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P97477 (AURKA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aurora kinase A

EC=2.7.11.1
Alternative name(s):
Aurora 2
Aurora 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 names
Name:Aurka
Synonyms:Aik, Airk, Ark1, Aura, Ayk1, Btak, Iak1, Stk15, Stk6
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length395 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mitotic serine/threonine kinases that contributes to the regulation of cell cycle progression. Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, centrosome separation as well as maturation, chromosomal alignment, spindle assembly checkpoint, and cytokinesis. Required for initial activation of CDK1 at centrosomes. Phosphorylates numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3, p53/TP53 and TPX2. Regulates KIF2A tubulin depolymerase activity. Required for normal axon formation. Plays a role in microtubule remodeling during neurite extension. Important for microtubule formation and/or stabilization. Also acts as a key regulatory component of the p53/TP53 pathway, and particularly the checkpoint-response pathways critical for oncogenic transformation of cells, by phosphorylating and stabilizing p53/TP53. Phosphorylates its own inhibitors, the protein phosphatase type 1 (PP1) isoforms, to inhibit their activity. Necessary for proper cilia disassembly prior to mitosis. Ref.1 Ref.7 Ref.8 Ref.9

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

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.

Subunit structure

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 FRY; this interaction facilitates AURKA-mediated PLK1 phosphorylation. Ref.9 Ref.10 Ref.11

Subcellular location

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 By similarity. Detected at the neurite hillock in developing neurons. Ref.1 Ref.7 Ref.8

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. Ref.1 Ref.8

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. Ref.1

Post-translational modification

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.

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. Ref.6 Ref.10

Disruption phenotype

Death at the blastocyst stage due to mitotic defects and failure of cell proliferation. Ref.7

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.

Sequence caution

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

Ontologies

Keywords
   Biological processCell cycle
Cell division
Cilium biogenesis/degradation
Mitosis
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
   Coding sequence diversityAlternative splicing
   DiseaseProto-oncogene
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanterior/posterior axis specification

Inferred from mutant phenotype PubMed 22939930. Source: MGI

centrosome localization

Inferred from mutant phenotype PubMed 22832491. Source: MGI

centrosome organization

Inferred from genetic interaction PubMed 17060449. Source: MGI

histone-serine phosphorylation

Inferred from mutant phenotype PubMed 21274965. Source: GOC

meiotic nuclear division

Inferred from mutant phenotype PubMed 21274965. Source: MGI

meiotic spindle organization

Inferred from mutant phenotype PubMed 14695913. Source: MGI

microtubule cytoskeleton organization

Inferred from genetic interaction Ref.8. Source: MGI

mitotic cell cycle

Inferred from mutant phenotype Ref.6. Source: MGI

mitotic centrosome separation

Inferred from mutant phenotype Ref.7. Source: MGI

mitotic nuclear division

Inferred from mutant phenotype PubMed 22832491. Source: MGI

mitotic spindle organization

Inferred from mutant phenotype PubMed 18345035PubMed 18801727. Source: MGI

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 22939930. Source: MGI

negative regulation of protein binding

Inferred from electronic annotation. Source: Ensembl

negative regulation of spindle checkpoint

Inferred from mutant phenotype Ref.7. Source: MGI

neuron projection extension

Inferred from genetic interaction Ref.8. Source: MGI

positive regulation of oocyte maturation

Inferred from mutant phenotype PubMed 14695913. Source: MGI

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype PubMed 17060449. Source: MGI

protein localization to centrosome

Inferred from mutant phenotype PubMed 17060449. Source: MGI

protein phosphorylation

Inferred from genetic interaction PubMed 17060449. Source: MGI

regulation of protein stability

Inferred from electronic annotation. Source: Ensembl

spindle assembly involved in female meiosis I

Inferred from mutant phenotype PubMed 21274965. Source: MGI

spindle stabilization

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentaxon hillock

Inferred from direct assay Ref.8. Source: MGI

centrosome

Inferred from direct assay Ref.1. Source: MGI

germinal vesicle

Inferred from direct assay PubMed 14695913. Source: MGI

meiotic spindle

Inferred from direct assay PubMed 14695913. Source: MGI

microtubule organizing center

Inferred from genetic interaction Ref.8. Source: MGI

mitotic spindle

Inferred from direct assay Ref.1. Source: MGI

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

pronucleus

Inferred from direct assay PubMed 14695913. Source: MGI

spindle microtubule

Inferred from electronic annotation. Source: Ensembl

spindle pole centrosome

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

histone serine kinase activity

Inferred from mutant phenotype PubMed 21274965. Source: MGI

protein binding

Inferred from physical interaction Ref.6. Source: UniProtKB

protein kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction Ref.6. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P97477-1)

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.
Isoform 2 (identifier: P97477-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAVEGEPGCCKRIGKAVWRRGDM
Note: May be less abundant or less stable.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 395395Aurora kinase A
PRO_0000086693

Regions

Domain124 – 374251Protein kinase
Nucleotide binding201 – 2044ATP By similarity
Region271 – 28414Activation segment By similarity

Sites

Active site2471Proton acceptor By similarity
Binding site1341ATP; via amide nitrogen By similarity
Binding site1531ATP By similarity
Binding site2651ATP By similarity

Amino acid modifications

Modified residue401Phosphoserine By similarity
Modified residue501Phosphoserine By similarity
Modified residue2781Phosphothreonine By similarity
Modified residue2791Phosphothreonine By similarity
Modified residue3331Phosphoserine; by PKA and PAK By similarity

Natural variations

Alternative sequence11M → MAVEGEPGCCKRIGKAVWRR GDM in isoform 2.
VSP_004871

Experimental info

Sequence conflict2341A → T in AAB63205. Ref.1

Secondary structure

............................................. 395
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 26B6B65105A1A812

FASTA39544,772
        10         20         30         40         50         60 
MDRCKENCVS RPVKTTVPFG PKRVLVTEQI PSQNLGSASS GQAQRVLCPS NSQRVPSQAQ 

        70         80         90        100        110        120 
KLGAGQKPAP KQLPAASVPR PVSRLNNPQK NEQPAASGND SEKEQASLQK TEDTKKRQWT 

       130        140        150        160        170        180 
LEDFDIGRPL GKGKFGNVYL ARERQSKFIL ALKVLFKTQL EKANVEHQLR REVEIQSHLR 

       190        200        210        220        230        240 
HPNILRLYGY FHDATRVYLI LEYAPLGTVY RELQKLSKFD EQRTATYITE LANALSYCHS 

       250        260        270        280        290        300 
KRVIHRDIKP ENLLLGSNGE LKIADFGWSV HAPSSRRTTM CGTLDYLPPE MIEGRMHDEK 

       310        320        330        340        350        360 
VDLWSLGVLC YEFLVGMPPF EAHTYQETYR RISRVEFTFP DFVTEGARDL ISRLLKHNAS 

       370        380        390 
QRLTLAEVLE HPWIKANSSK PPTGHTSKEP TSKSS 

« Hide

Isoform 2 [UniParc].

Checksum: C9FD861C803EF5C5
Show »

FASTA41747,173

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Chfr is required for tumor suppression and Aurora A regulation."
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.
Nat. Genet. 37:401-406(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION BY CHFR.
[7]"Aurora-A kinase is essential for bipolar spindle formation and early development."
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.
Mol. Cell. Biol. 29:1059-1071(2009) [PubMed] [Europe PMC] [Abstract]
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]"Pitchfork regulates primary cilia disassembly and left-right asymmetry."
Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B., Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H.
Dev. Cell 19:66-77(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PIFO, ACTIVATION BY PIFO.
[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]"Discovery of a potent and selective aurora kinase inhibitor."
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. expand/collapse author list , 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.
Bioorg. Med. Chem. Lett. 18:4880-4884(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 116-381 IN COMPLEX WITH SYNTHETIC INHIBITOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS17129.1. [P97477-2]
PIRJC5975.
RefSeqNP_001278114.1. NM_001291185.1. [P97477-1]
NP_035627.1. NM_011497.4. [P97477-2]
XP_006499138.1. XM_006499075.1. [P97477-1]
UniGeneMm.249363.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP97477.
SMRP97477. Positions 5-379.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203548. 6 interactions.
IntActP97477. 1 interaction.

Chemistry

BindingDBP97477.
ChEMBLCHEMBL2211.

PTM databases

PhosphoSiteP97477.

Proteomic databases

PaxDbP97477.
PRIDEP97477.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028997; ENSMUSP00000028997; ENSMUSG00000027496. [P97477-2]
ENSMUST00000109139; ENSMUSP00000104767; ENSMUSG00000027496. [P97477-1]
ENSMUST00000109140; ENSMUSP00000104768; ENSMUSG00000027496. [P97477-1]
GeneID20878.
KEGGmmu:20878.
UCSCuc008ocn.1. mouse. [P97477-2]
uc008oco.1. mouse. [P97477-1]

Organism-specific databases

CTD6790.
MGIMGI:894678. Aurka.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00550000074590.
HOVERGENHBG108519.
InParanoidQ8C3H8.
KOK11481.
OMAMERSKEN.
OrthoDBEOG74FF1F.
PhylomeDBP97477.
TreeFamTF105331.

Gene expression databases

ArrayExpressP97477.
BgeeP97477.
CleanExMM_AURKA.
GenevestigatorP97477.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP97477.
NextBio299731.
PROP97477.
SOURCESearch...

Entry information

Entry nameAURKA_MOUSE
AccessionPrimary (citable) accession number: P97477
Secondary accession number(s): O35624, Q8C3H8, Q91YU4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 27, 2003
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot