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O14965 (AURKA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 166. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

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
Short name=hARK1
Breast tumor-amplified kinase
Serine/threonine-protein kinase 15
Serine/threonine-protein kinase 6
Serine/threonine-protein kinase aurora-A
Gene names
Name:AURKA
Synonyms:AIK, AIRK1, ARK1, AURA, AYK1, BTAK, IAK1, STK15, STK6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length403 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 stabilizing p53/TP53. Phosphorylates its own inhibitors, the protein phosphatase type 1 (PP1) isoforms, to inhibit their activity. Necessary for proper cilia disassembly prior to mitosis. Ref.8 Ref.10 Ref.11 Ref.13 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.21 Ref.24 Ref.26 Ref.27 Ref.30 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.49

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.45 Ref.48 Ref.52 Ref.53

Enzyme regulation

Activation of CDK1, appears to be an upstream event of AURKA activation. 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. Activated during the early phase of cilia disassembly in the presence of PIFO. Ref.10 Ref.13 Ref.30

Subunit structure

Interacts with FBXL7 By similarity. Interacts with CPEB1, JTB, TACC1, TPX2, PPP2CA, as well as with the protein phosphatase type 1 (PP1) isoforms PPP1CA, PPP1CB and PPP1CC. Interacts also with its substrates ARHGEF2, BORA, BRCA1, KIF2A, PARD3, and p53/TP53. Interaction with BORA promotes phosphorylation of PLK1. Interacts with PIFO. Interacts with GADD45A, competing with its oligomerization. Interacts (via C-terminus) with AUNIP (via C-terminus). Identified in a complex with AUNIP and NIN. Interacts with FRY; this interaction facilitates AURKA-mediated PLK1 phosphorylation. Ref.11 Ref.17 Ref.19 Ref.21 Ref.22 Ref.25 Ref.28 Ref.29 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.41 Ref.44 Ref.50 Ref.51

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle pole. Note: Detected at the neurite hillock in developing neurons By similarity. Localizes at the centrosome in mitotic cells from early prophase until telophase, but also localizes to the spindle pole MTs from prophase to anaphase. Moves to the midbody during both telophase and cytokinesis. Associates with both the pericentriolar material (PCM) and centrioles. Ref.1 Ref.8 Ref.12 Ref.15 Ref.29 Ref.34 Ref.36 Ref.41

Tissue specificity

Highly expressed in testis and weakly in skeletal muscle, thymus and spleen. Also highly expressed in colon, ovarian, prostate, neuroblastoma, breast and cervical cancer cell lines.

Induction

Expression is cell-cycle regulated, low in G1/S, accumulates during G2/M, and decreases rapidly after. Ref.1 Ref.8 Ref.10 Ref.13 Ref.14 Ref.24 Ref.30

Post-translational modification

Activated by phosphorylation at Thr-288; this brings about a change in the conformation of the activation segment. Phosphorylation at Thr-288 varies during the cell cycle and is highest during M phase. Autophosphorylated at Thr-288 upon TPX2 binding. Thr-288 can be phosphorylated by several kinases, including PAK and PKA. Protein phosphatase type 1 (PP1) binds AURKA and inhibits its activity by dephosphorylating Thr-288 during mitosis. Phosphorylation at Ser-342 decreases the kinase activity. PPP2CA controls degradation by dephosphorylating Ser-51 at the end of mitosis. Ref.10 Ref.11 Ref.13 Ref.15 Ref.19 Ref.23 Ref.29 Ref.33 Ref.35 Ref.47 Ref.50

Ubiquitinated by the E3 ubiquitin-protein ligase complex SCF(FBXL7) during mitosis, leading to its degradation by the proteasome. Ubiquitinated by CHFR, leading to its degradation by the proteasome By similarity. Ubiquitinated by the anaphase-promoting complex (APC), leading to its degradation by the proteasome. Ref.9 Ref.10

Miscellaneous

Centrosome amplification can occur when the cycles are uncoupled, and this amplification is associated with cancer and with an increase in the levels of chromosomal instability.

Sequence similarities

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

Contains 1 protein kinase domain.

Caution

Authors initially considered AURKA/STK6 and STK15 as 2 different proteins (Ref.3). It is clear that they are the same protein.

Sequence caution

The sequence BAA23592.1 differs from that shown. Reason: Frameshift at positions 105, 125, 129, 235 and 241.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Cilium biogenesis/degradation
Mitosis
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
   Coding sequence diversityPolymorphism
   DiseaseProto-oncogene
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process

Traceable author statement. Source: Reactome

cell cycle

Non-traceable author statement PubMed 15504738. Source: UniProtKB

cell projection organization

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic nuclear division

Traceable author statement Ref.1. Source: ProtInc

negative regulation of protein binding

Inferred from direct assay PubMed 21820309. Source: UniProtKB

phosphatidylinositol-mediated signaling

Non-traceable author statement PubMed 15504738. Source: UniProtKB

positive regulation of mitosis

Traceable author statement Ref.43. Source: UniProtKB

protein autophosphorylation

Traceable author statement Ref.43. Source: UniProtKB

protein phosphorylation

Inferred from direct assay PubMed 21820309. Source: UniProtKB

regulation of centrosome cycle

Traceable author statement Ref.43. Source: UniProtKB

regulation of protein stability

Inferred from mutant phenotype Ref.24. Source: UniProtKB

spindle organization

Non-traceable author statement PubMed 15504738. Source: UniProtKB

spindle stabilization

Inferred from mutant phenotype PubMed 21820309. Source: UniProtKB

   Cellular_componentcentrosome

Inferred from direct assay PubMed 17726514PubMed 21399614. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule cytoskeleton

Inferred from direct assay Ref.51. Source: BHF-UCL

midbody

Traceable author statement Ref.43. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 20531406. Source: BHF-UCL

perinuclear region of cytoplasm

Inferred from direct assay PubMed 20531406. Source: BHF-UCL

spindle

Traceable author statement Ref.43. Source: UniProtKB

spindle pole centrosome

Inferred from direct assay Ref.51. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 12244051Ref.24PubMed 17726514PubMed 18521620Ref.50PubMed 18663142Ref.38Ref.37PubMed 22306998. Source: UniProtKB

protein kinase activity

Inferred from direct assay Ref.47. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.32. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from experiment. Source: Reactome

protein serine/threonine/tyrosine kinase activity

Traceable author statement Ref.43. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 403403Aurora kinase A
PRO_0000086692

Regions

Domain133 – 383251Protein kinase
Nucleotide binding210 – 2134ATP
Region280 – 29314Activation segment

Sites

Active site2561Proton acceptor Ref.47
Binding site1431ATP; via amide nitrogen
Binding site1621ATP
Binding site2741ATP

Amino acid modifications

Modified residue411Phosphoserine Ref.31
Modified residue511Phosphoserine Ref.29
Modified residue2871Phosphothreonine Ref.35 Ref.47
Modified residue2881Phosphothreonine Ref.10 Ref.15 Ref.19 Ref.23 Ref.35 Ref.47 Ref.50
Modified residue3421Phosphoserine; by PKA and PAK Ref.23

Natural variations

Natural variant111G → R.
Corresponds to variant rs6069717 [ dbSNP | Ensembl ].
VAR_030840
Natural variant311F → I. Ref.3 Ref.54 Ref.55 Ref.56 Ref.57
Corresponds to variant rs2273535 [ dbSNP | Ensembl ].
VAR_030841
Natural variant501P → L. Ref.57
Corresponds to variant rs34572020 [ dbSNP | Ensembl ].
VAR_041127
Natural variant571V → I. Ref.2 Ref.54 Ref.55 Ref.57
Corresponds to variant rs1047972 [ dbSNP | Ensembl ].
VAR_030842
Natural variant1041S → L.
Corresponds to variant rs2230743 [ dbSNP | Ensembl ].
VAR_061745
Natural variant1551S → R in a colorectal adenocarcinoma sample; somatic mutation; reduces interaction with TPX2. Ref.51 Ref.57
VAR_041128
Natural variant1741V → M in a metastatic melanoma sample; somatic mutation; constitutively enhanced kinase activity. Ref.51 Ref.57
VAR_041129
Natural variant3731M → V. Ref.57
Corresponds to variant rs33923703 [ dbSNP | Ensembl ].
VAR_041130

Experimental info

Mutagenesis1621K → R: Loss of kinase activity. Ref.19 Ref.21
Mutagenesis1651F → A: Decreases the interaction with phosphatase type 1 isoforms. Ref.11
Mutagenesis1981G → N: Reduces interaction with TPX2. Reduces kinase activity tenfold. Promotes interaction with the AURKB binding partners INCENP and BIRC5 that are normally not bound by AURKA. Ref.36
Mutagenesis2051R → A: Reduces ubiquitination and proteasomal degradation. Ref.9
Mutagenesis2741D → N: Abolishes autophosphorylation. Ref.47
Mutagenesis2871T → A: No direct effect on catalytic activity. Ref.35
Mutagenesis2871T → E: Enhances interaction with TPX2. Ref.35
Mutagenesis2881T → D: Mimics phosphorylation state and increases kinase activity. Ref.10
Mutagenesis3461F → A: Decreases the interaction with phosphatase type 1 isoforms. Ref.11

Secondary structure

...................................................... 403
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O14965 [UniParc].

Last modified January 27, 2003. Version 2.
Checksum: 125F3594834CD157

FASTA40345,809
        10         20         30         40         50         60 
MDRSKENCIS GPVKATAPVG GPKRVLVTQQ FPCQNPLPVN SGQAQRVLCP SNSSQRVPLQ 

        70         80         90        100        110        120 
AQKLVSSHKP VQNQKQKQLQ ATSVPHPVSR PLNNTQKSKQ PLPSAPENNP EEELASKQKN 

       130        140        150        160        170        180 
EESKKRQWAL EDFEIGRPLG KGKFGNVYLA REKQSKFILA LKVLFKAQLE KAGVEHQLRR 

       190        200        210        220        230        240 
EVEIQSHLRH PNILRLYGYF HDATRVYLIL EYAPLGTVYR ELQKLSKFDE QRTATYITEL 

       250        260        270        280        290        300 
ANALSYCHSK RVIHRDIKPE NLLLGSAGEL KIADFGWSVH APSSRRTTLC GTLDYLPPEM 

       310        320        330        340        350        360 
IEGRMHDEKV DLWSLGVLCY EFLVGKPPFE ANTYQETYKR ISRVEFTFPD FVTEGARDLI 

       370        380        390        400 
SRLLKHNPSQ RPMLREVLEH PWITANSSKP SNCQNKESAS KQS 

« Hide

References

« Hide 'large scale' references
[1]"Cell cycle-dependent expression and spindle pole localization of a novel human protein kinase, Aik, related to Aurora of Drosophila and yeast Ipl1."
Kimura M., Kotani S., Hattori T., Sumi N., Yoshioka T., Todokoro K., Okano Y.
J. Biol. Chem. 272:13766-13771(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, SUBCELLULAR LOCATION.
Tissue: Blood.
[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], VARIANT ILE-57.
[3]"Tumour amplified kinase STK15/BTAK induces centrosome amplification, aneuploidy and transformation."
Zhou H., Kuang J., Zhong L., Kuo W.-L., Gray J.W., Sahin A., Brinkley B.R., Sen S.
Nat. Genet. 20:189-193(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-31.
Tissue: Mammary gland.
[4]"Mutational analysis of the STK15 gene in human tumors."
Wang L., Thibodeau S.N.
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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: Cervix, Colon, Kidney and Muscle.
[8]"A homologue of Drosophila aurora kinase is oncogenic and amplified in human colorectal cancers."
Bischoff J.R., Anderson L., Zhu Y., Mossie K., Ng L., Souza B., Schryver B., Flanagan P., Clairvoyant F., Ginther C., Chan C.S., Novotny M., Slamon D.J., Plowman G.D.
EMBO J. 17:3052-3065(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, FUNCTION, SUBCELLULAR LOCATION.
[9]"Degradation of human Aurora2 protein kinase by the anaphase-promoting complex-ubiquitin-proteasome pathway."
Honda K., Mihara H., Kato Y., Yamaguchi A., Tanaka H., Yasuda H., Furukawa K., Urano T.
Oncogene 19:2812-2819(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, PROTEASOMAL DEGRADATION, MUTAGENESIS OF ARG-205.
[10]"The mitotic serine/threonine kinase Aurora2/AIK is regulated by phosphorylation and degradation."
Walter A.O., Seghezzi W., Korver W., Sheung J., Lees E.
Oncogene 19:4906-4916(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT THR-288, MUTAGENESIS OF THR-288, UBIQUITINATION, ENZYME REGULATION.
[11]"Interaction and feedback regulation between STK15/BTAK/Aurora-A kinase and protein phosphatase 1 through mitotic cell division cycle."
Katayama H., Zhou H., Li Q., Tatsuka M., Sen S.
J. Biol. Chem. 276:46219-46224(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PPP1CA; PPP1CB AND PPP1CC, MUTAGENESIS OF PHE-165 AND PHE-346, PHOSPHORYLATION.
[12]"Molecular dynamics of Aurora-A kinase in living mitotic cells simultaneously visualized with histone H3 and nuclear membrane protein importinalpha."
Sugimoto K., Urano T., Zushi H., Inoue K., Tasaka H., Tachibana M., Dotsu M.
Cell Struct. Funct. 27:457-467(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[13]"Roles of aurora-A kinase in mitotic entry and G2 checkpoint in mammalian cells."
Marumoto T., Hirota T., Morisaki T., Kunitoku N., Zhang D., Ichikawa Y., Sasayama T., Kuninaka S., Mimori T., Tamaki N., Kimura M., Okano Y., Saya H.
Genes Cells 7:1173-1182(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION, PHOSPHORYLATION, ENZYME REGULATION.
[14]"Cell-cycle-dependent regulation of human aurora A transcription is mediated by periodic repression of E4TF1."
