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P97477

- AURKA_MOUSE

UniProt

P97477 - AURKA_MOUSE

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Protein

Aurora kinase A

Gene

Aurka

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

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.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei134 – 1341ATP; via amide nitrogenPROSITE-ProRule annotation
Binding sitei153 – 1531ATPPROSITE-ProRule annotation
Active sitei247 – 2471Proton acceptorPROSITE-ProRule annotation
Binding sitei265 – 2651ATPPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi201 – 2044ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. histone serine kinase activity Source: MGI
  3. protein kinase activity Source: UniProtKB
  4. ubiquitin protein ligase binding Source: MGI

GO - Biological processi

  1. anterior/posterior axis specification Source: MGI
  2. centrosome localization Source: MGI
  3. centrosome organization Source: MGI
  4. histone-serine phosphorylation Source: GOC
  5. meiotic nuclear division Source: MGI
  6. meiotic spindle organization Source: MGI
  7. microtubule cytoskeleton organization Source: MGI
  8. mitotic cell cycle Source: MGI
  9. mitotic centrosome separation Source: MGI
  10. mitotic nuclear division Source: MGI
  11. mitotic spindle organization Source: MGI
  12. negative regulation of apoptotic process Source: MGI
  13. negative regulation of protein binding Source: Ensembl
  14. negative regulation of spindle checkpoint Source: MGI
  15. neuron projection extension Source: MGI
  16. positive regulation of oocyte maturation Source: MGI
  17. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: MGI
  18. protein localization to centrosome Source: MGI
  19. protein phosphorylation Source: MGI
  20. regulation of protein stability Source: Ensembl
  21. spindle assembly involved in female meiosis I Source: MGI
  22. spindle stabilization Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Cilium biogenesis/degradation, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_196635. Regulation of PLK1 Activity at G2/M Transition.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.

Names & Taxonomyi

Protein namesi
Recommended name:
Aurora kinase A (EC:2.7.11.1)
Alternative name(s):
Aurora 2
Aurora family kinase 1
Aurora/IPL1-related kinase 1
Short name:
ARK-1
Short name:
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
Gene namesi
Name:Aurka
Synonyms:Aik, Airk, Ark1, Aura, Ayk1, Btak, Iak1, Stk15, Stk6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:894678. Aurka.

Subcellular locationi

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle pole
Note: Localizes on centrosomes in interphase cells and at each spindle pole in mitosis. Associates with both the pericentriolar material (PCM) and centrioles. Colocalized with SIRT2 at centrosome (By similarity). Detected at the neurite hillock in developing neurons.By similarity

GO - Cellular componenti

  1. axon hillock Source: MGI
  2. centrosome Source: MGI
  3. germinal vesicle Source: MGI
  4. meiotic spindle Source: MGI
  5. microtubule organizing center Source: MGI
  6. mitotic spindle Source: MGI
  7. perinuclear region of cytoplasm Source: Ensembl
  8. pronucleus Source: MGI
  9. spindle microtubule Source: Ensembl
  10. spindle pole centrosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Disruption phenotypei

Death at the blastocyst stage due to mitotic defects and failure of cell proliferation.1 Publication

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 395395Aurora kinase APRO_0000086693Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei40 – 401PhosphoserineBy similarity
Modified residuei50 – 501PhosphoserineBy similarity
Modified residuei278 – 2781PhosphothreonineBy similarity
Modified residuei279 – 2791PhosphothreonineBy similarity
Modified residuei333 – 3331Phosphoserine; by PKA and PAKBy similarity

Post-translational modificationi

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).By similarity
Ubiquitinated by the anaphase-promoting complex (APC), leading to its degradation by the proteasome (By similarity). Ubiquitinated by CHFR, leading to its degradation by the proteasome. Ubiquitinated by the E3 ubiquitin-protein ligase complex SCF(FBXL7) during mitosis, leading to its degradation by the proteasome.By similarity2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP97477.
PaxDbiP97477.
PRIDEiP97477.

PTM databases

PhosphoSiteiP97477.

Expressioni

Tissue specificityi

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.2 Publications

Developmental stagei

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.

Inductioni

expression is cell cycle regulated and peaks at phase G2/M.1 Publication

Gene expression databases

BgeeiP97477.
CleanExiMM_AURKA.
ExpressionAtlasiP97477. baseline and differential.
GenevestigatoriP97477.

Interactioni

Subunit structurei

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.By similarity5 Publications

Protein-protein interaction databases

BioGridi203548. 6 interactions.
IntActiP97477. 1 interaction.

