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AURKB (aurora kinase B)

Written2014-03Sai-Ching Jim Yeung
The University of Texas M. D. Anderson Cancer Center, Department of General Internal Medicine, Ambulatory Treatment, Emergency Care, Department of Endocrine Neoplasia, Hormonal Disorders, 1515 Holcombe Boulevard, Unit 1468, Houston, Texas 77230-1402, USA

(Note : for Links provided by Atlas : click)


Alias (NCBI)AIK2
HGNC Alias symbAik2
HGNC Alias nameaurora-B
 protein phosphatase 1, regulatory subunit 48
HGNC Previous nameSTK12
HGNC Previous nameserine/threonine kinase 12
LocusID (NCBI) 9212
Atlas_Id 731
Location 17p13.1  [Link to chromosome band 17p13]
Location_base_pair Starts at 8204734 and ends at 8210575 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping AURKB.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
AURKB (17p13.1)::MYH10 (17p13.1)


Description Aurora kinases are conserved during eukaryotic evolution. While the genomes of yeasts encode only one Aurora kinase (Ipl1 in budding yeast and Ark1 in fission yeast), higher eukaryotes express two or more members of this family. In mammals, there are three members (Aurora A, B and C). Aurora A (Aurora 2, ARK1, and BTAK) is present among all vertebrates. Aurora B (Aurora 1, ARK2, and AIM1) and Aurora-C (Aurora 3 and AIK3) came into existence from gene duplication during the evolution of mammals (Brown et al., 2004).


  Schematic diagram of protein domains of Aurora B kinase and some key facts. DN -K106R marks the location of amino acid K at position 106 (ATP binding site), which will produce a dominant negative protein when K is mutated to R. T at position 232 is the phosphorylation site involved in autocatalysis. The A-Box and D-Box are consensus sequences for targeted polyubiquitination (King et al., 1996; Pfleger and Kirschner, 2000), and the A-Box in Aurora B is important for Aurora B degradation (Nguyen et al., 2005).
Description Size: 344 amino acids; molecular weight: 39.3 kDa.
The AURKB gene has 8 exons, but there are 4 isoforms of AURKB protein due to alternative splicing.
The molecular structure of Aurora B has been determined by crystallography (Sessa et al., 2005; Andersen et al., 2008; Girdler et al., 2008). When the amino acid sequences of the ATP-binding pockets of Aurora A, B and C are compared, 3 of the 26 residues lining the active site in Aurora A, Leu215, Thr217 and R220, are different from the corresponding residues in Aurora B and C (Brown et al., 2004); there is no difference in these 26 residues between Aurora B and C. The manner in which Aurora A binds to ATP (Bayliss et al., 2003) and ADP (Nowakowski et al., 2002) have been modeled. Because of the high degree of conservation of the active site between Aurora A and B, Aurora B is expected to interact with ATP and ADP in the same way as reported for Aurora A.
INCENP interacts with AURKB at an α-helix domain and activates AURKB. AURKB-Sv1 lacks the INCENP interaction domain because part of exon 5 is missing and intron 5 and intron 6 may form a new domain. Therefore, the conformation of AURKB-Sv1 is expected to be different from AURKB, and the interaction with INCENP will be affected.
In contrast, the α-helix domain for interacting with INCENP is intact in AURKB-Sv2, but AURKB-Sv2 is missing major parts of the kinase domain. Thus, AURKB-Sv2 does not have kinase activity and may act as a dominant negative competitor against AURKB.
Small molecule inhibitors target the ATP-binding pocket of aurora kinases. There are data available from the Protein Data Bank website ( regarding the interaction of Aurora B with 3 inhibitors [AD6 (4-[(5-bromo-1,3-thiazol-2-yl) amino]-N-methylbenzamide): PDB ID 2vgp (Andersen et al., 2008), ZM447439: PDB ID 2vrx (Girdler et al., 2008), and hesperadin: PDB ID 2bfy (Sessa et al., 2005)].
  AURKB has 4 alternative splicing variants: the longest one (344 aa); AURKB-Sv1 (312 aa), which loses part of exon 5 but contains a fragment of intron 5 and intron 6 instead; AURKB-Sv2 (303 aa), which lacks exon 6; and the shortest form (142 aa), which loses more than the C-terminal half of the protein (López-Saavedra and Herrera, 2010). The serines and threonines are highlighted to demonstrate the alignment. Helix domains are highlighted in magenta. The active site is highlighted in red. The nucleotide binding region is indicated by the rectangle.
