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P59241

- AURKA_RAT

UniProt

P59241 - AURKA_RAT

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Protein

Aurora kinase A

Gene
Aurka, Aik, Airk, Ark1, Aura, Ayk1, Btak, Iak1, Stk15, Stk6
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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. Interacts with SIRT2 By similarity.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei136 – 1361ATP; via amide nitrogen By similarity
Binding sitei155 – 1551ATP By similarity
Active sitei249 – 2491Proton acceptor By similarity
Binding sitei267 – 2671ATP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi203 – 2064ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein kinase activity Source: UniProtKB
  3. protein serine/threonine kinase activity Source: RGD

GO - Biological processi

  1. cell projection organization Source: UniProtKB-KW
  2. mitotic nuclear division Source: UniProtKB-KW
  3. protein phosphorylation Source: RGD
  4. response to estradiol Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Cilium biogenesis/degradation, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Aurka
Synonyms:Aik, Airk, Ark1, Aura, Ayk1, Btak, Iak1, Stk15, Stk6
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi628895. Aurka.

Subcellular locationi

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. Colocalized with SIRT2 at centrosome By similarity.

GO - Cellular componenti

  1. centrosome Source: RGD
  2. cytoplasm Source: UniProtKB-KW
  3. microtubule Source: UniProtKB-KW
  4. spindle Source: RGD
  5. spindle pole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 397397Aurora kinase APRO_0000086694Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei40 – 401Phosphoserine By similarity
Modified residuei50 – 501Phosphoserine By similarity
Modified residuei280 – 2801Phosphothreonine By similarity
Modified residuei281 – 2811Phosphothreonine By similarity
Modified residuei335 – 3351Phosphoserine; by PKA and PAK By similarity

Post-translational modificationi

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.1 Publication
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.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP59241.
PRIDEiP59241.

PTM databases

PhosphoSiteiP59241.

Expressioni

Tissue specificityi

Detected in neurons in brain cortex and hippocampus (at protein level). Expressed in mammary gland and tumor.1 Publication

Inductioni

Activated by progesterone.

Gene expression databases

GenevestigatoriP59241.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000051977.

Structurei

3D structure databases

ProteinModelPortaliP59241.
SMRiP59241. Positions 119-383.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini126 – 376251Protein kinaseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni273 – 28614Activation segment By similarityAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
HOVERGENiHBG108519.
InParanoidiP59241.
PhylomeDBiP59241.

Family and domain databases

InterProiIPR011009. 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]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P59241-1 [UniParc]FASTAAdd to Basket

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MDRCKENCVS RPVKSTVPFG PKRVLVTEQI PSQHPGSASS GQAQRVLCPS    50
NSQRVPPQAQ KPVAGQKPVL KQLPAASGPR PASRLSNPQK SEQPQPAASG 100
NNSEKEQTSI QKTEDSKKRQ WTLEDFDIGR PLGKGKFGNV YLAREKQSKF 150
ILALKVLFKV QLEKAGVEHQ LRREVEIQSH LRHPNILRLY GYFHDATRVY 200
LILEYAPLGT VYRELQKLSK FDEQRTATYI TELANALSYC HSKRVIHRDI 250
KPENLLLGSN GELKIADFGW SVHAPSSRRT TLCGTLDYQP PEMIEGRMHD 300
EKVDLWSLGV LCYEFLVGMP PFEAHTYQET YRRISRVEFT FPDFVTEGAR 350
DLISRLLKHN SSQRLTLAEV LEHPWIKANS SKPPTGHNSK EATSKSS 397
Length:397
Mass (Da):44,874
Last modified:January 27, 2003 - v1
Checksum:i95DECA2198DCED85
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF537333 mRNA. Translation: AAN06823.1.
UniGeneiRn.161874.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF537333 mRNA. Translation: AAN06823.1 .
UniGenei Rn.161874.

3D structure databases

ProteinModelPortali P59241.
SMRi P59241. Positions 119-383.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000051977.

PTM databases

PhosphoSitei P59241.

Proteomic databases

PaxDbi P59241.
PRIDEi P59241.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

RGDi 628895. Aurka.

Phylogenomic databases

eggNOGi COG0515.
HOVERGENi HBG108519.
InParanoidi P59241.
PhylomeDBi P59241.

Miscellaneous databases

PROi P59241.

Gene expression databases

Genevestigatori P59241.

Family and domain databases

InterProi 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 ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiAURKA_RAT
AccessioniPrimary (citable) accession number: P59241
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 27, 2003
Last sequence update: January 27, 2003
Last modified: September 3, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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