I., Ohta T., Aihara A., Tanaka S., Arii S., Tanaka H.
      Cancer Sci. 100:472-480(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), ALTERNATIVE SPLICING.
    7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT THR-298.
    8. "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 4).
    9. "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].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "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 5), VARIANT THR-298.
      Tissue: Lung, Lymph and Muscle.
    12. "INCENP is required for proper targeting of Survivin to the centromeres and the anaphase spindle during mitosis."
      Wheatley S.P., Carvalho A., Vagnarelli P., Earnshaw W.C.
      Curr. Biol. 11:886-890(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE CPC COMPLEX, SUBCELLULAR LOCATION, FUNCTION.
    13. "CENP-A is phosphorylated by Aurora B kinase and plays an unexpected role in completion of cytokinesis."
      Zeitlin S.G., Shelby R.D., Sullivan K.F.
      J. Cell Biol. 155:1147-1157(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    14. "Mitotic kinases as regulators of cell division and its checkpoints."
      Nigg E.A.
      Nat. Rev. Mol. Cell Biol. 2:21-32(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    15. "Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation."
      Goto H., Yasui Y., Nigg E.A., Inagaki M.
      Genes Cells 7:11-17(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
    16. "Mitotic phosphorylation of histone H3: spatio-temporal regulation by mammalian Aurora kinases."
      Crosio C., Fimia G.M., Loury R., Kimura M., Okano Y., Zhou H., Sen S., Allis C.D., Sassone-Corsi P.
      Mol. Cell. Biol. 22:874-885(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
    17. Cited for: FUNCTION, INTERACTION WITH RACGAP1.
    18. "Aurora-B regulates the cleavage furrow-specific vimentin phosphorylation in the cytokinetic process."
      Goto H., Yasui Y., Kawajiri A., Nigg E.A., Terada Y., Tatsuka M., Nagata K., Inagaki M.
      J. Biol. Chem. 278:8526-8530(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    19. "Functional significance of the specific sites phosphorylated in desmin at cleavage furrow: Aurora-B may phosphorylate and regulate type III intermediate filaments during cytokinesis coordinatedly with Rho-kinase."
      Kawajiri A., Yasui Y., Goto H., Tatsuka M., Takahashi M., Nagata K., Inagaki M.
      Mol. Biol. Cell 14:1489-1500(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-106.
    20. "Exploring the functional interactions between Aurora B, INCENP, and survivin in mitosis."
      Honda R., Korner R., Nigg E.A.
      Mol. Biol. Cell 14:3325-3341(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE CPC COMPLEX, FUNCTION OF THE CPC COMPLEX, INDUCTION, SUBCELLULAR LOCATION, ENZYME REGULATION, MUTAGENESIS OF LYS-106.
    21. "Human Aurora-B binds to a proteasome alpha-subunit HC8 and undergoes degradation in a proteasome-dependent manner."
      Shu F., Guo S., Dang Y., Qi M., Zhou G., Guo Z., Zhang Y., Wu C., Zhao S., Yu L.
      Mol. Cell. Biochem. 254:157-162(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PSMA3.
    22. "Aurora-B phosphorylation in vitro identifies a residue of survivin that is essential for its localization and binding to inner centromere protein (INCENP) in vivo."
      Wheatley S.P., Henzing A.J., Dodson H., Khaled W., Earnshaw W.C.
      J. Biol. Chem. 279:5655-5660(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    23. "Autophosphorylation of a newly identified site of Aurora-B is indispensable for cytokinesis."
      Yasui Y., Urano T., Kawajiri A., Nagata K., Tatsuka M., Saya H., Furukawa K., Takahashi T., Izawa I., Inagaki M.
      J. Biol. Chem. 279:12997-13003(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-232, FUNCTION, INTERACTION WITH INCENP, ENZYME REGULATION, MUTAGENESIS OF LYS-106.
    24. "Bub1 is required for kinetochore localization of BubR1, Cenp-E, Cenp-F and Mad2, and chromosome congression."
      Johnson V.L., Scott M.I., Holt S.V., Hussein D., Taylor S.S.
      J. Cell Sci. 117:1577-1589(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    25. "Borealin: a novel chromosomal passenger required for stability of the bipolar mitotic spindle."
      Gassmann R., Carvalho A., Henzing A.J., Ruchaud S., Hudson D.F., Honda R., Nigg E.A., Gerloff D.L., Earnshaw W.C.
      J. Cell Biol. 166:179-191(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDCA8, ENZYME REGULATION, FUNCTION.
    26. "Identification of the substrates and interaction proteins of aurora kinases from a protein-protein interaction model."
      Tien A.-C., Lin M.-H., Su L.-J., Hong Y.-R., Cheng T.-S., Lee Y.-C.G., Lin W.-J., Still I.H., Huang C.-Y.F.
      Mol. Cell. Proteomics 3:93-104(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CDCA1 AND NDC80.
    27. Cited for: INTERACTION WITH TACC1.
    28. "Septin1, a new interaction partner for human serine/threonine kinase aurora-B."
      Qi M., Yu W., Liu S., Jia H., Tang L., Shen M., Yan X., Saiyin H., Lang Q., Wan B., Zhao S., Yu L.
      Biochem. Biophys. Res. Commun. 336:994-1000(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SEPT1, MUTAGENESIS OF LYS-106.
    29. "An ECT2-centralspindlin complex regulates the localization and function of RhoA."
      Yuce O., Piekny A., Glotzer M.
      J. Cell Biol. 170:571-582(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    30. "EVI5 protein associates with the INCENP-aurora B kinase-survivin chromosomal passenger complex and is involved in the completion of cytokinesis."
      Faitar S.L., Sossey-Alaoui K., Ranalli T.A., Cowell J.K.
      Exp. Cell Res. 312:2325-2335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EVI5.
    31. "Shugoshin 1 plays a central role in kinetochore assembly and is required for kinetochore targeting of Plk1."
      Pouwels J., Kukkonen A.M., Lan W., Daum J.R., Gorbsky G.J., Stukenberg T., Kallio M.J.
      Cell Cycle 6:1579-1585(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    32. "A Cul3-based E3 ligase removes Aurora B from mitotic chromosomes, regulating mitotic progression and completion of cytokinesis in human cells."
      Sumara I., Quadroni M., Frei C., Olma M.H., Sumara G., Ricci R., Peter M.
      Dev. Cell 12:887-900(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    33. "Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during mitosis."
      North B.J., Verdin E.
      PLoS ONE 2:E784-E784(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SIRT2, SUBCELLULAR LOCATION.
    34. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    35. "A survivin-ran complex regulates spindle formation in tumor cells."
      Xia F., Canovas P.M., Guadagno T.M., Altieri D.C.
      Mol. Cell. Biol. 28:5299-5311(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BIRC5.
    36. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    37. "The Cul3-KLHL21 E3 ubiquitin ligase targets aurora B to midzone microtubules in anaphase and is required for cytokinesis."
      Maerki S., Olma M.H., Staubli T., Steigemann P., Gerlich D.W., Quadroni M., Sumara I., Peter M.
      J. Cell Biol. 187:791-800(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    38. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    39. Cited for: INTERACTION WITH SPDYC, SUBCELLULAR LOCATION.
    40. "Human POGZ modulates dissociation of HP1alpha from mitotic chromosome arms through Aurora B activation."
      Nozawa R.S., Nagao K., Masuda H.T., Iwasaki O., Hirota T., Nozaki N., Kimura H., Obuse C.
      Nat. Cell Biol. 12:719-727(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INCENP.
    41. "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-62 AND THR-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    42. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    43. "A positive feedback loop involving Haspin and Aurora B promotes CPC accumulation at centromeres in mitosis."
      Wang F., Ulyanova N.P., van der Waal M.S., Patnaik D., Lens S.M., Higgins J.M.
      Curr. Biol. 21:1061-1069(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF GSG2.
    44. "Aurora B interacts with NIR-p53, leading to p53 phosphorylation in its DNA-binding domain and subsequent functional suppression."
      Wu L., Ma C.A., Zhao Y., Jain A.
      J. Biol. Chem. 286:2236-2244(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF TP53, INTERACTION WITH NOC2L AND TP53, SUBCELLULAR LOCATION.
    45. "PAR, a protein involved in the cell cycle, is functionally related to chromosomal passenger proteins."
      Platica M., Ionescu A., Ivan E., Holland J.F., Mandeli J., Platica O.
      Int. J. Oncol. 38:777-785(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH JTB.
    46. "A novel big protein TPRBK possessing 25 units of TPR motif is essential for the progress of mitosis and cytokinesis."
      Izumiyama T., Minoshima S., Yoshida T., Shimizu N.
      Gene 511:202-217(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TTC28, SUBCELLULAR LOCATION.
    47. "ESCRT-III governs the Aurora B-mediated abscission checkpoint through CHMP4C."
      Carlton J.G., Caballe A., Agromayor M., Kloc M., Martin-Serrano J.
      Science 336:220-225(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CHMP4C.
    48. "ANCHR mediates Aurora-B-dependent abscission checkpoint control through retention of VPS4."
      Thoresen S.B., Campsteijn C., Vietri M., Schink K.O., Liestoel K., Andersen J.S., Raiborg C., Stenmark H.
      Nat. Cell Biol. 16:550-560(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    49. Cited for: VARIANT THR-298.
    50. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-52 AND MET-179.

    Entry informationi

    Entry nameiAURKB_HUMAN
    AccessioniPrimary (citable) accession number: Q96GD4
    Secondary accession number(s): B4DNM4
    , C7G533, C7G534, C7G535, D3DTR4, J9JID1, O14630, O60446, O95083, Q96DV5, Q9UQ46
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 17, 2003
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 160 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

    3D-structure, 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3