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Aurora kinase A (EC 2.7.11.1) (Aurora 2) (Aurora family kinase 1) (Aurora/IPL1-related kinase 1) (ARK-1) (Aurora-related kinase 1) (Ipl1- and aurora-related kinase 1) (Serine/threonine-protein kinase 6) (Serine/threonine-protein kinase Ayk1) (Serine/threonine-protein kinase aurora-A)

 AURKA_MOUSE             Reviewed;         395 AA.
P97477; O35624; Q8C3H8; Q91YU4;
27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
22-NOV-2017, entry version 171.
RecName: Full=Aurora kinase A;
EC=2.7.11.1 {ECO:0000250|UniProtKB:P04198};
AltName: Full=Aurora 2;
AltName: Full=Aurora family kinase 1;
AltName: Full=Aurora/IPL1-related kinase 1;
Short=ARK-1;
Short=Aurora-related kinase 1;
AltName: Full=Ipl1- and aurora-related kinase 1;
AltName: Full=Serine/threonine-protein kinase 6;
AltName: Full=Serine/threonine-protein kinase Ayk1;
AltName: Full=Serine/threonine-protein kinase aurora-A;
Name=Aurka;
Synonyms=Aik, Airk, Ark1, Aura, Ayk1, Btak, Iak1, Stk15, Stk6;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INDUCTION, TISSUE SPECIFICITY,
SUBCELLULAR LOCATION, AND FUNCTION.
STRAIN=BALB/cJ; TISSUE=Testis;
PubMed=9245792; DOI=10.1083/jcb.138.3.643;
Gopalan G., Chan C.S.M., Donovan P.J.;
"A novel mammalian, mitotic spindle-associated kinase is related to
yeast and fly chromosome segregation regulators.";
J. Cell Biol. 138:643-656(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=9205101; DOI=10.1038/sj.onc.1201144;
Yanai A., Arama E., Kilfin G., Motro B.;
"ayk1, a novel mammalian gene related to Drosophila aurora centrosome
separation kinase, is specifically expressed during meiosis.";
Oncogene 14:2943-2950(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=BALB/cJ;
PubMed=9514916; DOI=10.1006/bbrc.1998.8250;
Shindo M., Nakano H., Kuroyanagi H., Shirasawa T., Mihara M.,
Gilbert D.J., Jenkins N.A., Copeland N.G., Yagita H., Okumura K.;
"cDNA cloning, expression, subcellular localization, and chromosomal
assignment of mammalian aurora homologues, aurora-related kinase (ARK)
1 and 2.";
Biochem. Biophys. Res. Commun. 244:285-292(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Heart;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
UBIQUITINATION BY CHFR.
PubMed=15793587; DOI=10.1038/ng1538;
Yu X., Minter-Dykhouse K., Malureanu L., Zhao W.-M., Zhang D.,
Merkle C.J., Ward I.M., Saya H., Fang G., van Deursen J., Chen J.;
"Chfr is required for tumor suppression and Aurora A regulation.";
Nat. Genet. 37:401-406(2005).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=19075002; DOI=10.1128/MCB.01062-08;
Cowley D.O., Rivera-Perez J.A., Schliekelman M., He Y.J., Oliver T.G.,
Lu L., O'Quinn R., Salmon E.D., Magnuson T., Van Dyke T.;
"Aurora-A kinase is essential for bipolar spindle formation and early
development.";
Mol. Cell. Biol. 29:1059-1071(2009).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=19668197; DOI=10.1038/ncb1919;
Mori D., Yamada M., Mimori-Kiyosue Y., Shirai Y., Suzuki A., Ohno S.,
Saya H., Wynshaw-Boris A., Hirotsune S.;
"An essential role of the aPKC-Aurora A-NDEL1 pathway in neurite
elongation by modulation of microtubule dynamics.";
Nat. Cell Biol. 11:1057-1068(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
FUNCTION, INTERACTION WITH PIFO, AND ACTIVATION BY PIFO.
PubMed=20643351; DOI=10.1016/j.devcel.2010.06.005;
Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B.,
Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H.;
"Pitchfork regulates primary cilia disassembly and left-right
asymmetry.";
Dev. Cell 19:66-77(2010).
[11]
UBIQUITINATION, AND INTERACTION WITH FBXL7.
PubMed=22306998; DOI=10.4161/cc.11.4.19171;
Coon T.A., Glasser J.R., Mallampalli R.K., Chen B.B.;
"Novel E3 ligase component FBXL7 ubiquitinates and degrades Aurora A,
causing mitotic arrest.";
Cell Cycle 11:721-729(2012).
[12]
INTERACTION WITH FRY.
PubMed=22753416; DOI=10.1074/jbc.M112.378968;
Ikeda M., Chiba S., Ohashi K., Mizuno K.;
"Furry protein promotes Aurora A-mediated polo-like kinase 1
activation.";
J. Biol. Chem. 287:27670-27681(2012).
[13]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 116-381 IN COMPLEX WITH
SYNTHETIC INHIBITOR.
PubMed=18579375; DOI=10.1016/j.bmcl.2008.06.011;
Cancilla M.T., He M.M., Viswanathan N., Simmons R.L., Taylor M.,
Fung A.D., Cao K., Erlanson D.A.;
"Discovery of an Aurora kinase inhibitor through site-specific dynamic
combinatorial chemistry.";
Bioorg. Med. Chem. Lett. 18:3978-3981(2008).
[14]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 116-381 IN COMPLEX WITH
SYNTHETIC INHIBITOR.
PubMed=18678489; DOI=10.1016/j.bmcl.2008.07.073;
Oslob J.D., Romanowski M.J., Allen D.A., Baskaran S., Bui M.,
Elling R.A., Flanagan W.M., Fung A.D., Hanan E.J., Harris S.,
Heumann S.A., Hoch U., Jacobs J.W., Lam J., Lawrence C.E.,
McDowell R.S., Nannini M.A., Shen W., Silverman J.A., Sopko M.M.,
Tangonan B.T., Teague J., Yoburn J.C., Yu C.H., Zhong M.,
Zimmerman K.M., O'Brien T., Lew W.;
"Discovery of a potent and selective aurora kinase inhibitor.";
Bioorg. Med. Chem. Lett. 18:4880-4884(2008).
[15]
SUBCELLULAR LOCATION.
PubMed=23807208; DOI=10.1007/s00018-013-1401-6;
Kypri E., Christodoulou A., Maimaris G., Lethan M., Markaki M.,
Lysandrou C., Lederer C.W., Tavernarakis N., Geimer S., Pedersen L.B.,
Santama N.;
"The nucleotide-binding proteins Nubp1 and Nubp2 are negative
regulators of ciliogenesis.";
Cell. Mol. Life Sci. 71:517-538(2014).
-!- 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. {ECO:0000269|PubMed:19075002,
ECO:0000269|PubMed:19668197, ECO:0000269|PubMed:20643351,
ECO:0000269|PubMed:9245792}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000250|UniProtKB:O14965}.
-!- 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 (By similarity). Activated during the early
phase of cilia disassembly in the presence of PIFO. {ECO:0000250}.
-!- SUBUNIT: 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 GADD45A, competing with its oligomerization (By similarity).
Interacts with FBXL7 and PIFO. Interacts (via C-terminus) with
AUNIP (via C-terminus) (By similarity). Identified in a complex
with AUNIP and NIN (By similarity). Interacts with SIRT2 (By
similarity). Interacts with FRY; this interaction facilitates
AURKA-mediated PLK1 phosphorylation. Interacts with MYCN;
interaction is phospho-independent and triggers AURKA activation;
AURKA competes with FBXW7 for binding to unphosphorylated MYCN but
not for binding to phosphorylated MYCN (By similarity). Interacts
with HNRNPU (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:O14965, ECO:0000269|PubMed:18579375,
ECO:0000269|PubMed:18678489, ECO:0000269|PubMed:20643351,
ECO:0000269|PubMed:22306998, ECO:0000269|PubMed:22753416}.
-!- INTERACTION:
P04198:MYCN (xeno); NbExp=2; IntAct=EBI-6895349, EBI-878369;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:19668197,
ECO:0000269|PubMed:20643351}. Cytoplasm, cytoskeleton, spindle
pole {ECO:0000269|PubMed:19075002, ECO:0000269|PubMed:9245792}.
Cytoplasm, cytoskeleton, cilium basal body
{ECO:0000269|PubMed:23807208}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome, centriole
{ECO:0000269|PubMed:23807208}. Note=Localizes on centrosomes in
interphase cells and at each spindle pole in mitosis
(PubMed:9245792). Associates with both the pericentriolar material
(PCM) and centrioles (By similarity). Colocalized with SIRT2 at
centrosome (By similarity). Detected at the neurite hillock in
developing neurons (PubMed:19668197).
{ECO:0000250|UniProtKB:O14965, ECO:0000269|PubMed:19668197,
ECO:0000269|PubMed:9245792}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P97477-1; Sequence=Displayed;
Name=2;
IsoId=P97477-2; Sequence=VSP_004871;
Note=May be less abundant or less stable.;
-!- TISSUE SPECIFICITY: Detected in embryonic neurons in dorsal root
ganglia and brain cortex (at protein level). Highly expressed in
testis, in about one third of the seminiferous tubules. Expression
is restricted to specific spermatocytes nearing completion of
prophase, with levels falling off on transition to elongated
spermatids. Highly expressed in the ovary, expression in the
oocyte starts around the transition to large growing follicle.
Abundant expression is seen in the proliferating granulosa and
thecal cells of the growing follicle, and in the young corpus
luteum. Very weakly expressed in spleen and intestine.
{ECO:0000269|PubMed:19668197, ECO:0000269|PubMed:9245792}.
-!- DEVELOPMENTAL STAGE: At 7.5-9.5 dpc expressed evenly all over the
embryo. At later stages, expression is mainly restricted to
proliferating zones. The highest levels of expression at mid-
embryonic development (13.5 dpc) were observed in the liver, lung,
kidney and back (trapezius) muscle and all regions in active
proliferation.
-!- INDUCTION: expression is cell cycle regulated and peaks at phase
G2/M. {ECO:0000269|PubMed:9245792}.
-!- PTM: Activated by phosphorylation at Thr-279; this brings about a
change in the conformation of the activation segment.
Phosphorylation at Thr-279 varies during the cell cycle and is
highest during M phase. Autophosphorylated at Thr-279 upon TPX2
binding. Thr-279 can be phosphorylated by several kinases,
including PAK and PKA. Protein phosphatase type 1 (PP1) binds
AURKA and inhibits its activity by dephosphorylating Thr-279
during mitosis. Phosphorylation at Ser-333 decreases the kinase
activity. PPP2CA controls degradation by dephosphorylating Ser-52
at the end of mitosis (By similarity). {ECO:0000250}.
-!- PTM: 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. {ECO:0000250, ECO:0000269|PubMed:15793587,
ECO:0000269|PubMed:22306998}.
-!- DISRUPTION PHENOTYPE: Death at the blastocyst stage due to mitotic
defects and failure of cell proliferation.
{ECO:0000269|PubMed:19075002}.
-!- 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.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. Aurora subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=BAC39557.1; Type=Frameshift; Positions=382; Evidence={ECO:0000305};
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EMBL; U80932; AAB62982.1; -; mRNA.
EMBL; AF007817; AAB63205.1; -; mRNA.
EMBL; U69106; AAC12682.1; -; mRNA.
EMBL; AK085861; BAC39557.1; ALT_FRAME; mRNA.
EMBL; BC005425; AAH05425.1; -; mRNA.
EMBL; BC014711; AAH14711.1; -; mRNA.
CCDS; CCDS17129.1; -. [P97477-2]
CCDS; CCDS71204.1; -. [P97477-1]
PIR; JC5975; JC5975.
RefSeq; NP_001278114.1; NM_001291185.1. [P97477-1]
RefSeq; NP_035627.1; NM_011497.4. [P97477-2]
RefSeq; XP_006499138.1; XM_006499075.2. [P97477-1]
UniGene; Mm.249363; -.
PDB; 3D14; X-ray; 1.90 A; A=116-381.
PDB; 3D15; X-ray; 2.30 A; A=116-381.
PDB; 3D2I; X-ray; 2.90 A; A=116-381.
PDB; 3D2K; X-ray; 2.50 A; A=116-381.
PDB; 3DAJ; X-ray; 2.00 A; A=116-381.
PDB; 3DJ5; X-ray; 1.80 A; A=116-381.
PDB; 3DJ6; X-ray; 1.70 A; A=116-381.
PDB; 3DJ7; X-ray; 2.80 A; A=116-381.
PDBsum; 3D14; -.
PDBsum; 3D15; -.
PDBsum; 3D2I; -.
PDBsum; 3D2K; -.
PDBsum; 3DAJ; -.
PDBsum; 3DJ5; -.
PDBsum; 3DJ6; -.
PDBsum; 3DJ7; -.
ProteinModelPortal; P97477; -.
SMR; P97477; -.
BioGrid; 203548; 7.
IntAct; P97477; 1.
STRING; 10090.ENSMUSP00000028997; -.
BindingDB; P97477; -.
ChEMBL; CHEMBL2211; -.
iPTMnet; P97477; -.
PhosphoSitePlus; P97477; -.
EPD; P97477; -.
PaxDb; P97477; -.
PeptideAtlas; P97477; -.
PRIDE; P97477; -.
Ensembl; ENSMUST00000028997; ENSMUSP00000028997; ENSMUSG00000027496. [P97477-2]
Ensembl; ENSMUST00000109139; ENSMUSP00000104767; ENSMUSG00000027496. [P97477-1]
Ensembl; ENSMUST00000109140; ENSMUSP00000104768; ENSMUSG00000027496. [P97477-1]
GeneID; 20878; -.
KEGG; mmu:20878; -.
UCSC; uc008ocn.2; mouse. [P97477-2]
UCSC; uc008oco.2; mouse. [P97477-1]
CTD; 6790; -.
MGI; MGI:894678; Aurka.
eggNOG; KOG0580; Eukaryota.
eggNOG; ENOG410XNRB; LUCA.
GeneTree; ENSGT00870000136439; -.
HOVERGEN; HBG108519; -.
InParanoid; P97477; -.
KO; K11481; -.
OMA; QATSVPH; -.
OrthoDB; EOG091G0EU2; -.
PhylomeDB; P97477; -.
TreeFam; TF105331; -.
Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-MMU-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-MMU-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-MMU-8854518; AURKA Activation by TPX2.
Reactome; R-MMU-8854521; Interaction between PHLDA1 and AURKA.
EvolutionaryTrace; P97477; -.
PRO; PR:P97477; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027496; -.
CleanEx; MM_AURKA; -.
ExpressionAtlas; P97477; baseline and differential.
Genevisible; P97477; MM.
GO; GO:0043203; C:axon hillock; IDA:MGI.
GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
GO; GO:0005813; C:centrosome; IDA:MGI.
GO; GO:0032133; C:chromosome passenger complex; IBA:GO_Central.
GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
GO; GO:0000780; C:condensed nuclear chromosome, centromeric region; IBA:GO_Central.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0042585; C:germinal vesicle; IDA:MGI.
GO; GO:0072687; C:meiotic spindle; IDA:MGI.
GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
GO; GO:0005815; C:microtubule organizing center; IGI:MGI.
GO; GO:0072686; C:mitotic spindle; IDA:MGI.
GO; GO:0097431; C:mitotic spindle pole; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0045120; C:pronucleus; IDA:MGI.
GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
GO; GO:0051233; C:spindle midzone; IBA:GO_Central.
GO; GO:0031616; C:spindle pole centrosome; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0035174; F:histone serine kinase activity; IMP:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:MGI.
GO; GO:0009948; P:anterior/posterior axis specification; IMP:MGI.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0007098; P:centrosome cycle; IGI:MGI.
GO; GO:0051642; P:centrosome localization; IMP:MGI.
GO; GO:0097421; P:liver regeneration; ISO:MGI.
GO; GO:0051321; P:meiotic cell cycle; IMP:MGI.
GO; GO:0000212; P:meiotic spindle organization; IMP:MGI.
GO; GO:0000226; P:microtubule cytoskeleton organization; IGI:MGI.
GO; GO:0000278; P:mitotic cell cycle; IMP:MGI.
GO; GO:0007100; P:mitotic centrosome separation; IMP:MGI.
GO; GO:0007052; P:mitotic spindle organization; IMP:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
GO; GO:1990138; P:neuron projection extension; IGI:MGI.
GO; GO:1900195; P:positive regulation of oocyte maturation; IMP:MGI.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:MGI.
GO; GO:0071539; P:protein localization to centrosome; IMP:MGI.
GO; GO:0006468; P:protein phosphorylation; IGI:MGI.
GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
GO; GO:0009611; P:response to wounding; ISO:MGI.
GO; GO:0007057; P:spindle assembly involved in female meiosis I; IMP:MGI.
GO; GO:0007051; P:spindle organization; ISO:MGI.
InterPro; IPR030616; Aur.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR24350; PTHR24350; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell cycle;
Cell division; Cell projection; Cilium; Cilium biogenesis/degradation;
Complete proteome; Cytoplasm; Cytoskeleton; Isopeptide bond; Kinase;
Microtubule; Mitosis; Nucleotide-binding; Phosphoprotein;
Proto-oncogene; Reference proteome; Serine/threonine-protein kinase;
Transferase; Ubl conjugation.
CHAIN 1 395 Aurora kinase A.
/FTId=PRO_0000086693.
DOMAIN 124 374 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 201 204 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 251 252 ATP. {ECO:0000250|UniProtKB:O14965}.
REGION 271 284 Activation segment. {ECO:0000250}.
ACT_SITE 247 247 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 134 134 ATP; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
BINDING 153 153 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 265 265 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 40 40 Phosphoserine.
{ECO:0000250|UniProtKB:O14965}.
MOD_RES 50 50 Phosphoserine.
{ECO:0000250|UniProtKB:O14965}.
MOD_RES 278 278 Phosphothreonine.
{ECO:0000250|UniProtKB:O14965}.
MOD_RES 279 279 Phosphothreonine.
{ECO:0000250|UniProtKB:O14965}.
MOD_RES 333 333 Phosphoserine; by PKA and PAK.
{ECO:0000250|UniProtKB:O14965}.
CROSSLNK 249 249 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O14965}.
VAR_SEQ 1 1 M -> MAVEGEPGCCKRIGKAVWRRGDM (in isoform
2). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9245792}.
/FTId=VSP_004871.
CONFLICT 234 234 A -> T (in Ref. 1; AAB63205).
{ECO:0000305}.
HELIX 121 123 {ECO:0000244|PDB:3DJ6}.
STRAND 124 129 {ECO:0000244|PDB:3DJ6}.
HELIX 131 133 {ECO:0000244|PDB:3DJ6}.
STRAND 136 143 {ECO:0000244|PDB:3DJ6}.
TURN 144 146 {ECO:0000244|PDB:3DJ6}.
STRAND 149 156 {ECO:0000244|PDB:3DJ6}.
HELIX 157 163 {ECO:0000244|PDB:3DJ6}.
HELIX 166 176 {ECO:0000244|PDB:3DJ6}.
STRAND 187 192 {ECO:0000244|PDB:3DJ6}.
STRAND 194 201 {ECO:0000244|PDB:3DJ6}.
HELIX 209 216 {ECO:0000244|PDB:3DJ6}.
HELIX 221 240 {ECO:0000244|PDB:3DJ6}.
HELIX 250 252 {ECO:0000244|PDB:3DJ6}.
STRAND 253 255 {ECO:0000244|PDB:3DJ6}.
STRAND 261 263 {ECO:0000244|PDB:3DJ6}.
STRAND 270 272 {ECO:0000244|PDB:3D15}.
HELIX 284 286 {ECO:0000244|PDB:3DJ6}.
HELIX 289 292 {ECO:0000244|PDB:3DJ6}.
HELIX 299 315 {ECO:0000244|PDB:3DJ6}.
HELIX 325 333 {ECO:0000244|PDB:3DJ6}.
HELIX 345 354 {ECO:0000244|PDB:3DJ6}.
HELIX 359 361 {ECO:0000244|PDB:3DJ6}.
HELIX 365 370 {ECO:0000244|PDB:3DJ6}.
HELIX 372 377 {ECO:0000244|PDB:3DJ6}.
SEQUENCE 395 AA; 44772 MW; 26B6B65105A1A812 CRC64;
MDRCKENCVS RPVKTTVPFG PKRVLVTEQI PSQNLGSASS GQAQRVLCPS NSQRVPSQAQ
KLGAGQKPAP KQLPAASVPR PVSRLNNPQK NEQPAASGND SEKEQASLQK TEDTKKRQWT
LEDFDIGRPL GKGKFGNVYL ARERQSKFIL ALKVLFKTQL EKANVEHQLR REVEIQSHLR
HPNILRLYGY FHDATRVYLI LEYAPLGTVY RELQKLSKFD EQRTATYITE LANALSYCHS
KRVIHRDIKP ENLLLGSNGE LKIADFGWSV HAPSSRRTTM CGTLDYLPPE MIEGRMHDEK
VDLWSLGVLC YEFLVGMPPF EAHTYQETYR RISRVEFTFP DFVTEGARDL ISRLLKHNAS
QRLTLAEVLE HPWIKANSSK PPTGHTSKEP TSKSS


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