Structurei

Secondary structure

1
395
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi121 – 1233
Beta strandi124 – 1296
Helixi131 – 1333
Beta strandi136 – 1438
Turni144 – 1463
Beta strandi149 – 1568
Helixi157 – 1637
Helixi166 – 17611
Beta strandi187 – 1926
Beta strandi194 – 2018
Helixi209 – 2168
Helixi221 – 24020
Helixi250 – 2523
Beta strandi253 – 2553
Beta strandi261 – 2633
Beta strandi270 – 2723
Helixi284 – 2863
Helixi289 – 2924
Helixi299 – 31517
Helixi325 – 3339
Helixi345 – 35410
Helixi359 – 3613
Helixi365 – 3706
Helixi372 – 3776

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3D14X-ray1.90A116-381[»]
3D15X-ray2.30A116-381[»]
3D2IX-ray2.90A116-381[»]
3D2KX-ray2.50A116-381[»]
3DAJX-ray2.00A116-381[»]
3DJ5X-ray1.80A116-381[»]
3DJ6X-ray1.70A116-381[»]
3DJ7X-ray2.80A116-381[»]
ProteinModelPortaliP97477.
SMRiP97477. Positions 5-379.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP97477.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini124 – 374251Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni271 – 28414Activation segmentBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00550000074590.
HOVERGENiHBG108519.
InParanoidiP97477.
KOiK11481.
OMAiMERSKEN.
OrthoDBiEOG74FF1F.
PhylomeDBiP97477.
TreeFamiTF105331.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P97477-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDRCKENCVS RPVKTTVPFG PKRVLVTEQI PSQNLGSASS GQAQRVLCPS
60 70 80 90 100
NSQRVPSQAQ KLGAGQKPAP KQLPAASVPR PVSRLNNPQK NEQPAASGND
110 120 130 140 150
SEKEQASLQK TEDTKKRQWT LEDFDIGRPL GKGKFGNVYL ARERQSKFIL
160 170 180 190 200
ALKVLFKTQL EKANVEHQLR REVEIQSHLR HPNILRLYGY FHDATRVYLI
210 220 230 240 250
LEYAPLGTVY RELQKLSKFD EQRTATYITE LANALSYCHS KRVIHRDIKP
260 270 280 290 300
ENLLLGSNGE LKIADFGWSV HAPSSRRTTM CGTLDYLPPE MIEGRMHDEK
310 320 330 340 350
VDLWSLGVLC YEFLVGMPPF EAHTYQETYR RISRVEFTFP DFVTEGARDL
360 370 380 390
ISRLLKHNAS QRLTLAEVLE HPWIKANSSK PPTGHTSKEP TSKSS
Length:395
Mass (Da):44,772
Last modified:May 1, 1997 - v1
Checksum:i26B6B65105A1A812
GO
Isoform 2 (identifier: P97477-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAVEGEPGCCKRIGKAVWRRGDM

Note: May be less abundant or less stable.

Show »
Length:417
Mass (Da):47,173
Checksum:iC9FD861C803EF5C5
GO

Sequence cautioni

The sequence BAC39557.1 differs from that shown. Reason: Frameshift at position 382.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti234 – 2341A → T in AAB63205. (PubMed:9245792)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MAVEGEPGCCKRIGKAVWRR GDM in isoform 2. 2 PublicationsVSP_004871

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U80932 mRNA. Translation: AAB62982.1.
AF007817 mRNA. Translation: AAB63205.1.
U69106 mRNA. Translation: AAC12682.1.
AK085861 mRNA. Translation: BAC39557.1. Frameshift.
BC005425 mRNA. Translation: AAH05425.1.
BC014711 mRNA. Translation: AAH14711.1.
CCDSiCCDS17129.1. [P97477-2]
CCDS71204.1. [P97477-1]
PIRiJC5975.
RefSeqiNP_001278114.1. NM_001291185.1. [P97477-1]
NP_035627.1. NM_011497.4. [P97477-2]
XP_006499138.1. XM_006499075.1. [P97477-1]
UniGeneiMm.249363.

Genome annotation databases

EnsembliENSMUST00000028997; ENSMUSP00000028997; ENSMUSG00000027496. [P97477-2]
ENSMUST00000109139; ENSMUSP00000104767; ENSMUSG00000027496. [P97477-1]
ENSMUST00000109140; ENSMUSP00000104768; ENSMUSG00000027496. [P97477-1]
GeneIDi20878.
KEGGimmu:20878.
UCSCiuc008ocn.1. mouse. [P97477-2]
uc008oco.1. mouse. [P97477-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U80932 mRNA. Translation: AAB62982.1 .
AF007817 mRNA. Translation: AAB63205.1 .
U69106 mRNA. Translation: AAC12682.1 .
AK085861 mRNA. Translation: BAC39557.1 . Frameshift.
BC005425 mRNA. Translation: AAH05425.1 .
BC014711 mRNA. Translation: AAH14711.1 .
CCDSi CCDS17129.1. [P97477-2 ]
CCDS71204.1. [P97477-1 ]
PIRi JC5975.
RefSeqi NP_001278114.1. NM_001291185.1. [P97477-1 ]
NP_035627.1. NM_011497.4. [P97477-2 ]
XP_006499138.1. XM_006499075.1. [P97477-1 ]
UniGenei Mm.249363.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3D14 X-ray 1.90 A 116-381 [» ]
3D15 X-ray 2.30 A 116-381 [» ]
3D2I X-ray 2.90 A 116-381 [» ]
3D2K X-ray 2.50 A 116-381 [» ]
3DAJ X-ray 2.00 A 116-381 [» ]
3DJ5 X-ray 1.80 A 116-381 [» ]
3DJ6 X-ray 1.70 A 116-381 [» ]
3DJ7 X-ray 2.80 A 116-381 [» ]
ProteinModelPortali P97477.
SMRi P97477. Positions 5-379.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 203548. 6 interactions.
IntActi P97477. 1 interaction.

Chemistry

BindingDBi P97477.
ChEMBLi CHEMBL2211.

PTM databases

PhosphoSitei P97477.

Proteomic databases

MaxQBi P97477.
PaxDbi P97477.
PRIDEi P97477.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000028997 ; ENSMUSP00000028997 ; ENSMUSG00000027496 . [P97477-2 ]
ENSMUST00000109139 ; ENSMUSP00000104767 ; ENSMUSG00000027496 . [P97477-1 ]
ENSMUST00000109140 ; ENSMUSP00000104768 ; ENSMUSG00000027496 . [P97477-1 ]
GeneIDi 20878.
KEGGi mmu:20878.
UCSCi uc008ocn.1. mouse. [P97477-2 ]
uc008oco.1. mouse. [P97477-1 ]

Organism-specific databases

CTDi 6790.
MGIi MGI:894678. Aurka.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00550000074590.
HOVERGENi HBG108519.
InParanoidi P97477.
KOi K11481.
OMAi MERSKEN.
OrthoDBi EOG74FF1F.
PhylomeDBi P97477.
TreeFami TF105331.

Enzyme and pathway databases

Reactomei REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.

Miscellaneous databases

EvolutionaryTracei P97477.
NextBioi 299731.
PROi P97477.
SOURCEi Search...

Gene expression databases

Bgeei P97477.
CleanExi MM_AURKA.
ExpressionAtlasi P97477. baseline and differential.
Genevestigatori P97477.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A novel mammalian, mitotic spindle-associated kinase is related to yeast and fly chromosome segregation regulators."
    Gopalan G., Chan C.S.M., Donovan P.J.
    J. Cell Biol. 138:643-656(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INDUCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION.
    Strain: BALB/c.
    Tissue: Testis.
  2. "ayk1, a novel mammalian gene related to Drosophila aurora centrosome separation kinase, is specifically expressed during meiosis."
    Yanai A., Arama E., Kilfin G., Motro B.
    Oncogene 14:2943-2950(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Testis.
  3. "cDNA cloning, expression, subcellular localization, and chromosomal assignment of mammalian aurora homologues, aurora-related kinase (ARK) 1 and 2."
    Shindo M., Nakano H., Kuroyanagi H., Shirasawa T., Mihara M., Gilbert D.J., Jenkins N.A., Copeland N.G., Yagita H., Okumura K.
    Biochem. Biophys. Res. Commun. 244:285-292(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: BALB/c.
  4. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Heart.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Mammary gland.
  6. Cited for: UBIQUITINATION BY CHFR.
  7. Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  8. "An essential role of the aPKC-Aurora A-NDEL1 pathway in neurite elongation by modulation of microtubule dynamics."
    Mori D., Yamada M., Mimori-Kiyosue Y., Shirai Y., Suzuki A., Ohno S., Saya H., Wynshaw-Boris A., Hirotsune S.
    Nat. Cell Biol. 11:1057-1068(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  9. Cited for: FUNCTION, INTERACTION WITH PIFO, ACTIVATION BY PIFO.
  10. "Novel E3 ligase component FBXL7 ubiquitinates and degrades Aurora A, causing mitotic arrest."
    Coon T.A., Glasser J.R., Mallampalli R.K., Chen B.B.
    Cell Cycle 11:721-729(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, INTERACTION WITH FBXL7.
  11. "Furry protein promotes Aurora A-mediated polo-like kinase 1 activation."
    Ikeda M., Chiba S., Ohashi K., Mizuno K.
    J. Biol. Chem. 287:27670-27681(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FRY.
  12. "Discovery of an Aurora kinase inhibitor through site-specific dynamic combinatorial chemistry."
    Cancilla M.T., He M.M., Viswanathan N., Simmons R.L., Taylor M., Fung A.D., Cao K., Erlanson D.A.
    Bioorg. Med. Chem. Lett. 18:3978-3981(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 116-381 IN COMPLEX WITH SYNTHETIC INHIBITOR.
  13. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 116-381 IN COMPLEX WITH SYNTHETIC INHIBITOR.

Entry informationi

Entry nameiAURKA_MOUSE
AccessioniPrimary (citable) accession number: P97477
Secondary accession number(s): O35624, Q8C3H8, Q91YU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 27, 2003
Last sequence update: May 1, 1997
Last modified: October 29, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3