AURKA_MOUSE
ID AURKA_MOUSE Reviewed; 395 AA.
AC P97477; O35624; Q8C3H8; Q91YU4;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Aurora kinase A;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P04198};
DE AltName: Full=Aurora 2;
DE AltName: Full=Aurora family kinase 1;
DE AltName: Full=Aurora/IPL1-related kinase 1;
DE Short=ARK-1;
DE Short=Aurora-related kinase 1;
DE AltName: Full=Ipl1- and aurora-related kinase 1;
DE AltName: Full=Serine/threonine-protein kinase 6;
DE AltName: Full=Serine/threonine-protein kinase Ayk1;
DE AltName: Full=Serine/threonine-protein kinase aurora-A;
GN Name=Aurka; Synonyms=Aik, Airk, Ark1, Aura, Ayk1, Btak, Iak1, Stk15, Stk6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INDUCTION, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND FUNCTION.
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=9245792; DOI=10.1083/jcb.138.3.643;
RA Gopalan G., Chan C.S.M., Donovan P.J.;
RT "A novel mammalian, mitotic spindle-associated kinase is related to yeast
RT and fly chromosome segregation regulators.";
RL J. Cell Biol. 138:643-656(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=9205101; DOI=10.1038/sj.onc.1201144;
RA Yanai A., Arama E., Kilfin G., Motro B.;
RT "ayk1, a novel mammalian gene related to Drosophila aurora centrosome
RT separation kinase, is specifically expressed during meiosis.";
RL Oncogene 14:2943-2950(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ;
RX PubMed=9514916; DOI=10.1006/bbrc.1998.8250;
RA Shindo M., Nakano H., Kuroyanagi H., Shirasawa T., Mihara M., Gilbert D.J.,
RA Jenkins N.A., Copeland N.G., Yagita H., Okumura K.;
RT "cDNA cloning, expression, subcellular localization, and chromosomal
RT assignment of mammalian aurora homologues, aurora-related kinase (ARK) 1
RT and 2.";
RL Biochem. Biophys. Res. Commun. 244:285-292(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP UBIQUITINATION BY CHFR.
RX PubMed=15793587; DOI=10.1038/ng1538;
RA Yu X., Minter-Dykhouse K., Malureanu L., Zhao W.-M., Zhang D., Merkle C.J.,
RA Ward I.M., Saya H., Fang G., van Deursen J., Chen J.;
RT "Chfr is required for tumor suppression and Aurora A regulation.";
RL Nat. Genet. 37:401-406(2005).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19075002; DOI=10.1128/mcb.01062-08;
RA Cowley D.O., Rivera-Perez J.A., Schliekelman M., He Y.J., Oliver T.G.,
RA Lu L., O'Quinn R., Salmon E.D., Magnuson T., Van Dyke T.;
RT "Aurora-A kinase is essential for bipolar spindle formation and early
RT development.";
RL Mol. Cell. Biol. 29:1059-1071(2009).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19668197; DOI=10.1038/ncb1919;
RA Mori D., Yamada M., Mimori-Kiyosue Y., Shirai Y., Suzuki A., Ohno S.,
RA Saya H., Wynshaw-Boris A., Hirotsune S.;
RT "An essential role of the aPKC-Aurora A-NDEL1 pathway in neurite elongation
RT by modulation of microtubule dynamics.";
RL Nat. Cell Biol. 11:1057-1068(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP FUNCTION, INTERACTION WITH PIFO, AND ACTIVATION BY PIFO.
RX PubMed=20643351; DOI=10.1016/j.devcel.2010.06.005;
RA Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B.,
RA Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H.;
RT "Pitchfork regulates primary cilia disassembly and left-right asymmetry.";
RL Dev. Cell 19:66-77(2010).
RN [11]
RP UBIQUITINATION, AND INTERACTION WITH FBXL7.
RX PubMed=22306998; DOI=10.4161/cc.11.4.19171;
RA Coon T.A., Glasser J.R., Mallampalli R.K., Chen B.B.;
RT "Novel E3 ligase component FBXL7 ubiquitinates and degrades Aurora A,
RT causing mitotic arrest.";
RL Cell Cycle 11:721-729(2012).
RN [12]
RP INTERACTION WITH FRY.
RX PubMed=22753416; DOI=10.1074/jbc.m112.378968;
RA Ikeda M., Chiba S., Ohashi K., Mizuno K.;
RT "Furry protein promotes Aurora A-mediated polo-like kinase 1 activation.";
RL J. Biol. Chem. 287:27670-27681(2012).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 116-381 IN COMPLEX WITH SYNTHETIC
RP INHIBITOR.
RX PubMed=18579375; DOI=10.1016/j.bmcl.2008.06.011;
RA Cancilla M.T., He M.M., Viswanathan N., Simmons R.L., Taylor M., Fung A.D.,
RA Cao K., Erlanson D.A.;
RT "Discovery of an Aurora kinase inhibitor through site-specific dynamic
RT combinatorial chemistry.";
RL Bioorg. Med. Chem. Lett. 18:3978-3981(2008).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 116-381 IN COMPLEX WITH SYNTHETIC
RP INHIBITOR.
RX PubMed=18678489; DOI=10.1016/j.bmcl.2008.07.073;
RA Oslob J.D., Romanowski M.J., Allen D.A., Baskaran S., Bui M., Elling R.A.,
RA Flanagan W.M., Fung A.D., Hanan E.J., Harris S., Heumann S.A., Hoch U.,
RA Jacobs J.W., Lam J., Lawrence C.E., McDowell R.S., Nannini M.A., Shen W.,
RA Silverman J.A., Sopko M.M., Tangonan B.T., Teague J., Yoburn J.C., Yu C.H.,
RA Zhong M., Zimmerman K.M., O'Brien T., Lew W.;
RT "Discovery of a potent and selective aurora kinase inhibitor.";
RL Bioorg. Med. Chem. Lett. 18:4880-4884(2008).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=23807208; DOI=10.1007/s00018-013-1401-6;
RA Kypri E., Christodoulou A., Maimaris G., Lethan M., Markaki M.,
RA Lysandrou C., Lederer C.W., Tavernarakis N., Geimer S., Pedersen L.B.,
RA Santama N.;
RT "The nucleotide-binding proteins Nubp1 and Nubp2 are negative regulators of
RT ciliogenesis.";
RL Cell. Mol. Life Sci. 71:517-538(2014).
RN [16]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=27753540; DOI=10.1080/15384101.2016.1243630;
RA Lee S.Y., Kim E.Y., Kim K.H., Lee K.A.;
RT "Bcl2l10, a new Tpx2 binding partner, is a master regulator of Aurora
RT kinase A in mouse oocytes.";
RL Cell Cycle 15:3296-3305(2016).
CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the
CC regulation of cell cycle progression. Associates with the centrosome
CC and the spindle microtubules during mitosis and plays a critical role
CC in various mitotic events including the establishment of mitotic
CC spindle, centrosome duplication, centrosome separation as well as
CC maturation, chromosomal alignment, spindle assembly checkpoint, and
CC cytokinesis. Required for normal spindle positioning during mitosis and
CC for the localization of NUMA1 and DCTN1 to the cell cortex during
CC metaphase (By similarity). Required for initial activation of CDK1 at
CC centrosomes. Phosphorylates numerous target proteins, including
CC ARHGEF2, BORA, BRCA1, CDC25B, DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3,
CC PPP1R2, PLK1, RASSF1, TACC3, p53/TP53 and TPX2. Regulates KIF2A tubulin
CC depolymerase activity. Required for normal axon formation. Plays a role
CC in microtubule remodeling during neurite extension. Important for
CC microtubule formation and/or stabilization. Also acts as a key
CC regulatory component of the p53/TP53 pathway, and particularly the
CC checkpoint-response pathways critical for oncogenic transformation of
CC cells, by phosphorylating and destabilizing p53/TP53. Phosphorylates
CC its own inhibitors, the protein phosphatase type 1 (PP1) isoforms, to
CC inhibit their activity. Necessary for proper cilia disassembly prior to
CC mitosis. Regulates protein levels of the anti-apoptosis protein BIRC5
CC by suppressing the expression of the SCF(FBXL7) E3 ubiquitin-protein
CC ligase substrate adapter FBXL7 through the phosphorylation of the
CC transcription factor FOXP1 (By similarity).
CC {ECO:0000250|UniProtKB:O14965, ECO:0000269|PubMed:19075002,
CC ECO:0000269|PubMed:19668197, ECO:0000269|PubMed:20643351,
CC ECO:0000269|PubMed:9245792}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:O14965};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:O14965};
CC -!- ACTIVITY REGULATION: Activation of CDK1, appears to be an upstream
CC event of AURKA activation (By similarity). Phosphatase inhibitor-2
CC (PPP1R2) and TPX2 act also as activators (By similarity). Inactivated
CC by the G2 checkpoint (By similarity). Inhibited by GADD45A and
CC p53/TP53, and through dephosphorylation by protein phosphatase type 1
CC (PP1) (By similarity). MLN8054 is also a potent and selective inhibitor
CC (By similarity). Activated during the early phase of cilia disassembly
CC in the presence of PIFO (By similarity). Inhibited by the small
CC molecule inhibitor VX-680 (By similarity).
CC {ECO:0000250|UniProtKB:O14965}.
CC -!- SUBUNIT: Interacts with CPEB1, JTB, TACC1, TPX2, PPP2CA, as well as
CC with the protein phosphatase type 1 (PP1) isoforms PPP1CA, PPP1CB and
CC PPP1CC (By similarity). Interacts also with its substrates ARHGEF2,
CC BORA, KIF2A, PARD3, and p53/TP53 (By similarity). Interaction with BORA
CC promotes phosphorylation of PLK1 (By similarity). Interacts with
CC GADD45A, competing with its oligomerization (By similarity). Interacts
CC with FBXL7 and PIFO (PubMed:20643351, PubMed:22306998). Interacts (via
CC C-terminus) with AUNIP (via C-terminus) (By similarity). Identified in
CC a complex with AUNIP and NIN (By similarity). Interacts with SIRT2 (By
CC similarity). Interacts with FRY; this interaction facilitates AURKA-
CC mediated PLK1 phosphorylation (PubMed:22753416). Interacts with MYCN;
CC interaction is phospho-independent and triggers AURKA activation; AURKA
CC competes with FBXW7 for binding to unphosphorylated MYCN but not for
CC binding to phosphorylated MYCN (By similarity). Interacts with HNRNPU
CC (By similarity). Interacts with AAAS (By similarity). Interacts with
CC KLHL18 and CUL3 (By similarity). Interacts with FOXP1 (By similarity).
CC {ECO:0000250|UniProtKB:O14965, ECO:0000269|PubMed:18579375,
CC ECO:0000269|PubMed:18678489, ECO:0000269|PubMed:20643351,
CC ECO:0000269|PubMed:22306998, ECO:0000269|PubMed:22753416}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:19668197,
CC ECO:0000269|PubMed:20643351, ECO:0000269|PubMed:27753540}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000269|PubMed:19075002,
CC ECO:0000269|PubMed:27753540, ECO:0000269|PubMed:9245792}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000269|PubMed:23807208}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC centriole {ECO:0000269|PubMed:23807208}. Cell projection, neuron
CC projection {ECO:0000269|PubMed:19668197}. Note=Localizes on centrosomes
CC in interphase cells and at each spindle pole in mitosis
CC (PubMed:9245792). Associates with both the pericentriolar material
CC (PCM) and centrioles (By similarity). Colocalized with SIRT2 at
CC centrosome (By similarity). Detected at the neurite hillock in
CC developing neurons (PubMed:19668197). The localization to the spindle
CC poles is regulated by AAAS (By similarity).
CC {ECO:0000250|UniProtKB:O14965, ECO:0000269|PubMed:19668197,
CC ECO:0000269|PubMed:9245792}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P97477-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P97477-2; Sequence=VSP_004871;
CC -!- TISSUE SPECIFICITY: Detected in embryonic neurons in dorsal root
CC ganglia and brain cortex (at protein level). Highly expressed in
CC testis, in about one third of the seminiferous tubules. Expression is
CC restricted to specific spermatocytes nearing completion of prophase,
CC with levels falling off on transition to elongated spermatids. Highly
CC expressed in the ovary, expression in the oocyte starts around the
CC transition to large growing follicle. Abundant expression is seen in
CC the proliferating granulosa and thecal cells of the growing follicle,
CC and in the young corpus luteum. Very weakly expressed in spleen and
CC intestine. {ECO:0000269|PubMed:19668197, ECO:0000269|PubMed:9245792}.
CC -!- DEVELOPMENTAL STAGE: Expressed during all phases of oocyte maturation;
CC localized at the meiotic spindle and spindle poles during meiosis
CC (PubMed:27753540). At 7.5-9.5 dpc expressed evenly all over the embryo.
CC At later stages, expression is mainly restricted to proliferating
CC zones. The highest levels of expression at mid-embryonic development
CC (13.5 dpc) were observed in the liver, lung, kidney and back
CC (trapezius) muscle and all regions in active proliferation.
CC {ECO:0000269|PubMed:27753540}.
CC -!- INDUCTION: expression is cell cycle regulated and peaks at phase G2/M.
CC {ECO:0000269|PubMed:9245792}.
CC -!- PTM: Activated by phosphorylation at Thr-279; this brings about a
CC change in the conformation of the activation segment (By similarity).
CC Phosphorylation at Thr-279 varies during the cell cycle and is highest
CC during M phase (By similarity). Autophosphorylated at Thr-279 upon TPX2
CC binding (By similarity). Thr-279 can be phosphorylated by several
CC kinases, including PAK and PKA (By similarity). Protein phosphatase
CC type 1 (PP1) binds AURKA and inhibits its activity by dephosphorylating
CC Thr-279 during mitosis (By similarity). Phosphorylation at Ser-333
CC decreases the kinase activity (By similarity). PPP2CA controls
CC degradation by dephosphorylating Ser-52 at the end of mitosis (By
CC similarity). {ECO:0000250|UniProtKB:O14965}.
CC -!- PTM: Ubiquitinated by the anaphase-promoting complex (APC), leading to
CC its degradation by the proteasome (By similarity). Ubiquitinated by
CC CHFR, leading to its degradation by the proteasome (PubMed:15793587).
CC Ubiquitinated by the E3 ubiquitin-protein ligase complex SCF(FBXL7)
CC during mitosis, leading to its degradation by the proteasome
CC (PubMed:22306998). {ECO:0000250|UniProtKB:O14965,
CC ECO:0000269|PubMed:15793587, ECO:0000269|PubMed:22306998}.
CC -!- DISRUPTION PHENOTYPE: Death at the blastocyst stage due to mitotic
CC defects and failure of cell proliferation.
CC {ECO:0000269|PubMed:19075002}.
CC -!- MISCELLANEOUS: Centrosome amplification can occur when the cycles are
CC uncoupled, and this amplification is associated with cancer and with an
CC increase in the levels of chromosomal instability.
CC -!- MISCELLANEOUS: [Isoform 2]: May be less abundant or less stable.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. Aurora subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC39557.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U80932; AAB62982.1; -; mRNA.
DR EMBL; AF007817; AAB63205.1; -; mRNA.
DR EMBL; U69106; AAC12682.1; -; mRNA.
DR EMBL; AK085861; BAC39557.1; ALT_FRAME; mRNA.
DR EMBL; BC005425; AAH05425.1; -; mRNA.
DR EMBL; BC014711; AAH14711.1; -; mRNA.
DR CCDS; CCDS17129.1; -. [P97477-2]
DR CCDS; CCDS71204.1; -. [P97477-1]
DR PIR; JC5975; JC5975.
DR RefSeq; NP_001278114.1; NM_001291185.1. [P97477-1]
DR RefSeq; NP_035627.1; NM_011497.4. [P97477-2]
DR RefSeq; XP_006499138.1; XM_006499075.2. [P97477-1]
DR PDB; 3D14; X-ray; 1.90 A; A=116-381.
DR PDB; 3D15; X-ray; 2.30 A; A=116-381.
DR PDB; 3D2I; X-ray; 2.90 A; A=116-381.
DR PDB; 3D2K; X-ray; 2.50 A; A=116-381.
DR PDB; 3DAJ; X-ray; 2.00 A; A=116-381.
DR PDB; 3DJ5; X-ray; 1.80 A; A=116-381.
DR PDB; 3DJ6; X-ray; 1.70 A; A=116-381.
DR PDB; 3DJ7; X-ray; 2.80 A; A=116-381.
DR PDBsum; 3D14; -.
DR PDBsum; 3D15; -.
DR PDBsum; 3D2I; -.
DR PDBsum; 3D2K; -.
DR PDBsum; 3DAJ; -.
DR PDBsum; 3DJ5; -.
DR PDBsum; 3DJ6; -.
DR PDBsum; 3DJ7; -.
DR AlphaFoldDB; P97477; -.
DR SMR; P97477; -.
DR BioGRID; 203548; 12.
DR IntAct; P97477; 1.
DR STRING; 10090.ENSMUSP00000028997; -.
DR BindingDB; P97477; -.
DR ChEMBL; CHEMBL2211; -.
DR iPTMnet; P97477; -.
DR PhosphoSitePlus; P97477; -.
DR EPD; P97477; -.
DR MaxQB; P97477; -.
DR PaxDb; P97477; -.
DR PeptideAtlas; P97477; -.
DR PRIDE; P97477; -.
DR ProteomicsDB; 277137; -. [P97477-1]
DR ProteomicsDB; 277138; -. [P97477-2]
DR Antibodypedia; 1129; 1081 antibodies from 47 providers.
DR DNASU; 20878; -.
DR Ensembl; ENSMUST00000028997; ENSMUSP00000028997; ENSMUSG00000027496. [P97477-2]
DR Ensembl; ENSMUST00000109139; ENSMUSP00000104767; ENSMUSG00000027496. [P97477-1]
DR Ensembl; ENSMUST00000109140; ENSMUSP00000104768; ENSMUSG00000027496. [P97477-1]
DR GeneID; 20878; -.
DR KEGG; mmu:20878; -.
DR UCSC; uc008ocn.2; mouse. [P97477-2]
DR UCSC; uc008oco.2; mouse. [P97477-1]
DR CTD; 6790; -.
DR MGI; MGI:894678; Aurka.
DR VEuPathDB; HostDB:ENSMUSG00000027496; -.
DR eggNOG; KOG0580; Eukaryota.
DR GeneTree; ENSGT00940000154900; -.
DR HOGENOM; CLU_000288_63_6_1; -.
DR InParanoid; P97477; -.
DR OMA; PHTKNVD; -.
DR PhylomeDB; P97477; -.
DR TreeFam; TF105331; -.
DR Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR Reactome; R-MMU-8854521; Interaction between PHLDA1 and AURKA.
DR BioGRID-ORCS; 20878; 24 hits in 78 CRISPR screens.
DR ChiTaRS; Aurka; mouse.
DR EvolutionaryTrace; P97477; -.
DR PRO; PR:P97477; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P97477; protein.
DR Bgee; ENSMUSG00000027496; Expressed in secondary oocyte and 189 other tissues.
DR ExpressionAtlas; P97477; baseline and differential.
DR Genevisible; P97477; MM.
DR GO; GO:0043203; C:axon hillock; IDA:MGI.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0032133; C:chromosome passenger complex; IBA:GO_Central.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0042585; C:germinal vesicle; IDA:MGI.
DR GO; GO:0072687; C:meiotic spindle; IDA:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0005815; C:microtubule organizing center; IDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IDA:MGI.
DR GO; GO:0097431; C:mitotic spindle pole; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0045120; C:pronucleus; IDA:MGI.
DR GO; GO:0005819; C:spindle; ISO:MGI.
DR GO; GO:0005876; C:spindle microtubule; ISO:MGI.
DR GO; GO:0051233; C:spindle midzone; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0031616; C:spindle pole centrosome; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035174; F:histone serine kinase activity; IMP:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; IDA:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:MGI.
DR GO; GO:0009948; P:anterior/posterior axis specification; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007098; P:centrosome cycle; IGI:MGI.
DR GO; GO:0051642; P:centrosome localization; IMP:MGI.
DR GO; GO:0061523; P:cilium disassembly; ISS:UniProtKB.
DR GO; GO:0097421; P:liver regeneration; ISO:MGI.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:MGI.
DR GO; GO:0000212; P:meiotic spindle organization; IMP:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IGI:MGI.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:MGI.
DR GO; GO:0007100; P:mitotic centrosome separation; IMP:MGI.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:1990138; P:neuron projection extension; IGI:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; ISO:MGI.
DR GO; GO:1900195; P:positive regulation of oocyte maturation; IMP:MGI.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:MGI.
DR GO; GO:0071539; P:protein localization to centrosome; IMP:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IGI:MGI.
DR GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
DR GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
DR GO; GO:0009611; P:response to wounding; ISO:MGI.
DR GO; GO:0007057; P:spindle assembly involved in female meiosis I; IMP:MGI.
DR GO; GO:0007051; P:spindle organization; ISO:MGI.
DR InterPro; IPR030616; Aur.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24350; PTHR24350; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cell cycle; Cell division;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; Isopeptide bond; Kinase; Microtubule; Mitosis;
KW Nucleotide-binding; Phosphoprotein; Proto-oncogene; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT CHAIN 1..395
FT /note="Aurora kinase A"
FT /id="PRO_0000086693"
FT DOMAIN 124..374
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..284
FT /note="Activation segment"
FT /evidence="ECO:0000250|UniProtKB:O14965"
FT REGION 376..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 247
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 201..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 251..252
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O14965"
FT BINDING 265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14965"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14965"
FT MOD_RES 278
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O14965"
FT MOD_RES 279
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O14965"
FT MOD_RES 333
FT /note="Phosphoserine; by PKA and PAK"
FT /evidence="ECO:0000250|UniProtKB:O14965"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O14965"
FT VAR_SEQ 1
FT /note="M -> MAVEGEPGCCKRIGKAVWRRGDM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9245792"
FT /id="VSP_004871"
FT CONFLICT 234
FT /note="A -> T (in Ref. 1; AAB63205)"
FT /evidence="ECO:0000305"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:3DJ6"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:3DJ6"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:3DJ6"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:3DJ6"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:3DJ6"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:3DJ6"
FT HELIX 157..163
FT /evidence="ECO:0007829|PDB:3DJ6"
FT HELIX 166..176
FT /evidence="ECO:0007829|PDB:3DJ6"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:3DJ6"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:3DJ6"
FT HELIX 209..216
FT /evidence="ECO:0007829|PDB:3DJ6"
FT HELIX 221..240
FT /evidence="ECO:0007829|PDB:3DJ6"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:3DJ6"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:3DJ6"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:3DJ6"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:3D15"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:3DJ6"
FT HELIX 289..292
FT /evidence="ECO:0007829|PDB:3DJ6"
FT HELIX 299..315
FT /evidence="ECO:0007829|PDB:3DJ6"
FT HELIX 325..333
FT /evidence="ECO:0007829|PDB:3DJ6"
FT HELIX 345..354
FT /evidence="ECO:0007829|PDB:3DJ6"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:3DJ6"
FT HELIX 365..370
FT /evidence="ECO:0007829|PDB:3DJ6"
FT HELIX 372..377
FT /evidence="ECO:0007829|PDB:3DJ6"
SQ 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
