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O70126 (AURKB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length345 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. 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). 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.7 Ref.8

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.8

Cofactor

Magnesium.

Enzyme regulation

Activity is greatly increased when AURKB is within the CPC complex. In particular, AURKA-phosphorylated INCENP acts as an activator of AURKB By similarity.

Subunit structure

Component of the chromosomal passenger complex (CPC) composed of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB and AURKC By similarity. Associates with RACGAP1 during M phase. Interacts with CDCA1, EVI5, JTB, NDC80, PSMA3, SEPT1 and TACC1 By similarity. Interacts with SPDYC; this interaction may be required for proper localization of active, Thr-237-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) By similarity. Interacts with TTC28 By similarity. Interacts with RNF2/RING1B. Ref.8

Subcellular location

Nucleus By similarity. Chromosome By similarity. Chromosomecentromere By similarity. Cytoplasmcytoskeletonspindle By similarity. 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 By similarity. Proper localization of the active, Thr-237-phosphorylated form during metaphase may be dependent upon interaction with SPDYC By similarity.

Tissue specificity

Expressed in testis, intestine and spleen. All of them are tissues that contain a large number of proliferating cells. Expressed during S phase, in a cell-cycle-dependent fashion.

Developmental stage

Strongly expressed in 8.5 and 12.5 dpc.

Post-translational modification

The phosphorylation of Thr-237 requires the binding to INCENP and occurs by means of an autophosphorylation mechanism. Thr-237 phosphorylation is indispensable for the AURKB kinase activity By similarity.

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 By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Nucleus
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Inferred from electronic annotation. Source: Ensembl

cellular response to UV

Inferred from sequence or structural similarity. Source: UniProtKB

cleavage furrow formation

Inferred from sequence or structural similarity. Source: UniProtKB

histone H3-S28 phosphorylation

Inferred from direct assay Ref.8. Source: UniProtKB

negative regulation of B cell apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of protein binding

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cytokinesis

Inferred from sequence or structural similarity. Source: UniProtKB

protein localization to kinetochore

Inferred from sequence or structural similarity. Source: UniProtKB

spindle checkpoint

Inferred from electronic annotation. Source: InterPro

spindle midzone assembly involved in mitosis

Inferred from sequence or structural similarity. Source: UniProtKB

spindle stabilization

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentchromocenter

Inferred from direct assay PubMed 19283064. Source: MGI

chromosome passenger complex

Inferred from direct assay PubMed 20562830. Source: MGI

condensed nuclear chromosome, centromeric region

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

kinetochore

Inferred from sequence orthology PubMed 23036704. Source: MGI

midbody

Inferred from direct assay Ref.2. Source: MGI

mitotic spindle pole

Inferred from sequence orthology PubMed 23036704. Source: MGI

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

histone serine kinase activity

Inferred from direct assay Ref.8. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.8. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.8. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 345345Aurora kinase B
PRO_0000085657

Regions

Domain82 – 332251Protein kinase
Nucleotide binding88 – 969ATP By similarity

Sites

Active site2051Proton acceptor By similarity
Binding site1111ATP By similarity

Amino acid modifications

Modified residue351Phosphothreonine By similarity
Modified residue621Phosphoserine By similarity
Modified residue2371Phosphothreonine; by autocatalysis By similarity

Experimental info

Sequence conflict441R → W in BAA04658. Ref.1
Sequence conflict451F → S in BAA04658. Ref.1
Sequence conflict451F → S in AAC12683. Ref.2
Sequence conflict451F → S in AAH03261. Ref.6

Sequences

Sequence LengthMass (Da)Tools
O70126 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: D204D8B91CFF00A4

FASTA34539,384
        10         20         30         40         50         60 
MAQKENAYPW PYGSKTSQSG LNTLSQRVLR KEPATTSALA LVNRFNSQST AAPGQKLAEN 

        70         80         90        100        110        120 
KSQGSTASQG SQNKQPFTID NFEIGRPLGK GKFGNVYLAR EKKSRFIVAL KILFKSQIEK 

       130        140        150        160        170        180 
EGVEHQLRRE IEIQAHLKHP NILQLYNYFY DQQRIYLILE YAPRGELYKE LQKSRTFDEQ 

       190        200        210        220        230        240 
RTATIMEELS DALTYCHKKK VIHRDIKPEN LLLGLQGELK IADFGWSVHA PSLRRKTMCG 

       250        260        270        280        290        300 
TLDYLPPEMI EGRMHNEMVD LWCIGVLCYE LMVGNPPFES PSHSETYRRI VKVDLKFPSS 

       310        320        330        340 
VPSGAQDLIS KLLKHNPWQR LPLAEVAAHP WVRANSRRVL PPSAL 

« Hide

References

« Hide 'large scale' references
[1]"Cell-cycle-dependent expression of the STK-1 gene encoding a novel murine putative protein kinase."
Niwa H., Abe K., Kunisada T., Yamamura K.
Gene 169:197-201(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Testis.
[2]"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].
Strain: BALB/c.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo and Embryonic stem cell.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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].
Tissue: Mammary gland.
[7]"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.
[8]"The Aurora B kinase and the Polycomb protein Ring1B combine to regulate active promoters in quiescent lymphocytes."
Frangini A., Sjoberg M., Roman-Trufero M., Dharmalingam G., Haberle V., Bartke T., Lenhard B., Malumbres M., Vidal M., Dillon N.
Mol. Cell 51:647-661(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH RNF2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D21099 mRNA. Translation: BAA04658.1.
U69107 mRNA. Translation: AAC12683.1.
AK075951 mRNA. Translation: BAC36078.1.
AK132006 mRNA. Translation: BAE20935.1.
AL645902 Genomic DNA. Translation: CAI24442.1.
CH466601 Genomic DNA. Translation: EDL10472.1.
BC003261 mRNA. Translation: AAH03261.1.
CCDSCCDS24877.1.
PIRJC4665.
RefSeqNP_035626.1. NM_011496.1.
UniGeneMm.3488.

3D structure databases

ProteinModelPortalO70126.
SMRO70126. Positions 41-343.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203547. 16 interactions.
IntActO70126. 8 interactions.
MINTMINT-1341009.

Chemistry

ChEMBLCHEMBL1075275.

PTM databases

PhosphoSiteO70126.

Proteomic databases

PaxDbO70126.
PRIDEO70126.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021277; ENSMUSP00000021277; ENSMUSG00000020897.
ENSMUST00000108666; ENSMUSP00000104306; ENSMUSG00000020897.
GeneID20877.
KEGGmmu:20877.
UCSCuc007jpa.1. mouse.

Organism-specific databases

CTD9212.
MGIMGI:107168. Aurkb.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00550000074590.
HOGENOMHOG000233016.
HOVERGENHBG108519.
InParanoidQ8C6C1.
KOK11479.
OMAHPWVRAN.
OrthoDBEOG74FF1F.
TreeFamTF351439.

Gene expression databases

BgeeO70126.
CleanExMM_AURKB.
GenevestigatorO70126.

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

ChiTaRSAURKB. mouse.
NextBio299727.
PROO70126.
SOURCESearch...

Entry information

Entry nameAURKB_MOUSE
AccessionPrimary (citable) accession number: O70126
Secondary accession number(s): Q61882, Q8C6C1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot