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P59241 (AURKA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. 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 A

EC=2.7.11.1
Alternative name(s):
Aurora 2
Aurora/IPL1-related kinase 1
Short name=ARK-1
Short name=Aurora-related kinase 1
Serine/threonine-protein kinase 6
Serine/threonine-protein kinase aurora-A
Short name=ratAurA
Gene names
Name:Aurka
Synonyms:Aik, Airk, Ark1, Aura, Ayk1, Btak, Iak1, Stk15, Stk6
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length397 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mitotic serine/threonine kinases that contributes to the regulation of cell cycle progression. Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, centrosome separation as well as maturation, chromosomal alignment, spindle assembly checkpoint, and cytokinesis. Required for initial activation of CDK1 at centrosomes. Phosphorylates numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3, p53/TP53 and TPX2. Regulates KIF2A tubulin depolymerase activity. Required for normal axon formation. Plays a role in microtubule remodeling during neurite extension. Important for microtubule formation and/or stabilization. Also acts as a key regulatory component of the p53/TP53 pathway, and particularly the checkpoint-response pathways critical for oncogenic transformation of cells, by phosphorylating and stabilizating p53/TP53. Phosphorylates its own inhibitors, the protein phosphatase type 1 (PP1) isoforms, to inhibit their activity By similarity. Necessary for proper cilia disassembly prior to mitosis By similarity. Ref.2

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Activation of CDK1, appears to be an upstream event of AURKA activation. Phosphatase inhibitor-2 (PPP1R2) and TPX2 act also as activators. Phosphatase inhibitor-2 (PPP1R2) and TPX2 act also as activators. Inactivated by the G2 checkpoint. Inhibited by GADD45A and p53/TP53, and through dephosphorylation by protein phosphatase type 1 (PP1). MLN8054 is also a potent and selective inhibitor By similarity. Activated during the early phase of cilia disassembly in the presence of PIFO By similarity.

Subunit structure

Interacts with CPEB1, JTB, TACC1, TPX2, PPP2CA, as well as with the protein phosphatase type 1 (PP1) isoforms PPP1CA, PPP1CB and PPP1CC By similarity. Interacts also with its substrates ARHGEF2, BORA, BRCA1, KIF2A, PARD3, and p53/TP53. Interaction with BORA promotes phosphorylation of PLK1. Interacts with FBXL7 and PIFO. Interacts with GADD45A, competing with its oligomerization By similarity. Interacts (via C-terminus) with AUNIP (via C-terminus) By similarity. Identified in a complex with AUNIP and NIN By similarity. Interacts with FRY; this interaction facilitates AURKA-mediated PLK1 phosphorylation By similarity.

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cytoplasmcytoskeletonspindle pole By similarity. Note: Localizes on centrosomes in interphase cells and at each spindle pole in mitosis. Associates with both the pericentriolar material (PCM) and centrioles. Detected at the neurite hillock in developing neurons By similarity.

Tissue specificity

Detected in neurons in brain cortex and hippocampus (at protein level). Expressed in mammary gland and tumor. Ref.2

Induction

Activated by progesterone.

Post-translational modification

Activated by phosphorylation at Thr-281; this brings about a change in the conformation of the activation segment. Phosphorylation at Thr-281 varies during the cell cycle and is highest during M phase. Autophosphorylated at Thr-281 upon TPX2 binding. Thr-281 can be phosphorylated by several kinases, including PAK and PKA. Protein phosphatase type 1 (PP1) binds AURKA and inhibits its activity by dephosphorylating Thr-281 during mitosis. Phosphorylation at Ser-335 decreases the kinase activity. PPP2CA controls degradation by dephosphorylating Ser-52 at the end of mitosis By similarity. Phosphorylated in embryonic brain neurons. Ref.2

Ubiquitinated by the anaphase-promoting complex (APC), leading to its degradation by the proteasome By similarity. Ubiquitinated by CHFR, leading to its degradation by the proteasome. Ubiquitinated by the E3 ubiquitin-protein ligase complex SCF(FBXL7) during mitosis, leading 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 397397Aurora kinase A
PRO_0000086694

Regions

Domain126 – 376251Protein kinase
Nucleotide binding203 – 2064ATP By similarity
Region273 – 28614Activation segment By similarity

Sites

Active site2491Proton acceptor By similarity
Binding site1361ATP; via amide nitrogen By similarity
Binding site1551ATP By similarity
Binding site2671ATP By similarity

Amino acid modifications

Modified residue401Phosphoserine By similarity
Modified residue501Phosphoserine By similarity
Modified residue2801Phosphothreonine By similarity
Modified residue2811Phosphothreonine By similarity
Modified residue3351Phosphoserine; by PKA and PAK By similarity

Sequences

Sequence LengthMass (Da)Tools
P59241 [UniParc].

Last modified January 27, 2003. Version 1.
Checksum: 95DECA2198DCED85

FASTA39744,874
        10         20         30         40         50         60 
MDRCKENCVS RPVKSTVPFG PKRVLVTEQI PSQHPGSASS GQAQRVLCPS NSQRVPPQAQ 

        70         80         90        100        110        120 
KPVAGQKPVL KQLPAASGPR PASRLSNPQK SEQPQPAASG NNSEKEQTSI QKTEDSKKRQ 

       130        140        150        160        170        180 
WTLEDFDIGR PLGKGKFGNV YLAREKQSKF ILALKVLFKV QLEKAGVEHQ LRREVEIQSH 

       190        200        210        220        230        240 
LRHPNILRLY GYFHDATRVY LILEYAPLGT VYRELQKLSK FDEQRTATYI TELANALSYC 

       250        260        270        280        290        300 
HSKRVIHRDI KPENLLLGSN GELKIADFGW SVHAPSSRRT TLCGTLDYQP PEMIEGRMHD 

       310        320        330        340        350        360 
EKVDLWSLGV LCYEFLVGMP PFEAHTYQET YRRISRVEFT FPDFVTEGAR DLISRLLKHN 

       370        380        390 
SSQRLTLAEV LEHPWIKANS SKPPTGHNSK EATSKSS 

« Hide

References

[1]"Centrosome amplification and overexpression of aurora A are early events in rat mammary carcinogenesis."
Goepfert T.M., Adigun Y.E., Zhong L., Gay J., Medina D., Brinkley W.R.
Cancer Res. 62:4115-4122(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar Furth.
Tissue: Mammary gland.
[2]"Phosphorylation of the par polarity complex protein Par3 at serine 962 is mediated by aurora A and regulates its function in neuronal polarity."
Khazaei M.R., Puschel A.W.
J. Biol. Chem. 284:33571-33579(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF537333 mRNA. Translation: AAN06823.1.
UniGeneRn.161874.

3D structure databases

ProteinModelPortalP59241.
SMRP59241. Positions 119-383.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000051977.

PTM databases

PhosphoSiteP59241.

Proteomic databases

PaxDbP59241.
PRIDEP59241.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

RGD628895. Aurka.

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG108519.
InParanoidP59241.
PhylomeDBP59241.

Gene expression databases

GenevestigatorP59241.

Family and domain databases

InterProIPR011009. 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]
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

PROP59241.

Entry information

Entry nameAURKA_RAT
AccessionPrimary (citable) accession number: P59241
Entry history
Integrated into UniProtKB/Swiss-Prot: January 27, 2003
Last sequence update: January 27, 2003
Last modified: April 16, 2014
This is version 104 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