Tanaka M., Ueda A., Kanamori H., Ideguchi H., Yang J., Kitajima S., Ishigatsubo Y.
J. Biol. Chem. 277:10719-10726(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[15]"Aurora-A and an interacting activator, the LIM protein Ajuba, are required for mitotic commitment in human cells."
Hirota T., Kunitoku N., Sasayama T., Marumoto T., Zhang D., Nitta M., Hatakeyama K., Saya H.
Cell 114:585-598(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-288.
[16]"Aurora-A kinase maintains the fidelity of early and late mitotic events in HeLa cells."
Marumoto T., Honda S., Hara T., Nitta M., Hirota T., Kohmura E., Saya H.
J. Biol. Chem. 278:51786-51795(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"TACC1-chTOG-Aurora A protein complex in breast cancer."
Conte N., Delaval B., Ginestier C., Ferrand A., Isnardon D., Larroque C., Prigent C., Seraphin B., Jacquemier J., Birnbaum D.
Oncogene 22:8102-8116(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TACC1.
[18]"The centrosomal protein Lats2 is a phosphorylation target of Aurora-A kinase."
Toji S., Yabuta N., Hosomi T., Nishihara S., Kobayashi T., Suzuki S., Tamai K., Nojima H.
Genes Cells 9:383-397(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[19]"BRCA1 phosphorylation by Aurora-A in the regulation of G2 to M transition."
Ouchi M., Fujiuchi N., Sasai K., Katayama H., Minamishima Y.A., Ongusaha P.P., Deng C., Sen S., Lee S.W., Ouchi T.
J. Biol. Chem. 279:19643-19648(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BRCA1, PHOSPHORYLATION AT THR-288, MUTAGENESIS OF LYS-162.
[20]"Phosphorylation of CDC25B by Aurora-A at the centrosome contributes to the G2-M transition."
Dutertre S., Cazales M., Quaranta M., Froment C., Trabut V., Dozier C., Mirey G., Bouche J.P., Theis-Febvre N., Schmitt E., Monsarrat B., Prigent C., Ducommun B.
J. Cell Sci. 117:2523-2531(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[21]"Phosphorylation by aurora kinase A induces Mdm2-mediated destabilization and inhibition of p53."
Katayama H., Sasai K., Kawai H., Yuan Z.M., Bondaruk J., Suzuki F., Fujii S., Arlinghaus R.B., Czerniak B.A., Sen S.
Nat. Genet. 36:55-62(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF LYS-162, INTERACTION WITH TP53.
[22]"Over-expression of Aurora-A targets cytoplasmic polyadenylation element binding protein and promotes mRNA polyadenylation of Cdk1 and cyclin B1."
Sasayama T., Marumoto T., Kunitoku N., Zhang D., Tamaki N., Kohmura E., Saya H., Hirota T.
Genes Cells 10:627-638(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CPEB1.
[23]"The GIT-associated kinase PAK targets to the centrosome and regulates Aurora-A."
Zhao Z.S., Lim J.P., Ng Y.W., Lim L., Manser E.
Mol. Cell 20:237-249(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-288 AND SER-342.
[24]"Phosphorylation and stabilization of HURP by Aurora-A: implication of HURP as a transforming target of Aurora-A."
Yu C.T., Hsu J.M., Lee Y.C., Tsou A.P., Chou C.K., Huang C.Y.
Mol. Cell. Biol. 25:5789-5800(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, FUNCTION.
[25]"Mitotic activation of the kinase Aurora-A requires its binding partner Bora."
Hutterer A., Berdnik D., Wirtz-Peitz F., Zigman M., Schleiffer A., Knoblich J.A.
Dev. Cell 11:147-157(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BORA.
[26]"Aurora-A kinase regulates breast cancer associated gene 1 inhibition of centrosome-dependent microtubule nucleation."
Sankaran S., Crone D.E., Palazzo R.E., Parvin J.D.
Cancer Res. 67:11186-11194(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[27]"HEF1-dependent Aurora A activation induces disassembly of the primary cilium."
Pugacheva E.N., Jablonski S.A., Hartman T.R., Henske E.P., Golemis E.A.
Cell 129:1351-1363(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[28]"GEF-H1 modulates localized RhoA activation during cytokinesis under the control of mitotic kinases."
Birkenfeld J., Nalbant P., Bohl B.P., Pertz O., Hahn K.M., Bokoch G.M.
Dev. Cell 12:699-712(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARHGEF2.
[29]"Functional interaction of Aurora-A and PP2A during mitosis."
Horn V., Thelu J., Garcia A., Albiges-Rizo C., Block M.R., Viallet J.
Mol. Biol. Cell 18:1233-1241(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PPP2CA, PHOSPHORYLATION AT SER-51.
[30]"Antitumor activity of MLN8054, an orally active small-molecule inhibitor of Aurora A kinase."
Manfredi M.G., Ecsedy J.A., Meetze K.A., Balani S.K., Burenkova O., Chen W., Galvin K.M., Hoar K.M., Huck J.J., LeRoy P.J., Ray E.T., Sells T.B., Stringer B., Stroud S.G., Vos T.J., Weatherhead G.S., Wysong D.R., Zhang M., Bolen J.B., Claiborne C.F.
Proc. Natl. Acad. Sci. U.S.A. 104:4106-4111(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION.
[31]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[32]"Polo-like kinase-1 is activated by aurora A to promote checkpoint recovery."
Macurek L., Lindqvist A., Lim D., Lampson M.A., Klompmaker R., Freire R., Clouin C., Taylor S.S., Yaffe M.B., Medema R.H.
Nature 455:119-123(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[33]"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, AUTOPHOSPHORYLATION, INTERACTION WITH PARD3.
[34]"Plk1 and Aurora A regulate the depolymerase activity and the cellular localization of Kif2a."
Jang C.Y., Coppinger J.A., Seki A., Yates J.R. III, Fang G.
J. Cell Sci. 122:1334-1341(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KIF2A.
[35]"An essential role of the aPKC-Aurora A-NDEL1 pathway in neurite elongation by modulation of microtubule dynamics."
Mori D., Yamada M., Mimori-Kiyosue Y., Shirai Y., Suzuki A., Ohno S., Saya H., Wynshaw-Boris A., Hirotsune S.
Nat. Cell Biol. 11:1057-1068(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TPX2, PHOSPHORYLATION AT THR-287 AND THR-288, MUTAGENESIS OF THR-287.
[36]"A single amino acid change converts Aurora-A into Aurora-B-like kinase in terms of partner specificity and cellular function."
Fu J., Bian M., Liu J., Jiang Q., Zhang C.
Proc. Natl. Acad. Sci. U.S.A. 106:6939-6944(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TPX2, MUTAGENESIS OF GLY-198, SUBCELLULAR LOCATION, FUNCTION.
[37]"Pitchfork regulates primary cilia disassembly and left-right asymmetry."
Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B., Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H.
Dev. Cell 19:66-77(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PIFO, ACTIVATION BY PIFO.
[38]"Functional characterization of AIBp, a novel Aurora-A binding protein in centrosome structure and spindle formation."
Lieu A.S., Cheng T.S., Chou C.H., Wu C.H., Hsu C.Y., Huang C.Y., Chang L.K., Loh J.K., Chang C.S., Hsu C.M., Howng S.L., Hong Y.R.
Int. J. Oncol. 37:429-436(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AUNIP.
[39]"Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase."
Sanchez R., Pantoja-Uceda D., Prieto J., Diercks T., Marcaida M.J., Montoya G., Campos-Olivas R., Blanco F.J.
J. Biol. Chem. 285:22196-22201(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GADD45A.
[40]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[41]"PAR, a protein involved in the cell cycle, is functionally related to chromosomal passenger proteins."
Platica M., Ionescu A., Ivan E., Holland J.F., Mandeli J., Platica O.
Int. J. Oncol. 38:777-785(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH JTB.
[42]"The cellular geography of aurora kinases."
Carmena M., Earnshaw W.C.
Nat. Rev. Mol. Cell Biol. 4:842-854(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[43]"Aurora A, centrosome structure, and the centrosome cycle."
Lukasiewicz K.B., Lingle W.L.
Environ. Mol. Mutagen. 50:602-619(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[44]"Furry protein promotes Aurora A-mediated polo-like kinase 1 activation."
Ikeda M., Chiba S., Ohashi K., Mizuno K.
J. Biol. Chem. 287:27670-27681(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FRY.
[45]"Crystal structure of aurora-2, an oncogenic serine/threonine kinase."
Cheetham G.M., Knegtel R.M., Coll J.T., Renwick S.B., Swenson L., Weber P., Lippke J.A., Austen D.A.
J. Biol. Chem. 277:42419-42422(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 107-403 IN COMPLEX WITH ADENOSINE, CATALYTIC ACTIVITY.
