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Q96GD4 (AURKB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length344 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: phosphorylates CHMP4C, leading to retain abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis (Ref.46, Ref.47). AURKB phosphorylates the CPC complex subunits BIRC5/survivin, CDCA8/borealin and INCENP. Phosphorylation of INCENP leads to increased AURKB activity. Other known AURKB substrates involved in centromeric functions and mitosis are CENPA, DES/desmin, GPAF, KIF2C, NSUN2, RACGAP1, SEPT1, VIM/vimentin, GSG2/Haspin, and histone H3. A positive feedback loop involving GSG2 and AURKB contributes to localization of CPC to centromeres. Phosphorylation of VIM controls vimentin filament segregation in cytokinetic process, whereas histone H3 is phosphorylated at 'Ser-10' and 'Ser-28' during mitosis (H3S10ph and H3S28ph, respectively). A positive feedback between GSG2 and AURKB contributes to CPC localization. AURKB is also required for kinetochore localization of BUB1 and SGOL1. Phosphorylation of p53/TP53 negatively regulates its transcriptional activity. Key regulator of active promoters in resting B- and T-lymphocytes: acts by mediating phosphorylation of H3S28ph at active promoters in resting B-cells, inhibiting RNF2/RING1B-mediated ubiquitination of histone H2A and enhancing binding and activity of the USP16 deubiquitinase at transcribed genes. Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.29 Ref.31 Ref.42 Ref.43 Ref.46 Ref.47

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.20 Ref.23 Ref.25

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. Interacts with RNF2/RING1B. Ref.12 Ref.17 Ref.20 Ref.21 Ref.23 Ref.25 Ref.26 Ref.27 Ref.28 Ref.30 Ref.34 Ref.38 Ref.39 Ref.43 Ref.44 Ref.45 Ref.46

Subcellular location

Nucleus. Chromosome. Chromosomecentromere. Cytoplasmcytoskeletonspindle. 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.12 Ref.13 Ref.18 Ref.20 Ref.28 Ref.38 Ref.43 Ref.45

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.20 Ref.23 Ref.25

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.32 Ref.36

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 processCell cycle
Cell division
Mitosis
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

cellular response to UV

Inferred from direct assay Ref.43. Source: UniProtKB

cleavage furrow formation

Inferred from direct assay Ref.29. Source: UniProtKB

histone H3-S28 phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

histone modification

Traceable author statement PubMed 19774610. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of B cell apoptotic process

Inferred from direct assay Ref.43. Source: UniProtKB

negative regulation of protein binding

Inferred from direct assay PubMed 21820309. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.43. Source: UniProtKB

positive regulation of cytokinesis

Inferred from mutant phenotype Ref.29. Source: UniProtKB

protein autophosphorylation

Traceable author statement PubMed 19774610. Source: UniProtKB

protein localization to kinetochore

Inferred from mutant phenotype PubMed 19468067. Source: UniProtKB

protein phosphorylation

Inferred from direct assay PubMed 21820309. Source: UniProtKB

regulation of chromosome segregation

Traceable author statement PubMed 19774610. Source: UniProtKB

spindle checkpoint

Inferred from electronic annotation. Source: InterPro

spindle midzone assembly involved in mitosis

Inferred from mutant phenotype Ref.29. Source: UniProtKB

spindle stabilization

Inferred from mutant phenotype PubMed 21820309. Source: UniProtKB

   Cellular_componentchromocenter

Inferred from electronic annotation. Source: Ensembl

chromosome passenger complex

Inferred from physical interaction PubMed 15260989Ref.34. Source: UniProtKB

condensed chromosome, centromeric region

Inferred from direct assay PubMed 19465021. Source: UniProtKB

condensed nuclear chromosome, centromeric region

Inferred from direct assay PubMed 18195732. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

intercellular bridge

Inferred from direct assay. Source: HPA

midbody

Inferred from direct assay PubMed 17726514. Source: UniProtKB

nucleus

Inferred from direct assay Ref.43. Source: UniProtKB

spindle

Traceable author statement PubMed 19774610. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

histone serine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.17PubMed 16291752PubMed 17726514Ref.43. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay PubMed 22724069. Source: FlyBase

protein serine/threonine/tyrosine kinase activity

Traceable author statement PubMed 19774610. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 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.
Isoform 4 (identifier: Q96GD4-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-41: Missing.
Isoform 5 (identifier: Q96GD4-5)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 344344Aurora kinase B
PRO_0000085656

Regions

Domain77 – 327251Protein kinase
Nucleotide binding83 – 919ATP By similarity

Sites

Active site2001Proton acceptor By similarity
Binding site1061ATP By similarity

Amino acid modifications

Modified residue351Phosphothreonine Ref.35
Modified residue621Phosphoserine Ref.40
Modified residue641Phosphothreonine Ref.40
Modified residue2321Phosphothreonine; by autocatalysis Ref.23

Natural variations

Alternative sequence1 – 4141Missing in isoform 4.
VSP_047103
Alternative sequence691T → TR in isoform 3 and isoform 5.
VSP_044384
Alternative sequence86 – 13449GKFGN…AHLHH → ALLCLWPEASSVSSPSH in isoform 2.
VSP_044385
Alternative sequence133 – 1419HHPNILRLY → QSWRSWQML in isoform 3.
VSP_044386
Alternative sequence142 – 344203Missing in isoform 3.
VSP_044387
Natural variant521A → V. Ref.49
Corresponds to variant rs55878091 [ dbSNP | Ensembl ].
VAR_040383
Natural variant1001H → Q.
Corresponds to variant rs3027254 [ dbSNP | Ensembl ].
VAR_027970
Natural variant1791T → M. Ref.49
VAR_040384
Natural variant2981M → T. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.7 Ref.11 Ref.48
Corresponds to variant rs1059476 [ dbSNP | Ensembl ].
VAR_027971

Experimental info

Mutagenesis1061K → R: Leads to loss of kinase activity and severely impairs mitotic progression. Ref.19 Ref.20 Ref.23 Ref.28
Sequence conflict14 – 152RQ → DK in AAC98891. Ref.5
Sequence conflict1611E → M in AAB65786. Ref.4
Sequence conflict1611E → M in AAC98891. Ref.5
Sequence conflict167 – 1693QKS → HKT in AAB65786. Ref.4
Sequence conflict1791T → TVRR in AAB65786. Ref.4
Sequence conflict1801I → VRAV in AAC98891. Ref.5
Sequence conflict2261P → T in BAA82709. Ref.3
Sequence conflict249 – 2502MH → ID in BAA82709. Ref.3
Sequence conflict2711Missing in BAA82709. Ref.3

Secondary structure

....................................... 344
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 11, 2011. Version 3.
Checksum: A5ED13EF5A1FAFBF

FASTA34439,311
        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 

« Hide

Isoform 2 (aurkb-sv1) [UniParc].

Checksum: 9499DAE479793112
Show »

FASTA31235,302
Isoform 3 (aurkb-sv2) [UniParc].

Checksum: D8AB62DA2CCFA385
Show »

FASTA14216,211
Isoform 4 [UniParc].

Checksum: 301BAFF2494B3650
Show »

FASTA30334,760
Isoform 5 [UniParc].

Checksum: ACB05C191F35F38C
Show »

FASTA34539,467

References

« Hide '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]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
[9]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]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. expand/collapse author list , 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].
[11]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), VARIANT THR-298.
Tissue: Lung, Lymph and Muscle.
[12]"INCENP is required for proper targeting of Survivin to the centromeres and the anaphase spindle during mitosis."
Wheatley S.P., Carvalho A., Vagnarelli P., Earnshaw W.C.
Curr. Biol. 11:886-890(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE CPC COMPLEX, SUBCELLULAR LOCATION, FUNCTION.
[13]"CENP-A is phosphorylated by Aurora B kinase and plays an unexpected role in completion of cytokinesis."
Zeitlin S.G., Shelby R.D., Sullivan K.F.
J. Cell Biol. 155:1147-1157(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[14]"Mitotic kinases as regulators of cell division and its checkpoints."
Nigg E.A.
Nat. Rev. Mol. Cell Biol. 2:21-32(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[15]"Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation."
Goto H., Yasui Y., Nigg E.A., Inagaki M.
Genes Cells 7:11-17(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
[16]"Mitotic phosphorylation of histone H3: spatio-temporal regulation by mammalian Aurora kinases."
Crosio C., Fimia G.M., Loury R., Kimura M., Okano Y., Zhou H., Sen S., Allis C.D., Sassone-Corsi P.
Mol. Cell. Biol. 22:874-885(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
[17]"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.
[18]"Aurora-B regulates the cleavage furrow-specific vimentin phosphorylation in the cytokinetic process."
Goto H., Yasui Y., Kawajiri A., Nigg E.A., Terada Y., Tatsuka M., Nagata K., Inagaki M.
J. Biol. Chem. 278:8526-8530(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[19]"Functional significance of the specific sites phosphorylated in desmin at cleavage furrow: Aurora-B may phosphorylate and regulate type III intermediate filaments during cytokinesis coordinatedly with Rho-kinase."
Kawajiri A., Yasui Y., Goto H., Tatsuka M., Takahashi M., Nagata K., Inagaki M.
Mol. Biol. Cell 14:1489-1500(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF LYS-106.
[20]"Exploring the functional interactions between Aurora B, INCENP, and survivin in mitosis."
Honda R., Korner R., Nigg E.A.
Mol. Biol. Cell 14:3325-3341(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE CPC COMPLEX, FUNCTION OF THE CPC COMPLEX, INDUCTION, SUBCELLULAR LOCATION, ENZYME REGULATION, MUTAGENESIS OF LYS-106.
[21]"Human Aurora-B binds to a proteasome alpha-subunit HC8 and undergoes degradation in a proteasome-dependent manner."
Shu F., Guo S., Dang Y., Qi M., Zhou G., Guo Z., Zhang Y., Wu C., Zhao S., Yu L.
Mol. Cell. Biochem. 254:157-162(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PSMA3.
[22]"Aurora-B phosphorylation in vitro identifies a residue of survivin that is essential for its localization and binding to inner centromere protein (INCENP) in vivo."
Wheatley S.P., Henzing A.J., Dodson H., Khaled W., Earnshaw W.C.
J. Biol. Chem. 279:5655-5660(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[23]"Autophosphorylation of a newly identified site of Aurora-B is indispensable for cytokinesis."
Yasui Y., Urano T., Kawajiri A., Nagata K., Tatsuka M., Saya H., Furukawa K., Takahashi T., Izawa I., Inagaki M.
J. Biol. Chem. 279:12997-13003(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: AUTOPHOSPHORYLATION AT THR-232, FUNCTION, INTERACTION WITH INCENP, ENZYME REGULATION, MUTAGENESIS OF LYS-106.
[24]"Bub1 is required for kinetochore localization of BubR1, Cenp-E, Cenp-F and Mad2, and chromosome congression."
Johnson V.L., Scott M.I., Holt S.V., Hussein D., Taylor S.S.
J. Cell Sci. 117:1577-1589(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[25]"Borealin: a novel chromosomal passenger required for stability of the bipolar mitotic spindle."
Gassmann R., Carvalho A., Henzing A.J., Ruchaud S., Hudson D.F., Honda R., Nigg E.A., Gerloff D.L., Earnshaw W.C.
J. Cell Biol. 166:179-191(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDCA8, ENZYME REGULATION, FUNCTION.
[26]"Identification of the substrates and interaction proteins of aurora kinases from a protein-protein interaction model."
Tien A.-C., Lin M.-H., Su L.-J., Hong Y.-R., Cheng T.-S., Lee Y.-C.G., Lin W.-J., Still I.H., Huang C.-Y.F.
Mol. Cell. Proteomics 3:93-104(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CDCA1 AND NDC80.
[27]"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.
[28]"Septin1, a new interaction partner for human serine/threonine kinase aurora-B."
Qi M., Yu W., Liu S., Jia H., Tang L., Shen M., Yan X., Saiyin H., Lang Q., Wan B., Zhao S., Yu L.
Biochem. Biophys. Res. Commun. 336:994-1000(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SEPT1, MUTAGENESIS OF LYS-106.
[29]"An ECT2-centralspindlin complex regulates the localization and function of RhoA."
Yuce O., Piekny A., Glotzer M.
J. Cell Biol. 170:571-582(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[30]"EVI5 protein associates with the INCENP-aurora B kinase-survivin chromosomal passenger complex and is involved in the completion of cytokinesis."
Faitar S.L., Sossey-Alaoui K., Ranalli T.A., Cowell J.K.
Exp. Cell Res. 312:2325-2335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EVI5.
[31]"Shugoshin 1 plays a central role in kinetochore assembly and is required for kinetochore targeting of Plk1."
Pouwels J., Kukkonen A.M., Lan W., Daum J.R., Gorbsky G.J., Stukenberg T., Kallio M.J.
Cell Cycle 6:1579-1585(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[32]"A Cul3-based E3 ligase removes Aurora B from mitotic chromosomes, regulating mitotic progression and completion of cytokinesis in human cells."
Sumara I., Quadroni M., Frei C., Olma M.H., Sumara G., Ricci R., Peter M.
Dev. Cell 12:887-900(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[33]"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.
[34]"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.
[35]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[36]"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.
[37]"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].
[38]"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.
[39]"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.
[40]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND THR-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[41]"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].
[42]"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.
[43]"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.
[44]"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.
[45]"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.
[46]"ESCRT-III governs the Aurora B-mediated abscission checkpoint through CHMP4C."
Carlton J.G., Caballe A., Agromayor M., Kloc M., Martin-Serrano J.
Science 336:220-225(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CHMP4C.
[47]"ANCHR mediates Aurora-B-dependent abscission checkpoint control through retention of VPS4."
Thoresen S.B., Campsteijn C., Vietri M., Schink K.O., Liestoel K., Andersen J.S., Raiborg C., Stenmark H.
Nat. Cell Biol. 0:0-0(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[48]"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.
[49]"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. expand/collapse author list , 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.
AK297976 mRNA. Translation: BAG60286.1.
AC135178 Genomic DNA. No translation available.
CH471108 Genomic DNA. Translation: EAW90075.1.
CH471108 Genomic DNA. Translation: EAW90077.1.
CH471108 Genomic DNA. Translation: EAW90078.1.
BC000442 mRNA. Translation: AAH00442.3.
BC009751 mRNA. Translation: AAH09751.1.
BC013300 mRNA. Translation: AAH13300.2. Different initiation.
BC080581 mRNA. Translation: AAH80581.1.
CCDSCCDS11134.1. [Q96GD4-1]
CCDS58514.1. [Q96GD4-4]
RefSeqNP_001243763.1. NM_001256834.1. [Q96GD4-4]
NP_001271455.1. NM_001284526.1. [Q96GD4-5]
NP_004208.2. NM_004217.3. [Q96GD4-1]
XP_005256911.1. XM_005256854.2. [Q96GD4-1]
UniGeneHs.442658.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4AF3X-ray2.75A55-344[»]
ProteinModelPortalQ96GD4.
SMRQ96GD4. Positions 70-338.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114646. 81 interactions.
DIPDIP-34530N.
IntActQ96GD4. 29 interactions.
MINTMINT-1413997.
STRING9606.ENSP00000313950.

Chemistry

BindingDBQ96GD4.
ChEMBLCHEMBL2185.
GuidetoPHARMACOLOGY1937.

PTM databases

PhosphoSiteQ96GD4.

Polymorphism databases

DMDM317373473.

Proteomic databases

MaxQBQ96GD4.
PaxDbQ96GD4.
PRIDEQ96GD4.

Protocols and materials databases

DNASU9212.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000316199; ENSP00000313950; ENSG00000178999.
ENST00000534871; ENSP00000443869; ENSG00000178999. [Q96GD4-4]
ENST00000535053; ENSP00000445866; ENSG00000178999. [Q96GD4-3]
ENST00000578549; ENSP00000462207; ENSG00000178999. [Q96GD4-2]
ENST00000585124; ENSP00000463999; ENSG00000178999. [Q96GD4-1]
GeneID9212.
KEGGhsa:9212.
UCSCuc002gkm.4. human. [Q96GD4-1]
uc021tpy.1. human. [Q96GD4-2]

Organism-specific databases

CTD9212.
GeneCardsGC17M008108.
H-InvDBHIX0019005.
HGNCHGNC:11390. AURKB.
HPACAB005862.
HPA037708.
MIM604970. gene.
neXtProtNX_Q96GD4.
PharmGKBPA36199.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG108519.
InParanoidQ96GD4.
KOK11479.
OMAHPWVRAN.
PhylomeDBQ96GD4.
TreeFamTF351439.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
SignaLinkQ96GD4.

Gene expression databases

ArrayExpressQ96GD4.
BgeeQ96GD4.
CleanExHS_AIM1.
HS_AURKB.
GenevestigatorQ96GD4.

Family and domain databases

InterProIPR028772. AURKB.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERPTHR24350:SF4. PTHR24350:SF4. 1 hit.
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiAurora_B_kinase.
GenomeRNAi9212.
NextBio34535.
PROQ96GD4.
SOURCESearch...

Entry information

Entry nameAURKB_HUMAN
AccessionPrimary (citable) accession number: Q96GD4
Secondary accession number(s): B4DNM4 expand/collapse secondary AC list , C7G533, C7G534, C7G535, D3DTR4, J9JID1, O14630, O60446, O95083, Q96DV5, Q9UQ46
Entry history
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 158 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM