Q96GD4 (AURKB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	AURKB
Synonyms:	AIK2, AIM1, AIRK2, ARK2, STK1, STK12, STK5

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	344 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. 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. 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. Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.27 Ref.29 Ref.41 Ref.42
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium.
Enzyme regulation	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. Ref.18 Ref.21 Ref.23
Subunit structure	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 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). Ref.15 Ref.19 Ref.21 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28 Ref.31 Ref.39 Ref.40 Ref.42 Ref.43
Subcellular location	Nucleus. Chromosome. Chromosome › centromere. Cytoplasm › cytoskeleton › spindle. 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. Ref.10 Ref.11 Ref.16 Ref.18 Ref.26 Ref.39 Ref.42
Tissue specificity	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. Ref.2 Ref.3
Induction	Expression is cell cycle-regulated, with a low in G1/S, an increase during G2 and M. Expression decreases again after M phase. Ref.18 Ref.21 Ref.23
Post-translational modification	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. 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. Ref.30 Ref.37
Involvement in disease	Note=Disruptive regulation of expression is a possibile mechanism of the perturbation of chromosomal integrity in cancer cells through its dominant-negative effect on cytokinesis.
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily. Contains 1 protein kinase domain.
Sequence caution	The sequence AAH13300.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Centromere Chromosome Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Traceable author statement. Source: Reactome attachment of spindle microtubules to kinetochore Traceable author statement. Source: UniProtKB cellular response to UV Inferred from direct assay Ref.42. Source: UniProtKB histone modification Traceable author statement. Source: UniProtKB mitotic prometaphase Traceable author statement. Source: Reactome negative regulation of B cell apoptosis Inferred from direct assay Ref.42. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.42. Source: UniProtKB positive regulation of cell cycle cytokinesis Inferred from mutant phenotype Ref.27. Source: UniProtKB protein autophosphorylation Traceable author statement. Source: UniProtKB protein localization to kinetochore Inferred from mutant phenotype. Source: UniProtKB regulation of chromosome segregation Traceable author statement. Source: UniProtKB spindle midzone assembly involved in mitosis Inferred from mutant phenotype Ref.27. Source: UniProtKB
Cellular component	chromosome passenger complex Inferred from physical interaction Ref.31. Source: UniProtKB condensed nuclear chromosome, centromeric region Inferred from direct assay. Source: BHF-UCL cytosol Traceable author statement. Source: Reactome midbody Traceable author statement. Source: UniProtKB spindle Traceable author statement. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.15Ref.42. Source: UniProtKB protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine/tyrosine kinase activity Traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BIRC5	O15392	2	EBI-624291,EBI-518823
BIRC5	O15392-1	2	EBI-624291,EBI-518838
BIRC5	O15392-2	2	EBI-624291,EBI-518842
INCENP	Q9NQS7	3	EBI-624291,EBI-307907
SEPT1	Q8WYJ6	6	EBI-624291,EBI-693002
TACC1	O75410-6	2	EBI-624291,EBI-624278