Expression The expression of Aurora kinases varies with cell cycle phases, being at very low levels in the non-M phases (Fu et al., 2007; Gautschi et al., 2008; Mountzios et al., 2008). Although Aurora A and Aurora B are phylogenetically related, they have different biological functions and distinct temporo-spatial subcellular localization in mammals. In prophase, Aurora A is at the centrosomes while Aurora B starts to appear in the nucleus (Carmena and Earnshaw, 2003). In metaphase, Aurora A is near the spindle poles on the microtubules ends while Aurora B is on the centromeric regions of chromosomes as a chromosomal passenger protein. In anaphase, Aurora A is at the polar microtubules while Aurora B relocates from the centromeres to the spindle midzone (spindle equator) where the microtubules from opposite poles interdigitate (Keen and Taylor, 2004). In cytokinesis, Aurora B accumulates at the cleavage furrow before finally concentrating at the midbody.
  The surface model of ZM447439 bound to Aurora B (amino acid 77-361) is rendered using the program PyMOL. ZM447439 (in stick molecular structure) is shown in the active site ATP-binding pocket of Aurora B (blue), and the 3 residues that differ between Aurora B and A are highlighted in cyan. INCENP-A (amino acid 798-840) in complex with Aurora B is hidden by coloring it black.
Localisation The protein level and kinase activity of Aurora B are tightly controlled according to the phase of the cell cycle and the stages in mitosis. It expression peaks at the G2-M transition, whereas its kinase activity and subcellular localization change quickly according to the stage of mitosis. In mitosis, Aurora B, Survivin, Borealin and INCENP form the chromosomal passenger complex (Knauer et al., 2007). It is located at the chromosomes in prophase, the centromeres in prometaphase and metaphase, the central mitotic spindle in anaphase, and the cleavage furrow in cytokinesis (Adams et al., 2001). Analysis of the dynamics of Aurora B showed that the association of Aurora B with centromeres is dynamic (Murata-Hori et al., 2002) but the association with spindle microtubules during anaphase is static. Aurora B is transported to the equatorial cell cortex by astral microtubules.
Function In mitosis, the chromosomal passenger complex, composed of Aurora B, Survivin, Borealin and INCENP, controls chromosome alignment, histone modification, and cytokinesis (Knauer et al., 2007). Presence of this complex at the right place at the right time is the key to precise control of its enzymatic core, i.e., the Aurora B kinase (Vader et al., 2006). Although Aurora B Kinase is found in complexes that contain Borealin, it is not required for the mitotic phosphorylation of Borealin (Kaur et al., 2007). Thus far, there are a number of known substrates of Aurora B: the RNA methyltransferase NSUN2 (Sakita-Suto et al., 2007), Septin-1 (Qi et al., 2005), vimentin (Goto et al., 2003), histone H3 (Sugiyama et al., 2002), MgcRacGAP (Minoshima et al., 2003), INCENP (Bishop and Schumacher, 2002; Honda et al., 2003), Survivin (Wheatley et al., 2007) and TP53 (Gully et al., 2012).
Aurora B activity is regulated in a variety of ways. It autophosphorylates at T232 through interaction with INCENP (Yasui et al., 2004). The phosphorylation of T232 is indispensable for its kinase activity. The temporo-spatial dynamics of Aurora B is determined by its binding to tubulin (Warner et al., 2006), regulation by other kinases and phosphatases (Sugiyama et al., 2002; Gruneberg et al., 2004), and proteasomal degradation after poly-ubiquitination (Nguyen et al., 2005; Stewart and Fang, 2005; Sumara et al., 2007). Survivin (Chen et al., 2003) and protein serine/threonine phosphatase type 1 (PP1) or type 2A (PP2A) (Sugiyama et al., 2002) regulate Aurora B kinase activation while MKlp2 controls Aurora B localization in anaphase (Gruneberg et al., 2004).
Regarding mitotic chromosome condensation, Aurora B directly phosphorylates histone H3, not only at S10 but also at S28. The level of S28 phosphorylation is rendered undetectable by PP1 just prior to entry into mitosis (Goto et al., 2002). Aurora B binds three other chromosome passenger proteins - inner centromere protein (INCENP), Survivin and Borealin - to form a complex that targets Aurora B to both centromeres and the spindle. The assembly of the outer kinetochore, which binds microtubules to control chromosome movement, is restricted to mitosis, whereas the inner kinetochore remains tethered to the centromeres throughout the cell cycle. Aurora B and PP1 coordinate and mediate cell cycle-dependent changes in kinetochore assembly by regulating the phosphorylation status of kinetochore substrates (Emanuele et al., 2008). The binding of mitotic checkpoint kinase Budding Uninhibited by Benzimidazoles1 beta (BubR1) to kinetochores is regulated by the survivin/Aurora B complex. Aurora B phosphorylates mitotic centromere-associated kinesin (MCAK) at merotelic attachments and regulates the microtubule depolymerase activity of MCAK (Knowlton et al., 2006). These functions of Aurora B are essential for proper chromosome segregation (Lens and Medema, 2003). Aurora B regulates the cleavage furrow-specific vimentin by phosphorylation and controls vimentin filament segregation in cytokinesis (Goto et al., 2003).
Checkpoint kinase 1 (Chk1) is a component of the DNA damage checkpoint, and it augments spindle checkpoint signaling by activating Aurora B and BubR1 (Zachos et al., 2007). Aurora B kinase activity is also regulated by poly(ADP-ribosyl)ation; activation of Poly [ADP-ribose] polymerase 1 (PARP1) in response to DNA damage will lead to a striking inhibition of Aurora B kinase activity by poly(ADP-ribosyl)ation (Monaco et al., 2005).
Homology Intriguingly, replacing the amino acid residue G198 of Aurora A with the equivalent residue N142 of Aurora B, i.e., Aurora A (G198N), makes this single amino acid mutant behave like Aurora B (Fu et al., 2009). Aurora A (G198N) is localized in the inner centromere in metaphase and the midzone in anaphase just like Aurora B, and it can compensate for the loss of Aurora B in chromosome misalignment and premature exit from mitosis. It binds to and phosphorylates INCENP and Survivin. Therefore, the presence of glycine (G) or asparagines (N) at a single site assigns Aurora A-like or B-like functions and properties (Fu et al., 2009).

Implicated in

Entity Lung adenocarcinoma
Note (Smith et al., 2005; Vischioni et al., 2006)
Prognosis High Aurora B expression predicts short survival for lung adenocarcinoma (Vischioni et al., 2006).
Oncogenesis High Aurora B expression correlates with cell proliferation, dedifferentiation, and metastasis in lung cancer patients (Vischioni et al., 2006).
Entity Acute myeloid leukemia
Note (Ikezoe et al., 2007)
Oncogenesis In an analysis comparing 44 samples of freshly isolated AML cells with 11 bone marrow mononuclear cells from healthy volunteers and 12 peripheral blood mononuclear cells from healthy volunteers, measurement of relative mRNA expression of Aurora B shows that it is upregulated in the majority of cases (Ikezoe et al., 2007). In high-risk myelodysplastic syndrome and secondary AML, surviving and aurora B are expressed in high levels in the CD34+ cells (Yoshida et al., 2012). Aurora B overexpression may have contributed to genomic instability and progression from myelodysplastic syndrome to AML.
Entity Prostate cancer
Note (Ditchfield et al., 2003; Chieffi et al., 2006)
Oncogenesis Aurora B expression correlates with prostate cancer cell proliferation (Chieffi et al., 2006).
Entity Anaplastic thyroid carcinomas
Note (Sorrentino et al., 2005)
Oncogenesis Aurora B overexpression promotes thyroid carcinoma cell proliferation and is associated with undifferentiated thyroid cancer (Sorrentino et al., 2005).
Entity Hepatocellular carcinoma
Note (Sistayanarain et al., 2006)
Prognosis High Aurora B expression predicts short survival for hepatocellular carcinoma (Tanaka et al., 2008). Yasen et al. (Yasen et al., 2009) studied the expression of the isoforms of Aurora B in 10 HCC cell lines and 253 samples from patients with varying degrees of HCC malignancy. AURKB was aberrantly expressed in HCC cell lines and primary HCC tumors.
Abnormal Protein Expression of AURKB-Sv2 is associated with advanced stages of HCC, high levels of α-fetoprotein, tumor invasion, multiple tumor formation, and shortened disease-free survival (Yasen et al., 2009). AURKB-Sv2 may be a marker of poor prognosis.
Oncogenesis Cell cycle phase-inappropriate phosphorylation of histone H3 in the entire cell cycle may enhance proliferation of liver cancer cells (Sistayanarain et al., 2006).
Entity Glioblastoma multiforme
Note (Zeng et al., 2007)
Prognosis High Aurora B expression predicts short survival for glioblastoma multiforme (Zeng et al., 2007).


Chromosomal passengers and the (aurora) ABCs of mitosis.
Adams RR, Carmena M, Earnshaw WC.
Trends Cell Biol. 2001 Feb;11(2):49-54. (REVIEW)
PMID 11166196
Discovery of selective aminothiazole aurora kinase inhibitors.
Andersen CB, Wan Y, Chang JW, Riggs B, Lee C, Liu Y, Sessa F, Villa F, Kwiatkowski N, Suzuki M, Nallan L, Heald R, Musacchio A, Gray NS.
ACS Chem Biol. 2008 Mar 20;3(3):180-92. doi: 10.1021/cb700200w. Epub 2008 Feb 29.
PMID 18307303
Structural basis of Aurora-A activation by TPX2 at the mitotic spindle.
Bayliss R, Sardon T, Vernos I, Conti E.
Mol Cell. 2003 Oct;12(4):851-62.
PMID 14580337
Phosphorylation of the carboxyl terminus of inner centromere protein (INCENP) by the Aurora B Kinase stimulates Aurora B kinase activity.
Bishop JD, Schumacher JM.
J Biol Chem. 2002 Aug 2;277(31):27577-80. Epub 2002 Jun 4.
PMID 12048181
Evolutionary relationships of Aurora kinases: implications for model organism studies and the development of anti-cancer drugs.
Brown JR, Koretke KK, Birkeland ML, Sanseau P, Patrick DR.
BMC Evol Biol. 2004 Oct 12;4:39.
PMID 15476560
The cellular geography of aurora kinases.
Carmena M, Earnshaw WC.
Nat Rev Mol Cell Biol. 2003 Nov;4(11):842-54. (REVIEW)
PMID 14625535
Survivin enhances Aurora-B kinase activity and localizes Aurora-B in human cells.
Chen J, Jin S, Tahir SK, Zhang H, Liu X, Sarthy AV, McGonigal TP, Liu Z, Rosenberg SH, Ng SC.
J Biol Chem. 2003 Jan 3;278(1):486-90. Epub 2002 Nov 4.
PMID 12419797
Aurora B expression directly correlates with prostate cancer malignancy and influence prostate cell proliferation.
Chieffi P, Cozzolino L, Kisslinger A, Libertini S, Staibano S, Mansueto G, De Rosa G, Villacci A, Vitale M, Linardopoulos S, Portella G, Tramontano D.
Prostate. 2006 Feb 15;66(3):326-33.
PMID 16267859
Aurora B couples chromosome alignment with anaphase by targeting BubR1, Mad2, and Cenp-E to kinetochores.
Ditchfield C, Johnson VL, Tighe A, Ellston R, Haworth C, Johnson T, Mortlock A, Keen N, Taylor SS.
J Cell Biol. 2003 Apr 28;161(2):267-80.
PMID 12719470
Aurora B kinase and protein phosphatase 1 have opposing roles in modulating kinetochore assembly.
Emanuele MJ, Lan W, Jwa M, Miller SA, Chan CS, Stukenberg PT.
J Cell Biol. 2008 Apr 21;181(2):241-54. doi: 10.1083/jcb.200710019.
PMID 18426974
A single amino acid change converts Aurora-A into Aurora-B-like kinase in terms of partner specificity and cellular function.
Fu J, Bian M, Liu J, Jiang Q, Zhang C.
Proc Natl Acad Sci U S A. 2009 Apr 28;106(17):6939-44. doi: 10.1073/pnas.0900833106. Epub 2009 Apr 8.
PMID 19357306
Aurora kinases as anticancer drug targets.
Gautschi O, Heighway J, Mack PC, Purnell PR, Lara PN Jr, Gandara DR.
Clin Cancer Res. 2008 Mar 15;14(6):1639-48. doi: 10.1158/1078-0432.CCR-07-2179. (REVIEW)
PMID 18347165
Molecular basis of drug resistance in aurora kinases.
Girdler F, Sessa F, Patercoli S, Villa F, Musacchio A, Taylor S.
Chem Biol. 2008 Jun;15(6):552-62. doi: 10.1016/j.chembiol.2008.04.013.