[46]"Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography."
Nowakowski J., Cronin C.N., McRee D.E., Knuth M.W., Nelson C.G., Pavletich N.P., Rogers J., Sang B.C., Scheibe D.N., Swanson R.V., Thompson D.A.
Structure 10:1659-1667(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 125-391 IN COMPLEX WITH ADP.
[47]"Structural basis of Aurora-A activation by TPX2 at the mitotic spindle."
Bayliss R., Sardon T., Vernos I., Conti E.
Mol. Cell 12:851-862(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 122-403 IN COMPLEX WITH TPX2, MUTAGENESIS OF ASP-274, ACTIVE SITE, PHOSPHORYLATION AT THR-287 AND THR-288.
[48]"SAR and inhibitor complex structure determination of a novel class of potent and specific Aurora kinase inhibitors."
Heron N.M., Anderson M., Blowers D.P., Breed J., Eden J.M., Green S., Hill G.B., Johnson T., Jung F.H., McMiken H.H., Mortlock A.A., Pannifer A.D., Pauptit R.A., Pink J., Roberts N.J., Rowsell S.
Bioorg. Med. Chem. Lett. 16:1320-1323(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 123-401 IN COMPLEXES WITH ADPNP AND 5-AMINOPYRIMIDINYL QUINAZOLINE INHIBITOR, CATALYTIC ACTIVITY.
[49]"1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazoles: identification of a potent aurora kinase inhibitor with a favorable antitumor kinase inhibition profile."
Fancelli D., Moll J., Varasi M., Bravo R., Artico R., Berta D., Bindi S., Cameron A., Candiani I., Cappella P., Carpinelli P., Croci W., Forte B., Giorgini M.L., Klapwijk J., Marsiglio A., Pesenti E., Rocchetti M. expand/collapse author list , Roletto F., Severino D., Soncini C., Storici P., Tonani R., Zugnoni P., Vianello P.
J. Med. Chem. 49:7247-7251(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 100-403 IN COMPLEXES WITH SYNTHETIC INHIBITORS, FUNCTION.
[50]"Modulation of kinase-inhibitor interactions by auxiliary protein binding: crystallography studies on Aurora A interactions with VX-680 and with TPX2."
Zhao B., Smallwood A., Yang J., Koretke K., Nurse K., Calamari A., Kirkpatrick R.B., Lai Z.
Protein Sci. 17:1791-1797(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 125-391 IN COMPLEX WITH VX-680 AND TPX2, PHOSPHORYLATION AT THR-288, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT.
[51]"A cancer-associated aurora A mutant is mislocalized and misregulated due to loss of interaction with TPX2."
Bibby R.A., Tang C., Faisal A., Drosopoulos K., Lubbe S., Houlston R., Bayliss R., Linardopoulos S.
J. Biol. Chem. 284:33177-33184(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 127-388 IN COMPLEX WITH ADP, CHARACTERIZATION OF VARIANTS ARG-155 AND MET-174, INTERACTION WITH TPX2.
[52]"Structure-based drug design of novel Aurora kinase A inhibitors: structural basis for potency and specificity."
Coumar M.S., Leou J.S., Shukla P., Wu J.S., Dixit A.K., Lin W.H., Chang C.Y., Lien T.W., Tan U.K., Chen C.H., Hsu J.T., Chao Y.S., Wu S.Y., Hsieh H.P.
J. Med. Chem. 52:1050-1062(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 123-401 IN COMPLEX WITH SYNTHETIC INHIBITOR, CATALYTIC ACTIVITY.
[53]"A class of 2,4-bisanilinopyrimidine Aurora A inhibitors with unusually high selectivity against Aurora B."
Aliagas-Martin I., Burdick D., Corson L., Dotson J., Drummond J., Fields C., Huang O.W., Hunsaker T., Kleinheinz T., Krueger E., Liang J., Moffat J., Phillips G., Pulk R., Rawson T.E., Ultsch M., Walker L., Wiesmann C. expand/collapse author list , Zhang B., Zhu B.Y., Cochran A.G.
J. Med. Chem. 52:3300-3307(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 125-391 IN COMPLEX WITH SYNTHETIC INHIBITOR, CATALYTIC ACTIVITY.
[54]"Two functional coding single nucleotide polymorphisms in STK15 (Aurora-A) coordinately increase esophageal cancer risk."
Kimura M.T., Mori T., Conroy J., Nowak N.J., Satomi S., Tamai K., Nagase H.
Cancer Res. 65:3548-3554(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ILE-31 AND ILE-57.
[55]"Linkage disequilibrium and haplotype analysis of two single nucleotide polymorphisms in STK15 in Chinese."
Chen L., Ao X., Ren Q., Wang Z.N., Lu C., Xu Y., Jiang L., Luo Y., Xu H.M., Zhang X.