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 344	343	Aurora kinase B		PRO_0000085656
Regions
	Domain	77 – 327	251	Protein kinase
	Nucleotide binding	83 – 91	9	ATP By similarity
Sites
	Active site	200	1	Proton acceptor By similarity
	Binding site	106	1	ATP By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.33
	Modified residue	7	1	Phosphoserine Ref.32 Ref.33 Ref.35
	Modified residue	12	1	Phosphotyrosine Ref.32
	Modified residue	16	1	Phosphothreonine Ref.33
	Modified residue	35	1	Phosphothreonine Ref.33 Ref.35 Ref.36
	Modified residue	45	1	Phosphoserine Ref.33 Ref.35
	Modified residue	61	1	Phosphoserine Ref.33 Ref.35 Ref.38
	Modified residue	62	1	Phosphoserine Ref.33
	Modified residue	64	1	Phosphothreonine Ref.33 Ref.35
	Modified residue	92	1	Phosphotyrosine Ref.35
	Modified residue	227	1	Phosphoserine Ref.35
	Modified residue	232	1	Phosphothreonine; by autocatalysis Ref.21 Ref.32 Ref.34 Ref.35
	Modified residue	236	1	Phosphothreonine Ref.35
	Modified residue	313	1	Phosphoserine Ref.35
Natural variations
	Natural variant	52	1	A → V. Ref.45		VAR_040383
	Natural variant	100	1	H → Q. Corresponds to variant rs3027254 [ dbSNP | Ensembl ].		VAR_027970
	Natural variant	179	1	T → M. Ref.45		VAR_040384
	Natural variant	298	1	M → T. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.9 Ref.44 Corresponds to variant rs1059476 [ dbSNP | Ensembl ].		VAR_027971
Experimental info
	Mutagenesis	106	1	K → R: Leads to loss of kinase activity and severely impairs mitotic progression. Ref.17 Ref.18 Ref.21 Ref.26
	Sequence conflict	14 – 15	2	RQ → DK in AAC98891. Ref.5
	Sequence conflict	70	1	R → RR in AAH13300. Ref.9
	Sequence conflict	161	1	E → M in AAB65786. Ref.4
	Sequence conflict	161	1	E → M in AAC98891. Ref.5
	Sequence conflict	167 – 169	3	QKS → HKT in AAB65786. Ref.4
	Sequence conflict	179	1	T → TVRR in AAB65786. Ref.4
	Sequence conflict	180	1	I → VRAV in AAC98891. Ref.5
	Sequence conflict	226	1	P → T in BAA82709. Ref.3
	Sequence conflict	249 – 250	2	MH → ID in BAA82709. Ref.3
	Sequence conflict	271	1	Missing in BAA82709. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q96GD4 [UniParc]. Last modified January 11, 2011. Version 3. Checksum: A5ED13EF5A1FAFBF	FASTA	344	39,311
	10 20 30 40 50 60 MAQKENSYPW PYGRQTAPSG LSTLPQRVLR KEPVTPSALV LMSRSNVQPT AAPGQKVMEN 70 80 90 100 110 120 SSGTPDILTR HFTIDDFEIG RPLGKGKFGN VYLAREKKSH FIVALKVLFK SQIEKEGVEH 130 140 150 160 170 180 QLRREIEIQA HLHHPNILRL YNYFYDRRRI YLILEYAPRG ELYKELQKSC TFDEQRTATI 190 200 210 220 230 240 MEELADALMY CHGKKVIHRD IKPENLLLGL KGELKIADFG WSVHAPSLRR KTMCGTLDYL 250 260 270 280 290 300 PPEMIEGRMH NEKVDLWCIG VLCYELLVGN PPFESASHNE TYRRIVKVDL KFPASVPMGA 310 320 330 340 QDLISKLLRH NPSERLPLAQ VSAHPWVRAN SRRVLPPSAL QSVA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9514916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 9809983] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 9858806] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 11471245] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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], VARIANT THR-298.
[6]	"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], VARIANT THR-298.
[7]	"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: 16625196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-298. Tissue: Lung, Lymph and Muscle.
[10]	"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: 11516652] [Abstract] Cited for: IDENTIFICATION IN THE CPC COMPLEX, SUBCELLULAR LOCATION, FUNCTION.
[11]	"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: 11756469] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[12]	"Mitotic kinases as regulators of cell division and its checkpoints." Nigg E.A. Nat. Rev. Mol. Cell Biol. 2:21-32(2001) [PubMed: 11413462] [Abstract] Cited for: REVIEW.
[13]	"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: 11856369] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
[14]	"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: 11784863] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
[15]	"Phosphorylation by aurora B converts MgcRacGAP to a RhoGAP during cytokinesis." Minoshima Y., Kawashima T., Hirose K., Tonozuka Y., Kawajiri A., Bao Y.C., Deng X., Tatsuka M., Narumiya S., May W.S. Jr., Nosaka T., Semba K., Inoue T., Satoh T., Inagaki M., Kitamura T. Dev. Cell 4:549-560(2003) [PubMed: 12689593] [Abstract] Cited for: FUNCTION, INTERACTION WITH RACGAP1.
[16]	"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: 12458200] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[17]	"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: 12686604] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF LYS-106.
[18]	"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: 12925766] [Abstract] Cited for: IDENTIFICATION IN THE CPC COMPLEX, FUNCTION OF THE CPC COMPLEX, INDUCTION, SUBCELLULAR LOCATION, ENZYME REGULATION, MUTAGENESIS OF LYS-106.
[19]	"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: 14674694] [Abstract] Cited for: INTERACTION WITH PSMA3.
[20]	"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: 14610074] [Abstract] Cited for: FUNCTION.
[21]	"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: 14722118] [Abstract] Cited for: AUTOPHOSPHORYLATION AT THR-232, FUNCTION, INTERACTION WITH INCENP, ENZYME REGULATION, MUTAGENESIS OF LYS-106.
[22]	"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: 15020684] [Abstract] Cited for: FUNCTION.
[23]	"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: 15249581] [Abstract] Cited for: INTERACTION WITH CDCA8, ENZYME REGULATION, FUNCTION.
[24]	"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: 14602875] [Abstract] Cited for: FUNCTION, INTERACTION WITH CDCA1 AND NDC80.
[25]	"Aurora B -TACC1 protein complex in cytokinesis." Delaval B., Ferrand A., Conte N., Larroque C., Hernandez-Verdun D., Prigent C., Birnbaum D. Oncogene 23:4516-4522(2004) [PubMed: 15064709] [Abstract] Cited for: INTERACTION WITH TACC1.
[26]	"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: 16179162] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SEPT1, MUTAGENESIS OF LYS-106.
[27]	"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: 16103226] [Abstract] Cited for: FUNCTION.
[28]	"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: 16764853] [Abstract] Cited for: INTERACTION WITH EVI5.
[29]	"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: 17617734] [Abstract] Cited for: FUNCTION.
[30]	"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: 17543862] [Abstract] Cited for: UBIQUITINATION.
[31]	"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: 18591255] [Abstract] Cited for: INTERACTION WITH BIRC5.
[32]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; TYR-12 AND THR-232, MASS SPECTROMETRY. Tissue: Cervix adenocarcinoma.
[33]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; THR-16; THR-35; SER-45; SER-61; SER-62 AND THR-64, ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[34]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-232, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[35]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; THR-35; SER-45; SER-61; THR-64; TYR-92; SER-227; THR-232; THR-236 AND SER-313, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[36]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35, MASS SPECTROMETRY. 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: 19995937] [Abstract] Cited for: UBIQUITINATION.
[38]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, MASS SPECTROMETRY.
[39]	"RINGO C is required to sustain the spindle-assembly checkpoint." Mouron S., de Carcer G., Seco E., Fernandez-Miranda G., Malumbres M., Nebreda A.R. J. Cell Sci. 123:2586-2595(2010) [PubMed: 20605920] [Abstract] 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: 20562864] [Abstract] Cited for: INTERACTION WITH INCENP.
[41]	"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: 21658950] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF GSG2.
[42]	"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: 20959462] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF TP53, INTERACTION WITH NOC2L AND TP53, SUBCELLULAR LOCATION.
[43]	"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: 21225229] [Abstract] Cited for: INTERACTION WITH JTB.
[44]	"Aurora kinases A and B and familial breast cancer risk." Tchatchou S., Wirtenberger M., Hemminki K., Sutter C., Meindl A., Wappenschmidt B., Kiechle M., Bugert P., Schmutzler R.K., Bartram C.R., Burwinkel B. Cancer Lett. 247:266-272(2007) [PubMed: 16762494] [Abstract] Cited for: VARIANT THR-298.
[45]	"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: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-52 AND MET-179.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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. BT019534 mRNA. Translation: AAV38341.1. 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.
IPI	IPI00176642.
RefSeq	NP_004208.2. NM_004217.2.
UniGene	Hs.442658.
3D structure databases
ProteinModelPortal	Q96GD4.
SMR	Q96GD4. Positions 70-337.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-34530N.
IntAct	Q96GD4. 25 interactions.
MINT	MINT-1413997.
STRING	Q96GD4.
PTM databases
PhosphoSite	Q96GD4.
Polymorphism databases
DMDM	27805737.
Proteomic databases
PRIDE	Q96GD4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000316199; ENSP00000313950; ENSG00000178999.
GeneID	9212.
KEGG	hsa:9212.
UCSC	uc002gkm.1. human.
Organism-specific databases
CTD	9212.
GeneCards	GC17M008108.
H-InvDB	HIX0019005.
HGNC	HGNC:11390. AURKB.
HPA	CAB005862.
MIM	604970. gene.
neXtProt	NX_Q96GD4.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG08834.
GeneTree	ENSGT00550000074590.
HOGENOM	HBG755340.
HOVERGEN	HBG108519.
InParanoid	Q96GD4.
OMA	VPTGAQD.
OrthoDB	EOG4TTGJG.
PhylomeDB	Q96GD4.
Enzyme and pathway databases
Pathway_Interaction_DB	aurora_a_pathway. Aurora A signaling. aurora_b_pathway. Aurora B signaling. aurora_c_pathway. Aurora C signaling. foxm1pathway. FOXM1 transcription factor network. aurora_kinase_pathway. Signaling by Aurora kinases.
Reactome	REACT_152. Cell Cycle, Mitotic. REACT_383. DNA Replication.
Gene expression databases
ArrayExpress	Q96GD4.
Bgee	Q96GD4.
CleanEx	HS_AIM1. HS_AURKB.
Genevestigator	Q96GD4.
GermOnline	ENSG00000178999. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. [Graphical view]
KO	K11479.
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	34535.
SOURCE	Search...

Entry information

Entry name

AURKB_HUMAN

Accession

Primary (citable) accession number: Q96GD4
Secondary accession number(s): D3DTR4 , O14630, O60446, O95083, Q96DV5, Q9UQ46

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 17, 2003
Last sequence update:	January 11, 2011
Last modified:	January 25, 2012
This is version 129 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.