PMID 18559266
Aurora-B regulates the cleavage furrow-specific vimentin phosphorylation in the cytokinetic process.
Goto H, Yasui Y, Kawajiri A, Nigg EA, Terada Y, Tatsuka M, Nagata K, Inagaki M.
J Biol Chem. 2003 Mar 7;278(10):8526-30. Epub 2002 Nov 27.
PMID 12458200
Relocation of Aurora B from centromeres to the central spindle at the metaphase to anaphase transition requires MKlp2.
Gruneberg U, Neef R, Honda R, Nigg EA, Barr FA.
J Cell Biol. 2004 Jul 19;166(2):167-72.
PMID 15263015
Aurora B kinase phosphorylates and instigates degradation of p53.
Gully CP, Velazquez-Torres G, Shin JH, Fuentes-Mattei E, Wang E, Carlock C, Chen J, Rothenberg D, Adams HP, Choi HH, Guma S, Phan L, Chou PC, Su CH, Zhang F, Chen JS, Yang TY, Yeung SC, Lee MH.
Proc Natl Acad Sci U S A. 2012 Jun 12;109(24):E1513-22. doi: 10.1073/pnas.1110287109. Epub 2012 May 18.
PMID 22611192
Exploring the functional interactions between Aurora B, INCENP, and survivin in mitosis.
Honda R, Korner R, Nigg EA.
Mol Biol Cell. 2003 Aug;14(8):3325-41. Epub 2003 May 29.
PMID 12925766
A novel treatment strategy targeting Aurora kinases in acute myelogenous leukemia.
Ikezoe T, Yang J, Nishioka C, Tasaka T, Taniguchi A, Kuwayama Y, Komatsu N, Bandobashi K, Togitani K, Koeffler HP, Taguchi H.
Mol Cancer Ther. 2007 Jun;6(6):1851-7. Epub 2007 May 31.
PMID 17541033
Analysis of mitotic phosphorylation of borealin.
Kaur H, Stiff AC, Date DA, Taylor WR.
BMC Cell Biol. 2007 Jan 22;8:5.
PMID 17241471
Aurora-kinase inhibitors as anticancer agents.
Keen N, Taylor S.
Nat Rev Cancer. 2004 Dec;4(12):927-36. (REVIEW)
PMID 15573114
Mutagenic analysis of the destruction signal of mitotic cyclins and structural characterization of ubiquitinated intermediates.
King RW, Glotzer M, Kirschner MW.
Mol Biol Cell. 1996 Sep;7(9):1343-57.
PMID 8885231
Survivin's dual role: an export's view.
Knauer SK, Mann W, Stauber RH.
Cell Cycle. 2007 Mar 1;6(5):518-21. Epub 2007 Mar 21. (REVIEW)
PMID 17361097
Aurora B is enriched at merotelic attachment sites, where it regulates MCAK.
Knowlton AL, Lan W, Stukenberg PT.
Curr Biol. 2006 Sep 5;16(17):1705-10.
PMID 16950107
The survivin/Aurora B complex: its role in coordinating tension and attachment.
Lens SM, Medema RH.
Cell Cycle. 2003 Nov-Dec;2(6):507-10. (REVIEW)
PMID 14504461
The role of alternative mRNA splicing in chromosome instability.
Lopez-Saavedra A, Herrera LA.
Mutat Res. 2010 Dec;705(3):246-51. doi: 10.1016/j.mrrev.2010.09.002. Epub 2010 Oct 20. (REVIEW)
PMID 20932937
Phosphorylation by aurora B converts MgcRacGAP to a RhoGAP during cytokinesis.
Minoshima Y, Kawashima T, Hirose K, Tonozuka Y, Kawajiri A, Bao YC, Deng X, Tatsuka M, Narumiya S, May WS Jr, Nosaka T, Semba K, Inoue T, Satoh T, Inagaki M, Kitamura T.
Dev Cell. 2003 Apr;4(4):549-60.
PMID 12689593
Inhibition of Aurora-B kinase activity by poly(ADP-ribosyl)ation in response to DNA damage.
Monaco L, Kolthur-Seetharam U, Loury R, Murcia JM, de Murcia G, Sassone-Corsi P.
Proc Natl Acad Sci U S A. 2005 Oct 4;102(40):14244-8. Epub 2005 Sep 22.
PMID 16179389
Aurora kinases as targets for cancer therapy.
Mountzios G, Terpos E, Dimopoulos MA.
Cancer Treat Rev. 2008 Apr;34(2):175-82. Epub 2007 Nov 19. (REVIEW)
PMID 18023292
Probing the dynamics and functions of aurora B kinase in living cells during mitosis and cytokinesis.
Murata-Hori M, Tatsuka M, Wang YL.
Mol Biol Cell. 2002 Apr;13(4):1099-108.
PMID 11950924
Mechanism of Aurora-B degradation and its dependency on intact KEN and A-boxes: identification of an aneuploidy-promoting property.
Nguyen HG, Chinnappan D, Urano T, Ravid K.
Mol Cell Biol. 2005 Jun;25(12):4977-92.
PMID 15923616
Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography.
Nowakowski J, Cronin CN, McRee DE, Knuth MW, Nelson CG, Pavletich NP, Rogers J, Sang BC, Scheibe DN, Swanson RV, Thompson DA.
Structure. 2002 Dec;10(12):1659-67.
PMID 12467573
The KEN box: an APC recognition signal distinct from the D box targeted by Cdh1.
Pfleger CM, Kirschner MW.
Genes Dev. 2000 Mar 15;14(6):655-65.
PMID 10733526
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. 2005 Oct 28;336(3):994-1000.
PMID 16179162
Aurora-B regulates RNA methyltransferase NSUN2.
Sakita-Suto S, Kanda A, Suzuki F, Sato S, Takata T, Tatsuka M.
Mol Biol Cell. 2007 Mar;18(3):1107-17. Epub 2007 Jan 10.
PMID 17215513
Mechanism of Aurora B activation by INCENP and inhibition by hesperadin.
Sessa F, Mapelli M, Ciferri C, Tarricone C, Areces LB, Schneider TR, Stukenberg PT, Musacchio A.
Mol Cell. 2005 Apr 29;18(3):379-91.
PMID 15866179
Expression of Aurora-B kinase and phosphorylated histone H3 in hepatocellular carcinoma.
Sistayanarain A, Tsuneyama K, Zheng H, Takahashi H, Nomoto K, Cheng C, Murai Y, Tanaka A, Takano Y.
Anticancer Res. 2006 Sep-Oct;26(5A):3585-93.
PMID 17094487
Overexpression of aurora B kinase (AURKB) in primary non-small cell lung carcinoma is frequent, generally driven from one allele, and correlates with the level of genetic instability.
Smith SL, Bowers NL, Betticher DC, Gautschi O, Ratschiller D, Hoban PR, Booton R, Santibanez-Koref MF, Heighway J.
Br J Cancer. 2005 Sep 19;93(6):719-29.
PMID 16222316
Aurora B overexpression associates with the thyroid carcinoma undifferentiated phenotype and is required for thyroid carcinoma cell proliferation.
Sorrentino R, Libertini S, Pallante PL, Troncone G, Palombini L, Bavetsias V, Spalletti-Cernia D, Laccetti P, Linardopoulos S, Chieffi P, Fusco A, Portella G.
J Clin Endocrinol Metab. 2005 Feb;90(2):928-35. Epub 2004 Nov 23.
PMID 15562011
Destruction box-dependent degradation of aurora B is mediated by the anaphase-promoting complex/cyclosome and Cdh1.
Stewart S, Fang G.
Cancer Res. 2005 Oct 1;65(19):8730-5.
PMID 16204042
Aurora-B associated protein phosphatases as negative regulators of kinase activation.
Sugiyama K, Sugiura K, Hara T, Sugimoto K, Shima H, Honda K, Furukawa K, Yamashita S, Urano T.
Oncogene. 2002 May 9;21(20):3103-11.
PMID 12082625
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 MH, Sumara G, Ricci R, Peter M.
Dev Cell. 2007 Jun;12(6):887-900.
PMID 17543862
Aurora kinase B is a predictive factor for the aggressive recurrence of hepatocellular carcinoma after curative hepatectomy.
Tanaka S, Arii S, Yasen M, Mogushi K, Su NT, Zhao C, Imoto I, Eishi Y, Inazawa J, Miki Y, Tanaka H.
Br J Surg. 2008 May;95(5):611-9. doi: 10.1002/bjs.6011.
PMID 18311747
The chromosomal passenger complex: guiding Aurora-B through mitosis.
Vader G, Medema RH, Lens SM.
J Cell Biol. 2006 Jun 19;173(6):833-7. Epub 2006 Jun 12. (REVIEW)
PMID 16769825
Frequent overexpression of aurora B kinase, a novel drug target, in non-small cell lung carcinoma patients.
Vischioni B, Oudejans JJ, Vos W, Rodriguez JA, Giaccone G.
Mol Cancer Ther. 2006 Nov;5(11):2905-13.
PMID 17121938
Tubulin-associated drug targets: Aurora kinases, Polo-like kinases, and others.
Warner SL, Gray PJ, Von Hoff DD.
Semin Oncol. 2006 Aug;33(4):436-48. (REVIEW)
PMID 16890798
Phosphorylation by aurora-B negatively regulates survivin function during mitosis.
Wheatley SP, Barrett RM, Andrews PD, Medema RH, Morley SJ, Swedlow JR, Lens SM.
Cell Cycle. 2007 May 15;6(10):1220-30. Epub 2007 May 21.
PMID 17457057
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. 2009 Mar;100(3):472-80. doi: 10.1111/j.1349-7006.2008.01068.x. Epub 2009 Jan 2.
PMID 19134008
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. 2004 Mar 26;279(13):12997-3003. Epub 2004 Jan 13.
PMID 14722118
Marked upregulation of Survivin and Aurora-B kinase is associated with disease progression in the myelodysplastic syndromes.
Yoshida A, Zokumasu K, Wano Y, Yamauchi T, Imamura S, Takagi K, Kishi S, Urasaki Y, Tohyama K, Ueda T.
Haematologica. 2012 Sep;97(9):1372-9. doi: 10.3324/haematol.2011.055681. Epub 2012 Mar 14.
PMID 22419576
Chk1 is required for spindle checkpoint function.
Zachos G, Black EJ, Walker M, Scott MT, Vagnarelli P, Earnshaw WC, Gillespie DA.
Dev Cell. 2007 Feb;12(2):247-60.
PMID 17276342
Aurora B expression correlates with aggressive behaviour in glioblastoma multiforme.
Zeng WF, Navaratne K, Prayson RA, Weil RJ.
J Clin Pathol. 2007 Feb;60(2):218-21.
PMID 17264249


This paper should be referenced as such :
SCJ Yeung
AURKB (aurora kinase B)
Atlas Genet Cytogenet Oncol Haematol. 2014;18(12):872-878.
Free journal version : [ pdf ]   [ DOI ]

External links

HGNC (Hugo)AURKB   11390
Entrez_Gene (NCBI)AURKB    aurora kinase B
AliasesAIK2; AIM-1; AIM1; ARK-2; 
ARK2; AurB; IPL1; PPP1R48; STK-1; STK12; STK5; aurkb-sv1; aurkb-sv2
GeneCards (Weizmann)AURKB
Ensembl hg19 (Hinxton)ENSG00000178999 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000178999 [Gene_View]  ENSG00000178999 [Sequence]  chr17:8204734-8210575 [Contig_View]  AURKB [Vega]
ICGC DataPortalENSG00000178999
Genatlas (Paris)AURKB
Genetics Home Reference (NIH)AURKB
Genomic and cartography
GoldenPath hg38 (UCSC)AURKB  -     chr17:8204734-8210575 -  17p13.1   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)AURKB  -     17p13.1   [Description]    (hg19-Feb_2009)
GoldenPathAURKB - 17p13.1 [CytoView hg19]  AURKB - 17p13.1 [CytoView hg38]
Genome Data Viewer NCBIAURKB [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AB011446 AB011450 AB519677 AB519678 AB519679
RefSeq transcript (Entrez)NM_001256834 NM_001284526 NM_001313950 NM_001313951 NM_001313952 NM_001313953 NM_001313954 NM_001313955 NM_004217
Consensus coding sequences : CCDS (NCBI)AURKB
Gene Expression Viewer (FireBrowse)AURKB [ Firebrowse - Broad ]
GenevisibleExpression of AURKB in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)9212
GTEX Portal (Tissue expression)AURKB
Human Protein AtlasENSG00000178999-AURKB [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
Domain families : Pfam (Sanger)
Domain families : Pfam (NCBI)
Conserved Domain (NCBI)AURKB
Human Protein Atlas [tissue]ENSG00000178999-AURKB [tissue]
Protein Interaction databases
Complex Portal (EBI) CPX-116 Chromosomal passenger complex
Ontologies - Pathways
PubMed455 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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indexed on : Fri Oct 8 21:12:59 CEST 2021

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