Aurora kinase A - Rattus norvegicus (Rat)

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P59241 (AURKA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 97. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	Aurka
Synonyms:	Aik, Airk, Ark1, Aura, Ayk1, Btak, Iak1, Stk15, Stk6

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	397 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › cytoskeleton › centrosome By similarity. Cytoplasm › cytoskeleton › spindle 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.

Ontologies

Keywords
Biological process	Cell cycle Cell division Cilium biogenesis/degradation Mitosis
Cellular component	Cytoplasm Cytoskeleton Microtubule
Disease	Proto-oncogene
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Traceable author statement Ref.1. Source: RGD cell division Inferred from electronic annotation. Source: UniProtKB-KW cell projection organization Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW response to estradiol stimulus Inferred from expression pattern PubMed 15601761. Source: RGD
Cellular_component	centrosome Inferred from direct assay Ref.1. Source: RGD cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW microtubule Inferred from electronic annotation. Source: UniProtKB-KW spindle Inferred from direct assay Ref.1. Source: RGD spindle pole Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from direct assay Ref.1. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 397

397

Aurora kinase A

PRO_0000086694

Regions

Domain

126 – 376

251

Protein kinase

Nucleotide binding

203 – 206

ATP By similarity

Region

273 – 286

Activation segment By similarity

Sites

Active site

249

Proton acceptor By similarity

Binding site

136

ATP; via amide nitrogen By similarity

Binding site

155

ATP By similarity

Binding site

267

ATP By similarity

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

280

Phosphothreonine By similarity

Modified residue

281

Phosphothreonine By similarity

Modified residue

335

Phosphoserine; by PKA and PAK By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P59241 [UniParc].

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

397

44,874

        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

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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.
IPI	IPI00325622.
UniGene	Rn.161874.
3D structure databases
ProteinModelPortal	P59241.
SMR	P59241. Positions 119-383.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000051977.
PTM databases
PhosphoSite	P59241.
Proteomic databases
PaxDb	P59241.
PRIDE	P59241.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
RGD	628895. Aurka.
Phylogenomic databases
eggNOG	COG0515.
HOVERGEN	HBG108519.
InParanoid	P59241.
OrthoDB	EOG4HX512.
Gene expression databases
ArrayExpress	P59241.
Genevestigator	P59241.
GermOnline	ENSRNOG00000004479. Rattus norvegicus.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AURKA_RAT

Accession

Primary (citable) accession number: P59241

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 27, 2003
Last sequence update:	January 27, 2003
Last modified:	April 3, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents