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O55099 (AURKB_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length343 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 By similarity. Ref.1

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 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-235-phosphorylated AURKB form during prometaphase and metaphase By similarity. Interacts with TTC28. Interacts with RNF2/RING1B By similarity.

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-235-phosphorylated form during metaphase may be dependent upon interaction with SPDYC. Interacts with p53/TP53. Interacts (via the middle kinase domain) with NOC2L (via the N- and C-terminus domains) By similarity.

Tissue specificity

High level expression seen in the testis. It is also expressed in the spleen, lung and heart. Expressed in the G2/M phase of the cell cycle. Ref.1

Post-translational modification

The phosphorylation of Thr-235 requires the binding to INCENP and occurs by means of an autophosphorylation mechanism. Thr-235 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 expression pattern PubMed 19204916. Source: RGD

cell proliferation

Inferred from expression pattern PubMed 17914147. Source: RGD

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 sequence or structural similarity. 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 electronic annotation. Source: Ensembl

chromosome passenger complex

Inferred from electronic annotation. Source: Ensembl

condensed nuclear chromosome, centromeric region

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

midbody

Inferred from direct assay Ref.1. Source: RGD

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

spindle

Inferred from direct assay Ref.1. Source: RGD

   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 kinase activity

Inferred from mutant phenotype Ref.1. Source: RGD

protein serine/threonine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 343343Aurora kinase B
PRO_0000085659

Regions

Domain80 – 330251Protein kinase
Nucleotide binding86 – 949ATP By similarity

Sites

Active site2031Proton acceptor By similarity
Binding site1091ATP

Amino acid modifications

Modified residue2351Phosphothreonine; by autocatalysis By similarity

Experimental info

Mutagenesis1091K → R: Loss of kinase activity, disruption of cleavage furrow formation, failure of cytokinesis leading to cell polyploidy death. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O55099 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 27B740D20E287598

FASTA34339,234
        10         20         30         40         50         60 
MAQKENVYPW PYGSKTSQSG LNTLPQRVLR KEPAVTPAQA LMNRSNSQST AVPGQKLTEN 

        70         80         90        100        110        120 
KGATALQGSQ SRQPFTIDNF EIGRPLGKGK FGNVYLAREK KSRFIVALKI LFKSQIEKEG 

       130        140        150        160        170        180 
VEHQLRREIE IQAHLKHPNI LQLYNYFYDQ QRIYLILEYA PRGELYKELQ KSGTFDEQRT 

       190        200        210        220        230        240 
ATIMEELSDA LMYCHKKKVI HRDIKPENLL LGLQGELKIA DFGWSVHAPS LRRKTMCGTL 

       250        260        270        280        290        300 
DYLPPEMIEG RMHNEMVDLW CIGVLCYELM VGNPPFESPS HSETYRRIVK VDLKFPSSMP 

       310        320        330        340 
LGAKDLISKL LKHNPSQRLP LEQVSAHPWV RANSRRVLPP SAL 

« Hide

References

« Hide 'large scale' references
[1]"AIM-1: a mammalian midbody-associated protein required for cytokinesis."
Terada Y., Tatsuka M., Suzuki F., Yasuda Y., Fujita S., Otsu M.
EMBO J. 17:667-676(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-109.
Tissue: Kidney.
[2]"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: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D89731 mRNA. Translation: BAA23794.1.
BC097297 mRNA. Translation: AAH97297.1.
RefSeqNP_446201.1. NM_053749.1.
XP_006246631.1. XM_006246569.1.
UniGeneRn.10865.

3D structure databases

ProteinModelPortalO55099.
SMRO55099. Positions 75-340.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000008492.

PTM databases

PhosphoSiteO55099.

Proteomic databases

PRIDEO55099.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000008492; ENSRNOP00000008492; ENSRNOG00000005659.
GeneID114592.
KEGGrno:114592.
UCSCRGD:621625. rat.

Organism-specific databases

CTD9212.
RGD621625. Aurkb.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00550000074590.
HOGENOMHOG000233016.
HOVERGENHBG108519.
InParanoidO55099.
KOK11479.
OMAHPWVRAN.
OrthoDBEOG74FF1F.
PhylomeDBO55099.
TreeFamTF351439.

Gene expression databases

GenevestigatorO55099.

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

NextBio618749.
PROO55099.

Entry information

Entry nameAURKB_RAT
AccessionPrimary (citable) accession number: O55099
Secondary accession number(s): Q4V8N1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 132 of the entry and version 1 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