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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	344 AA.
Sequence status	Complete.
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.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.28 Ref.30 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.19 Ref.22 Ref.24
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). Interacts with TTC28. Ref.11 Ref.16 Ref.19 Ref.20 Ref.22 Ref.24 Ref.25 Ref.26 Ref.27 Ref.29 Ref.33 Ref.37 Ref.38 Ref.42 Ref.43 Ref.44
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.11 Ref.12 Ref.17 Ref.19 Ref.27 Ref.37 Ref.42 Ref.44
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.19 Ref.22 Ref.24
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.31 Ref.35
Involvement in disease	Disruptive regulation of expression is a possible 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	Alternative splicing Polymorphism
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aging Inferred from electronic annotation. Source: Compara anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Traceable author statement. Source: Reactome attachment of spindle microtubules to kinetochore Traceable author statement PubMed 19774610. Source: UniProtKB cell proliferation Inferred from electronic annotation. Source: Compara cellular response to UV Inferred from direct assay Ref.42. Source: UniProtKB cleavage furrow formation Inferred from direct assay Ref.28. Source: UniProtKB histone modification Traceable author statement PubMed 19774610. Source: UniProtKB mitotic prometaphase Traceable author statement. Source: Reactome negative regulation of B cell apoptotic process 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.28. Source: UniProtKB protein autophosphorylation Traceable author statement PubMed 19774610. Source: UniProtKB protein localization to kinetochore Inferred from mutant phenotype PubMed 19468067. Source: UniProtKB regulation of chromosome segregation Traceable author statement PubMed 19774610. Source: UniProtKB spindle midzone assembly involved in mitosis Inferred from mutant phenotype Ref.28. Source: UniProtKB
Cellular_component	chromocenter Inferred from electronic annotation. Source: Compara chromosome passenger complex Inferred from physical interaction PubMed 15260989Ref.33. Source: UniProtKB condensed nuclear chromosome, centromeric region Inferred from direct assay PubMed 18195732. Source: BHF-UCL cytosol Traceable author statement. Source: Reactome midbody Traceable author statement PubMed 19774610. Source: UniProtKB spindle Traceable author statement PubMed 19774610. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine/tyrosine kinase activity Traceable author statement PubMed 19774610. 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
HSP90AB1	P08238	2	EBI-624291,EBI-352572
INCENP	Q9NQS7	3	EBI-624291,EBI-307907
SEPT1	Q8WYJ6	6	EBI-624291,EBI-693002
TACC1	O75410-6	2	EBI-624291,EBI-624278

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q96GD4-1)

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.

Isoform 2 (identifier: Q96GD4-2)

Also known as: aurkb-sv1;

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

Isoform 3 (identifier: Q96GD4-3)

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 344

344

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

35

1

Phosphothreonine Ref.34

Modified residue

62

1

Phosphoserine Ref.39

Modified residue

64

1

Phosphothreonine Ref.39

Modified residue

232

1

Phosphothreonine; by autocatalysis Ref.22

Natural variations

Alternative sequence

69

1

T → TR in isoform 3.

VSP_044384

Alternative sequence

86 – 134

49

GKFGN…AHLHH → ALLCLWPEASSVSSPSH in isoform 2.

VSP_044385

Alternative sequence

133 – 141

9

HHPNILRLY → QSWRSWQML in isoform 3.

VSP_044386

Alternative sequence

142 – 344

203

Missing in isoform 3.

VSP_044387

Natural variant

52

1

A → V. Ref.46

VAR_040383

Natural variant

100

1

H → Q.
Corresponds to variant rs3027254 [ dbSNP | Ensembl ].

VAR_027970

Natural variant

179

1

T → M. Ref.46

VAR_040384

Natural variant

298

1

M → T. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.7 Ref.10 Ref.45
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.18 Ref.19 Ref.22 Ref.27

Sequence conflict

14 – 15

2

RQ → DK in AAC98891. Ref.5

Sequence conflict

70

1

R → RR in AAH13300. Ref.10

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

Secondary structure

1

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344

Helix Strand Turn

Details...

Helix

74 – 76

3

Beta strand

77 – 82

6

Beta strand

89 – 96

8

Turn

97 – 99

3

Beta strand

102 – 109

8

Helix

110 – 116

7

Helix

119 – 130

12

Beta strand

140 – 145

6

Beta strand

147 – 155

9

Helix

162 – 169

8

Helix

174 – 193

20

Helix

203 – 205

3

Beta strand

206 – 208

3

Beta strand

214 – 216

3

Helix

242 – 245

4

Helix

253 – 268

16

Helix

278 – 286

9

Helix

298 – 307

10

Helix

312 – 314

3

Helix

318 – 322

5

Helix

325 – 330

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [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
	Isoform 2 (aurkb-sv1) [UniParc]. Checksum: 9499DAE479793112	FASTA	312	35,302
	10 20 30 40 50 60 MAQKENSYPW PYGRQTAPSG LSTLPQRVLR KEPVTPSALV LMSRSNVQPT AAPGQKVMEN 70 80 90 100 110 120 SSGTPDILTR HFTIDDFEIG RPLGKALLCL WPEASSVSSP SHPNILRLYN YFYDRRRIYL 130 140 150 160 170 180 ILEYAPRGEL YKELQKSCTF DEQRTATIME ELADALMYCH GKKVIHRDIK PENLLLGLKG 190 200 210 220 230 240 ELKIADFGWS VHAPSLRRKT MCGTLDYLPP EMIEGRMHNE KVDLWCIGVL CYELLVGNPP 250 260 270 280 290 300 FESASHNETY RRIVKVDLKF PASVPMGAQD LISKLLRHNP SERLPLAQVS AHPWVRANSR 310 RVLPPSALQS VA
	Isoform 3 (aurkb-sv2) [UniParc]. Checksum: D8AB62DA2CCFA385	FASTA	142	16,211
	10 20 30 40 50 60 MAQKENSYPW PYGRQTAPSG LSTLPQRVLR KEPVTPSALV LMSRSNVQPT AAPGQKVMEN 70 80 90 100 110 120 SSGTPDILTR RHFTIDDFEI GRPLGKGKFG NVYLAREKKS HFIVALKVLF KSQIEKEGVE 130 140 HQLRREIEIQ AHLQSWRSWQ ML

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] [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]	"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].
[9]	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].
[10]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT THR-298. Tissue: Lung, Lymph and Muscle.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH RACGAP1.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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: AUTOPHOSPHORYLATION AT THR-232, FUNCTION, INTERACTION WITH INCENP, ENZYME REGULATION, MUTAGENESIS OF LYS-106.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TACC1.
[27]	"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.
[28]	"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.
[29]	"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.
[30]	"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.
[31]	"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.
[32]	"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.
[33]	"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.
[34]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[35]	"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.
[36]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[37]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SPDYC, SUBCELLULAR LOCATION.
[38]	"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.
[39]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[40]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH JTB.
[44]	"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.
[45]	"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] [Europe PMC] [Abstract] Cited for: VARIANT THR-298.
[46]	"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.
+	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.
AB519677 mRNA. Translation: BAI23190.1.
AB519678 mRNA. Translation: BAI23191.1.
AB519679 mRNA. Translation: BAI23192.1.
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.
IPI00946543.
IPI00947382.

RefSeq

NP_004208.2. NM_004217.3.

UniGene

Hs.442658.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4AF3	X-ray	2.75	A	55-344	[»]

ProteinModelPortal

Q96GD4.

SMR

Q96GD4. Positions 70-338.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-34530N.

IntAct

Q96GD4. 23 interactions.

MINT

MINT-1413997.

STRING

9606.ENSP00000313950.

PTM databases

PhosphoSite

Q96GD4.

Polymorphism databases

DMDM

27805737.

Proteomic databases

PaxDb

Q96GD4.

PRIDE

Q96GD4.

Protocols and materials databases

DNASU

9212.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000535053; ENSP00000445866; ENSG00000178999.
ENST00000578549; ENSP00000462207; ENSG00000178999.
ENST00000585124; ENSP00000463999; ENSG00000178999.

GeneID

9212.

KEGG

hsa:9212.

UCSC

uc002gkm.3. human.

Organism-specific databases

CTD

9212.

GeneCards

GC17M008108.

H-InvDB

HIX0019005.

HGNC

HGNC:11390. AURKB.

HPA

CAB005862.

MIM

604970. gene.

neXtProt

NX_Q96GD4.

PharmGKB

PA36199.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOVERGEN

HBG108519.

InParanoid

Q96GD4.

KO

K11479.

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_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

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.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

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

BindingDB

Q96GD4.

ChEMBL

CHEMBL2185.

GenomeRNAi

9212.

NextBio

34535.

SOURCE

Search...

Entry information

Entry name

AURKB_HUMAN

Accession

Primary (citable) accession number: Q96GD4
Secondary accession number(s): C7G533 , C7G534, C7G535, D3DTR4, O14630, O60446, O95083, Q96DV5, Q9UQ46

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 17, 2003
Last sequence update:	January 11, 2011
Last modified:	May 1, 2013
This is version 144 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.