O14965 (AURKA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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
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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	403 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. 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.34 Ref.35 Ref.36 Ref.38 Ref.39 Ref.40 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/C1orf88. Ref.10 Ref.13 Ref.30
Subunit structure	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/C1orf88. Ref.11 Ref.17 Ref.19 Ref.21 Ref.22 Ref.25 Ref.28 Ref.29 Ref.35 Ref.36 Ref.38 Ref.39 Ref.40 Ref.42 Ref.50 Ref.51
Subcellular location	Cytoplasm › cytoskeleton › centrosome. Cytoplasm › cytoskeleton › spindle 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.36 Ref.39 Ref.42
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. Phosphorylated upon DNA damage, probably by ATM or ATR. 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.31 Ref.32 Ref.33 Ref.35 Ref.37 Ref.38 Ref.47 Ref.50 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 process	Cell cycle Cell division Cilium biogenesis/degradation Mitosis
Cellular component	Cytoplasm Cytoskeleton Microtubule
Coding sequence diversity	Polymorphism
Disease	Proto-oncogene
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Traceable author statement. Source: Reactome cell division Inferred from electronic annotation. Source: UniProtKB-KW cell projection organization Inferred from electronic annotation. Source: UniProtKB-KW mitosis Traceable author statement. Source: ProtInc phosphatidylinositol-mediated signaling Non-traceable author statement. Source: UniProtKB positive regulation of mitosis Traceable author statement Ref.44. Source: UniProtKB protein autophosphorylation Traceable author statement Ref.44. Source: UniProtKB regulation of centrosome cycle Traceable author statement Ref.44. Source: UniProtKB regulation of protein stability Inferred from mutant phenotype Ref.24. Source: UniProtKB spindle organization Non-traceable author statement. Source: UniProtKB
Cellular component	cytosol Traceable author statement. Source: Reactome midbody Traceable author statement Ref.44. Source: UniProtKB nucleus Inferred from direct assay. Source: BHF-UCL perinuclear region of cytoplasm Inferred from direct assay. Source: BHF-UCL spindle microtubule Inferred from direct assay Ref.51. Source: BHF-UCL spindle pole centrosome Inferred from direct assay Ref.51. Source: BHF-UCL
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein kinase binding Inferred from physical interaction Ref.34. Source: UniProtKB protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine/tyrosine kinase activity Traceable author statement Ref.44. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AURKAIP1	Q9NWT8	2	EBI-448680,EBI-448665
MYCN	P04198	2	EBI-448680,EBI-878369

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 403

403

Aurora kinase A

PRO_0000086692

Regions

Domain

133 – 383

251

Protein kinase

Nucleotide binding

210 – 213

4

ATP

Region

280 – 293

14

Activation segment

Sites

Active site

256

1

Proton acceptor Ref.47

Binding site

143

1

ATP; via amide nitrogen

Binding site

162

1

ATP

Binding site

274

1

ATP

Amino acid modifications

Modified residue

41

1

Phosphoserine Ref.33

Modified residue

51

1

Phosphoserine Ref.29 Ref.32 Ref.33

Modified residue

53

1

Phosphoserine Ref.37

Modified residue

83

1

Phosphoserine Ref.33

Modified residue

287

1

Phosphothreonine Ref.38 Ref.47

Modified residue

288

1

Phosphothreonine Ref.10 Ref.15 Ref.19 Ref.23 Ref.38 Ref.47 Ref.50

Modified residue

342

1

Phosphoserine; by PKA and PAK Ref.23

Modified residue

369

1

Phosphoserine Ref.31

Natural variations

Natural variant

11

1

G → R.
Corresponds to variant rs6069717 [ dbSNP | Ensembl ].

VAR_030840

Natural variant

31

1

F → I. Ref.3 Ref.54 Ref.55 Ref.56 Ref.57
Corresponds to variant rs2273535 [ dbSNP | Ensembl ].

VAR_030841

Natural variant

50

1

P → L. Ref.57
Corresponds to variant rs34572020 [ dbSNP | Ensembl ].

VAR_041127

Natural variant

57

1

V → I. Ref.2 Ref.54 Ref.55 Ref.57
Corresponds to variant rs1047972 [ dbSNP | Ensembl ].

VAR_030842

Natural variant

104

1

S → L.
Corresponds to variant rs2230743 [ dbSNP | Ensembl ].

VAR_061745

Natural variant

155

1

S → R in a colorectal adenocarcinoma sample; somatic mutation; reduces interaction with TPX2. Ref.51 Ref.57

VAR_041128

Natural variant

174

1

V → M in a metastatic melanoma sample; somatic mutation; constitutively enhanced kinase activity. Ref.51 Ref.57

VAR_041129

Natural variant

373

1

M → V. Ref.57
Corresponds to variant rs33923703 [ dbSNP | Ensembl ].

VAR_041130

Experimental info

Mutagenesis

162

1

K → R: Loss of kinase activity. Ref.19 Ref.21 Ref.38

Mutagenesis

165

1

F → A: Decreases the interaction with phosphatase type 1 isoforms. Ref.11 Ref.38

Mutagenesis

198

1

G → 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.38 Ref.39

Mutagenesis

205

1

R → A: Reduces ubiquitination and proteasomal degradation. Ref.9 Ref.38

Mutagenesis

274

1

D → N: Abolishes autophosphorylation. Ref.38 Ref.47

Mutagenesis

287

1

T → A: No direct effect on catalytic activity. Ref.38

Mutagenesis

287

1

T → E: Enhances interaction with TPX2. Ref.38

Mutagenesis

288

1

T → D: Mimics phosphorylation state and increases kinase activity. Ref.10 Ref.38

Mutagenesis

346

1

F → A: Decreases the interaction with phosphatase type 1 isoforms. Ref.11 Ref.38

Secondary structure

1

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403

Helix Strand Turn

Details...

Helix

130 – 132

3

Beta strand

133 – 141

9

Beta strand

143 – 152

10

Turn

153 – 155

3

Beta strand

158 – 165

8

Helix

166 – 172

7

Helix

175 – 187

13

Beta strand

196 – 201

6

Beta strand

203 – 210

8

Helix

218 – 225

8

Helix

230 – 249

20

Helix

259 – 261

3

Beta strand

262 – 264

3

Beta strand

270 – 272

3

Helix

275 – 277

3

Beta strand

279 – 283

5

Helix

298 – 301

4

Helix

309 – 324

16

Helix

334 – 343

10

Helix

354 – 363

10

Helix

368 – 370

3

Helix

374 – 378

5

Helix

381 – 386

6

Sequences

	Sequence		Length	Mass (Da)
	O14965 [UniParc]. Last modified January 27, 2003. Version 2. Checksum: 125F3594834CD157	FASTA	403	45,809
	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

References

	« Hide 'large scale' referencesShow '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: 9153231] [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: 9514916] [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: 9771714] [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. , 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: 11780052] [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. , 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: 15489334] [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: 9606188] [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: 10851084] [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: 11039908] [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: 11551964] [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: 12576638] [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: 12390251] [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: 11790771] [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: 13678582] [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: 14523000] [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: 14603251] [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: 15147269] [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: 14990569] [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: 15128871] [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: 14702041] [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: 15966895] [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: 16246726] [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: 15987997] [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: 16890155] [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: 18056443] [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: 17604723] [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: 17488622] [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: 17229885] [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: 17360485] [Abstract] Cited for: FUNCTION, ENZYME REGULATION.
[31]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-369, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[32]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[33]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-51 AND SER-83, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[34]	"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: 18615013] [Abstract] Cited for: FUNCTION.
[35]	"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: 19812038] [Abstract] Cited for: FUNCTION, AUTOPHOSPHORYLATION, INTERACTION WITH PARD3.
[36]	"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: 19351716] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KIF2A.
[37]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53, MASS SPECTROMETRY.
[38]	"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: 19668197] [Abstract] Cited for: FUNCTION, INTERACTION WITH TPX2, PHOSPHORYLATION AT THR-287 AND THR-288, MUTAGENESIS OF THR287.
[39]	"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: 19357306] [Abstract] Cited for: INTERACTION WITH TPX2, MUTAGENESIS OF GLY-198, SUBCELLULAR LOCATION, FUNCTION.
[40]	"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: 20643351] [Abstract] Cited for: FUNCTION, INTERACTION WITH PIFO, ACTIVATION BY PIFO.
[41]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[42]	"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: 21225229] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH JTB.
[43]	"The cellular geography of aurora kinases." Carmena M., Earnshaw W.C. Nat. Rev. Mol. Cell Biol. 4:842-854(2003) [PubMed: 14625535] [Abstract] Cited for: REVIEW ON FUNCTION.
[44]	"Aurora A, centrosome structure, and the centrosome cycle." Lukasiewicz K.B., Lingle W.L. Environ. Mol. Mutagen. 50:602-619(2009) [PubMed: 19774610] [Abstract] Cited for: REVIEW ON FUNCTION.
[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: 12237287] [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: 12467573] [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: 14580337] [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: 16337122] [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. , Roletto F., Severino D., Soncini C., Storici P., Tonani R., Zugnoni P., Vianello P. J. Med. Chem. 49:7247-7251(2006) [PubMed: 17125279] [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: 18662907] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 125-391 IN COMPLEX WITH VX-680 AND TPX2, PHOSPHORYLATION AT THR-288, 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: 19801554] [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: 19140666] [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. , Zhang B., Zhu B.Y., Cochran A.G. J. Med. Chem. 52:3300-3307(2009) [PubMed: 19402633] [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: 15867347] [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: 16011022] [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: 16762494] [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. , 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: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-31; LEU-50; ILE-57; ARG-155; MET-174 AND VAL-373.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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 , 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.

IPI

IPI00298940.

PIR

JC5974.

RefSeq

NP_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.

UniGene

Hs.250822.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MQ4	X-ray	1.90	A	125-391	[»]
1MUO	X-ray	2.90	A	107-403	[»]
1OL5	X-ray	2.50	A	122-403	[»]
1OL6	X-ray	3.00	A	122-403	[»]
1OL7	X-ray	2.75	A	122-403	[»]
2BMC	X-ray	2.60	A/B/C/D/E/F	100-403	[»]
2C6D	X-ray	2.20	A	124-398	[»]
2C6E	X-ray	2.10	A/B	123-401	[»]
2DWB	X-ray	2.50	A	122-403	[»]
2J4Z	X-ray	2.00	A/B	100-403	[»]
2J50	X-ray	3.00	A/B	126-403	[»]
2NP8	X-ray	2.25	A	125-391	[»]
2W1C	X-ray	3.24	A	122-389	[»]
2W1D	X-ray	2.97	A	122-389	[»]
2W1E	X-ray	2.93	A	122-389	[»]
2W1F	X-ray	2.85	A	122-389	[»]
2W1G	X-ray	2.71	A	122-389	[»]
2WQE	X-ray	2.50	A	127-388	[»]
2WTV	X-ray	2.40	A/B/C/D	122-403	[»]
2WTW	X-ray	3.30	A	122-403	[»]
2X6D	X-ray	2.80	A	122-403	[»]
2X6E	X-ray	3.35	A	122-403	[»]
2X81	X-ray	2.91	A	125-391	[»]
2XNE	X-ray	2.80	A	122-392	[»]
2XNG	X-ray	2.60	A	122-403	[»]
2XRU	X-ray	2.90	A	126-403	[»]
3COH	X-ray	2.70	A/B	125-391	[»]
3E5A	X-ray	2.30	A	125-391	[»]
3EFW	X-ray	2.29	A/B	1-403	[»]
3FDN	X-ray	1.90	A	123-401	[»]
3H0Y	X-ray	2.50	A	125-391	[»]
3H0Z	X-ray	2.92	A/B/C	125-391	[»]
3H10	X-ray	2.20	A/B/D	125-391	[»]
3HA6	X-ray	2.36	A	125-391	[»]
3K5U	X-ray	2.35	A	123-401	[»]
3LAU	X-ray	2.10	A	125-399	[»]
3M11	X-ray	2.75	A	123-401	[»]
3MYG	X-ray	2.40	A	125-391	[»]
3NRM	X-ray	3.05	A	126-403	[»]
3O50	X-ray	2.00	A/B	125-391	[»]
3O51	X-ray	3.20	A	125-391	[»]
3P9J	X-ray	2.80	A	125-391	[»]
3R21	X-ray	2.90	A	126-391	[»]
3R22	X-ray	2.90	A	126-391	[»]

ProteinModelPortal

O14965.

SMR

O14965. Positions 126-394.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33068N.

IntAct

O14965. 16 interactions.

STRING

O14965.

PTM databases

PhosphoSite

O14965.

Proteomic databases

PRIDE

O14965.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000312783; ENSP00000321591; ENSG00000087586.
ENST00000347343; ENSP00000216911; ENSG00000087586.
ENST00000371356; ENSP00000360407; ENSG00000087586.
ENST00000395909; ENSP00000379245; ENSG00000087586.
ENST00000395911; ENSP00000379247; ENSG00000087586.
ENST00000395913; ENSP00000379249; ENSG00000087586.
ENST00000395914; ENSP00000379250; ENSG00000087586.
ENST00000395915; ENSP00000379251; ENSG00000087586.

GeneID

6790.

KEGG

hsa:6790.

Organism-specific databases

CTD

6790.

GeneCards

GC20M054944.

H-InvDB

HIX0015930.

HGNC

HGNC:11393. AURKA.

HPA

CAB001454.
HPA002636.

MIM

603072. gene.

neXtProt

NX_O14965.

PharmGKB

PA36201.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG755340.

HOVERGEN

HBG108519.

InParanoid

O14965.

OrthoDB

EOG4HX512.

PhylomeDB

O14965.

Enzyme and pathway databases

Pathway_Interaction_DB

aurora_a_pathway. Aurora A signaling.
aurora_b_pathway. Aurora B signaling.
aurora_kinase_pathway. Signaling by Aurora kinases.

Reactome

REACT_152. Cell Cycle, Mitotic.

Gene expression databases

ArrayExpress

O14965.

Bgee

O14965.

CleanEx

HS_AURKA.

Genevestigator

O14965.

GermOnline

ENSG00000087586. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_kinase-like_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR002290. Ser/Thr_kinase_dom.
[Graphical view]

KO

K11481.

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...

Other

BindingDB

O14965.

NextBio

26512.

SOURCE

Search...

Entry information

Entry name

AURKA_HUMAN

Accession

Primary (citable) accession number: O14965
Secondary accession number(s): E1P5F9 , O60445, O75873, Q9BQD6, Q9UPG5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 27, 2003
Last sequence update:	January 27, 2003
Last modified:	January 25, 2012
This is version 139 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.