Yi Chuan Xue Bao 32:331-336(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ILE-31 AND ILE-57.
[56]"Aurora kinases A and B and familial breast cancer risk."
Tchatchou S., Wirtenberger M., Hemminki K., Sutter C., Meindl A., Wappenschmidt B., Kiechle M., Bugert P., Schmutzler R.K., Bartram C.R., Burwinkel B.
Cancer Lett. 247:266-272(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ILE-31.
[57]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-31; LEU-50; ILE-57; ARG-155; MET-174 AND VAL-373.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D84212 mRNA. Translation: BAA23592.1. Frameshift.
AF008551 mRNA. Translation: AAC12708.1.
AF011467 Genomic DNA. Translation: AAC23448.1.
AF011468 mRNA. Translation: AAC63902.1.
AF195947 expand/collapse EMBL AC list , AF195942, AF195943, AF195944, AF195945, AF195946 Genomic DNA. Translation: AAF29508.1.
AL121914 Genomic DNA. Translation: CAC12717.1.
CH471077 Genomic DNA. Translation: EAW75550.1.
CH471077 Genomic DNA. Translation: EAW75551.1.
CH471077 Genomic DNA. Translation: EAW75552.1.
CH471077 Genomic DNA. Translation: EAW75553.1.
CH471077 Genomic DNA. Translation: EAW75554.1.
CH471077 Genomic DNA. Translation: EAW75555.1.
CH471077 Genomic DNA. Translation: EAW75556.1.
CH471077 Genomic DNA. Translation: EAW75557.1.
CH471077 Genomic DNA. Translation: EAW75558.1.
CH471077 Genomic DNA. Translation: EAW75559.1.
CH471077 Genomic DNA. Translation: EAW75561.1.
CH471077 Genomic DNA. Translation: EAW75562.1.
BC001280 mRNA. Translation: AAH01280.1.
BC002499 mRNA. Translation: AAH02499.1.
BC006423 mRNA. Translation: AAH06423.1.
BC027464 mRNA. Translation: AAH27464.1.
CCDSCCDS13451.1.
PIRJC5974.
RefSeqNP_003591.2. NM_003600.2.
NP_940835.1. NM_198433.1.
NP_940836.1. NM_198434.1.
NP_940837.1. NM_198435.1.
NP_940838.1. NM_198436.1.
NP_940839.1. NM_198437.1.
XP_005260591.1. XM_005260534.1.
XP_006723935.1. XM_006723872.1.
UniGeneHs.250822.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MQ4X-ray1.90A125-391[»]
1MUOX-ray2.90A107-403[»]
1OL5X-ray2.50A122-403[»]
1OL6X-ray3.00A122-403[»]
1OL7X-ray2.75A122-403[»]
2BMCX-ray2.60A/B/C/D/E/F100-403[»]
2C6DX-ray2.20A124-398[»]
2C6EX-ray2.10A/B123-401[»]
2DWBX-ray2.50A122-403[»]
2J4ZX-ray2.00A/B100-403[»]
2J50X-ray3.00A/B126-403[»]
2NP8X-ray2.25A125-391[»]
2W1CX-ray3.24A122-389[»]
2W1DX-ray2.97A122-389[»]
2W1EX-ray2.93A122-389[»]
2W1FX-ray2.85A122-389[»]
2W1GX-ray2.71A122-389[»]
2WQEX-ray2.50A127-388[»]
2WTVX-ray2.40A/B/C/D122-403[»]
2WTWX-ray3.30A122-403[»]
2X6DX-ray2.80A122-403[»]
2X6EX-ray3.35A122-403[»]
2X81X-ray2.91A126-391[»]
2XNEX-ray2.80A122-392[»]
2XNGX-ray2.60A122-403[»]
2XRUX-ray2.90A126-403[»]
3COHX-ray2.70A/B124-391[»]
3E5AX-ray2.30A125-391[»]
3EFWX-ray2.29A/B125-391[»]
3FDNX-ray1.90A123-401[»]
3H0YX-ray2.50A124-391[»]
3H0ZX-ray2.92A/B/C124-391[»]
3H10X-ray2.20A/B/D124-391[»]
3HA6X-ray2.36A125-391[»]
3K5UX-ray2.35A123-401[»]
3LAUX-ray2.10A125-399[»]
3M11X-ray2.75A123-401[»]
3MYGX-ray2.40A125-391[»]
3NRMX-ray3.05A126-403[»]
3O50X-ray2.00A/B125-391[»]
3O51X-ray3.20A125-391[»]
3P9JX-ray2.80A125-391[»]
3QBNX-ray3.50A124-403[»]
3R21X-ray2.90A126-391[»]
3R22X-ray2.90A126-391[»]
3UNZX-ray2.80A/B123-401[»]
3UO4X-ray2.45A123-401[»]
3UO5X-ray2.70A123-401[»]
3UO6X-ray2.80A/B123-401[»]
3UODX-ray2.50A123-401[»]
3UOHX-ray2.80A/B123-401[»]
3UOJX-ray2.90A/B123-401[»]
3UOKX-ray2.95A/B123-401[»]
3UOLX-ray2.40A/B123-401[»]
3UP2X-ray2.30A123-401[»]
3UP7X-ray3.05A123-401[»]
3VAPX-ray2.66A125-391[»]
3W10X-ray2.70A126-403[»]
3W16X-ray2.80A126-403[»]
3W18X-ray2.50A/B126-403[»]
3W2CX-ray2.45A/C/E/G128-388[»]
4B0GX-ray2.50A122-403[»]
4BN1X-ray2.50A122-403[»]
4BYIX-ray2.60A122-403[»]
4BYJX-ray2.75A122-403[»]
4DEAX-ray2.45A123-401[»]
4DEBX-ray3.05A123-401[»]
4DEDX-ray3.05A123-401[»]
4DEEX-ray2.30A123-401[»]
4DHFX-ray2.80A/B126-391[»]
4JAIX-ray3.20A122-396[»]
4JAJX-ray2.70A122-396[»]
4JBOX-ray2.49A123-401[»]
4JBPX-ray2.45A123-401[»]
4JBQX-ray2.30A123-401[»]
ProteinModelPortalO14965.
SMRO14965. Positions 76-394.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112666. 88 interactions.
DIPDIP-33068N.
IntActO14965. 26 interactions.
MINTMINT-254096.
STRING9606.ENSP00000216911.

Chemistry

BindingDBO14965.
ChEMBLCHEMBL4722.
GuidetoPHARMACOLOGY1936.

PTM databases

PhosphoSiteO14965.

Proteomic databases

MaxQBO14965.
PaxDbO14965.
PRIDEO14965.

Protocols and materials databases

DNASU6790.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000312783; ENSP00000321591; ENSG00000087586.
ENST00000347343; ENSP00000216911; ENSG00000087586.
ENST00000371356; ENSP00000360407; ENSG00000087586.
ENST00000395909; ENSP00000379245; ENSG00000087586.
ENST00000395911; ENSP00000379247; ENSG00000087586.
ENST00000395913; ENSP00000379249; ENSG00000087586.
ENST00000395914; ENSP00000379250; ENSG00000087586.
ENST00000395915; ENSP00000379251; ENSG00000087586.
GeneID6790.
KEGGhsa:6790.
UCSCuc002xxd.1. human.

Organism-specific databases

CTD6790.
GeneCardsGC20M054944.
H-InvDBHIX0015930.
HGNCHGNC:11393. AURKA.
HPACAB001454.
HPA002636.
MIM603072. gene.
neXtProtNX_O14965.
PharmGKBPA36201.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG108519.
InParanoidO14965.
KOK11481.
OrthoDBEOG74FF1F.
PhylomeDBO14965.
TreeFamTF105331.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
SignaLinkO14965.

Gene expression databases

ArrayExpressO14965.
BgeeO14965.
CleanExHS_AURKA.
GenevestigatorO14965.

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

EvolutionaryTraceO14965.
GeneWikiAurora_A_kinase.
GenomeRNAi6790.
NextBio26512.
PROO14965.
SOURCESearch...

Entry information

Entry nameAURKA_HUMAN
AccessionPrimary (citable) accession number: O14965
Secondary accession number(s): E1P5F9 expand/collapse secondary AC list , O60445, O75873, Q9BQD6, Q9UPG5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 27, 2003
Last sequence update: January 27, 2003
Last modified: July 9, 2014
This is version 166 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM