Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Aurora kinase A

Gene

AURKA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mitotic serine/threonine kinase 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.21 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.4 Publications

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. Activated during the early phase of cilia disassembly in the presence of PIFO.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei143ATP; via amide nitrogen1
Binding sitei162ATP1
Active sitei256Proton acceptorPROSITE-ProRule annotation1 Publication1
Binding sitei274ATP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi210 – 213ATP4

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • histone serine kinase activity Source: GO_Central
  • protein kinase activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein serine/threonine/tyrosine kinase activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: Reactome

GO - Biological processi

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

BioCyciZFISH:HS01581-MONOMER.
BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-6804114. TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-HSA-8854518. AURKA Activation by TPX2.
R-HSA-8854521. Interaction between PHLDA1 and AURKA.
SignaLinkiO14965.
SIGNORiO14965.

Names & Taxonomyi

Protein namesi
Recommended name:
Aurora kinase A (EC:2.7.11.1)
Alternative name(s):
Aurora 2
Aurora/IPL1-related kinase 1
Short name:
ARK-1
Short name:
Aurora-related kinase 1
Short name:
hARK1
Breast tumor-amplified kinase
Serine/threonine-protein kinase 15
Serine/threonine-protein kinase 6
Serine/threonine-protein kinase aurora-A
Gene namesi
Name:AURKA
Synonyms:AIK, AIRK1, ARK1, AURA, AYK1, BTAK, IAK1, STK15, STK6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:11393. AURKA.

Subcellular locationi

GO - Cellular componenti

  • axon hillock Source: Ensembl
  • centriole Source: UniProtKB-SubCell
  • centrosome Source: UniProtKB
  • chromosome passenger complex Source: GO_Central
  • cilium Source: UniProtKB-KW
  • condensed nuclear chromosome, centromeric region Source: GO_Central
  • cytosol Source: Reactome
  • germinal vesicle Source: Ensembl
  • meiotic spindle Source: Ensembl
  • microtubule Source: UniProtKB-KW
  • microtubule cytoskeleton Source: BHF-UCL
  • midbody Source: UniProtKB
  • mitotic spindle Source: Ensembl
  • nucleoplasm Source: Reactome
  • nucleus Source: BHF-UCL
  • perinuclear region of cytoplasm Source: BHF-UCL
  • pronucleus Source: Ensembl
  • spindle Source: UniProtKB
  • spindle midzone Source: GO_Central
  • spindle pole centrosome Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi162K → R: Loss of kinase activity. 2 Publications1
Mutagenesisi165F → A: Decreases the interaction with phosphatase type 1 isoforms. 1 Publication1
Mutagenesisi198G → N: Reduces interaction with TPX2. Reduces kinase activity tenfold. Promotes interaction with the AURKB binding partners INCENP and BIRC5 that are normally not bound by AURKA. 1 Publication1
Mutagenesisi205R → A: Reduces ubiquitination and proteasomal degradation. 1 Publication1
Mutagenesisi274D → N: Abolishes autophosphorylation. 1 Publication1
Mutagenesisi287T → A: No direct effect on catalytic activity. 1 Publication1
Mutagenesisi287T → E: Enhances interaction with TPX2. 1 Publication1
Mutagenesisi288T → D: Mimics phosphorylation state and increases kinase activity. 1 Publication1
Mutagenesisi346F → A: Decreases the interaction with phosphatase type 1 isoforms. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi6790.
MalaCardsiAURKA.
PharmGKBiPA36201.

Chemistry databases

ChEMBLiCHEMBL4722.
GuidetoPHARMACOLOGYi1936.

Polymorphism and mutation databases

BioMutaiAURKA.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000866921 – 403Aurora kinase AAdd BLAST403

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei41PhosphoserineCombined sources1
Modified residuei51Phosphoserine1 Publication1
Modified residuei287Phosphothreonine2 Publications1
Modified residuei288Phosphothreonine7 Publications1
Modified residuei342Phosphoserine; by PKA and PAK1 Publication1

Post-translational modificationi

Activated by phosphorylation at Thr-288; this brings about a change in the conformation of the activation segment. Phosphorylation at Thr-288 varies during the cell cycle and is highest during M phase. Autophosphorylated at Thr-288 upon TPX2 binding. Thr-288 can be phosphorylated by several kinases, including PAK and PKA. Protein phosphatase type 1 (PP1) binds AURKA and inhibits its activity by dephosphorylating Thr-288 during mitosis. Phosphorylation at Ser-342 decreases the kinase activity. PPP2CA controls degradation by dephosphorylating Ser-51 at the end of mitosis.10 Publications
Ubiquitinated by the E3 ubiquitin-protein ligase complex SCF(FBXL7) during mitosis, leading to its degradation by the proteasome. Ubiquitinated by CHFR, leading to its degradation by the proteasome (By similarity). Ubiquitinated by the anaphase-promoting complex (APC), leading to its degradation by the proteasome.By similarity2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO14965.
MaxQBiO14965.
PaxDbiO14965.
PeptideAtlasiO14965.
PRIDEiO14965.

PTM databases

iPTMnetiO14965.
PhosphoSitePlusiO14965.

Expressioni

Tissue specificityi

Highly expressed in testis and weakly in skeletal muscle, thymus and spleen. Also highly expressed in colon, ovarian, prostate, neuroblastoma, breast and cervical cancer cell lines.

Inductioni

Expression is cell-cycle regulated, low in G1/S, accumulates during G2/M, and decreases rapidly after.5 Publications

Gene expression databases

BgeeiENSG00000087586.
CleanExiHS_AURKA.
ExpressionAtlasiO14965. baseline and differential.
GenevisibleiO14965. HS.

Organism-specific databases

HPAiCAB001454.
HPA002636.

Interactioni

Subunit structurei

Interacts with FBXL7 (By similarity). Interacts with CPEB1, JTB, TACC1, TPX2, PPP2CA, as well as with the protein phosphatase type 1 (PP1) isoforms PPP1CA, PPP1CB and PPP1CC. Interacts also with its substrates ARHGEF2, BORA, BRCA1, KIF2A, PARD3, and p53/TP53. Interaction with BORA promotes phosphorylation of PLK1. Interacts with PIFO. Interacts with GADD45A, competing with its oligomerization. Interacts (via C-terminus) with AUNIP (via C-terminus). Identified in a complex with AUNIP and NIN. Interacts with FRY; this interaction facilitates AURKA-mediated PLK1 phosphorylation. Interacts with SIRT2.By similarity26 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AURKAIP1Q9NWT82EBI-448680,EBI-448665
EGFRP005334EBI-448680,EBI-297353
HNRNPKP619782EBI-448680,EBI-304185
IKQ131233EBI-448680,EBI-713456
MYCNP041989EBI-448680,EBI-878369
NPM1P067483EBI-448680,EBI-78579
Sirt2Q8VDQ85EBI-448680,EBI-911012From a different organism.
TP73O1535011EBI-448680,EBI-389606
TPX2Q9ULW02EBI-448680,EBI-1037322

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112666. 279 interactors.
DIPiDIP-33068N.
IntActiO14965. 98 interactors.
MINTiMINT-254096.
STRINGi9606.ENSP00000216911.

Chemistry databases

BindingDBiO14965.

Structurei

Secondary structure

1403
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi130 – 132Combined sources3
Beta strandi133 – 141Combined sources9
Beta strandi143 – 152Combined sources10
Turni153 – 155Combined sources3
Beta strandi158 – 165Combined sources8
Helixi166 – 171Combined sources6
Turni172 – 174Combined sources3
Helixi175 – 185Combined sources11
Beta strandi191 – 193Combined sources3
Beta strandi196 – 201Combined sources6
Beta strandi203 – 210Combined sources8
Beta strandi214 – 217Combined sources4
Helixi218 – 225Combined sources8
Helixi230 – 249Combined sources20
Helixi259 – 261Combined sources3
Beta strandi262 – 264Combined sources3
Beta strandi266 – 268Combined sources3
Beta strandi270 – 272Combined sources3
Beta strandi277 – 279Combined sources3
Beta strandi280 – 283Combined sources4
Beta strandi287 – 289Combined sources3
Helixi290 – 292Combined sources3
Helixi293 – 295Combined sources3
Helixi298 – 302Combined sources5
Helixi307 – 309Combined sources3
Helixi310 – 324Combined sources15
Helixi334 – 342Combined sources9
Beta strandi350 – 352Combined sources3
Helixi354 – 363Combined sources10
Helixi368 – 370Combined sources3
Helixi374 – 378Combined sources5
Helixi381 – 386Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MQ4X-ray1.90A125-391[»]
1MUOX-ray2.90A107-403[»]
1OL5X-ray2.50A122-403[»]
1OL6X-ray3.00A122-403[»]
1OL7X-ray2.75A122-403[»]
2BMCX-ray2.60A/B/C/D/E/F100-403[»]
2C6DX-ray2.20A124-398[»]
2C6EX-ray2.10A/B123-401[»]
2DWBX-ray2.50A122-403[»]
2J4ZX-ray2.00A/B100-403[»]
2J50X-ray3.00A/B126-403[»]
2NP8X-ray2.25A125-391[»]
2W1CX-ray3.24A122-389[»]
2W1DX-ray2.97A122-389[»]
2W1EX-ray2.93A122-389[»]
2W1FX-ray2.85A122-389[»]
2W1GX-ray2.71A122-389[»]
2WQEX-ray2.50A127-388[»]
2WTVX-ray2.40A/B/C/D122-403[»]
2WTWX-ray3.30A122-403[»]
2X6DX-ray2.80A122-403[»]
2X6EX-ray3.35A122-403[»]
2X81X-ray2.91A126-391[»]
2XNEX-ray2.80A122-392[»]
2XNGX-ray2.60A122-403[»]
2XRUX-ray2.90A126-403[»]
3COHX-ray2.70A/B124-391[»]
3E5AX-ray2.30A125-391[»]
3EFWX-ray2.29A/B125-391[»]
3FDNX-ray1.90A123-401[»]
3H0YX-ray2.50A124-391[»]
3H0ZX-ray2.92A/B/C124-391[»]
3H10X-ray2.20A/B/D124-391[»]
3HA6X-ray2.36A125-391[»]
3K5UX-ray2.35A123-401[»]
3LAUX-ray2.10A125-399[»]
3M11X-ray2.75A123-401[»]
3MYGX-ray2.40A125-391[»]
3NRMX-ray3.05A126-403[»]
3O50X-ray2.00A/B125-391[»]
3O51X-ray3.20A125-391[»]
3P9JX-ray2.80A125-391[»]
3QBNX-ray3.50A124-403[»]
3R21X-ray2.90A126-391[»]
3R22X-ray2.90A126-391[»]
3UNZX-ray2.80A/B123-401[»]
3UO4X-ray2.45A123-401[»]
3UO5X-ray2.70A123-401[»]
3UO6X-ray2.80A/B123-401[»]
3UODX-ray2.50A123-401[»]
3UOHX-ray2.80A/B123-401[»]
3UOJX-ray2.90A/B123-401[»]
3UOKX-ray2.95A/B123-401[»]
3UOLX-ray2.40A/B123-401[»]
3UP2X-ray2.30A123-401[»]
3UP7X-ray3.05A123-401[»]
3VAPX-ray2.66A125-391[»]
3W10X-ray2.70A126-403[»]
3W16X-ray2.80A126-403[»]
3W18X-ray2.50A/B126-403[»]
3W2CX-ray2.45A/C/E/G128-388[»]
4B0GX-ray2.50A122-403[»]
4BN1X-ray2.50A122-403[»]
4BYIX-ray2.60A122-403[»]
4BYJX-ray2.75A122-403[»]
4C3PX-ray2.69A/D122-403[»]
4C3RX-ray2.79A122-403[»]
4CEGX-ray2.10A122-403[»]
4DEAX-ray2.45A123-401[»]
4DEBX-ray3.05A123-401[»]
4DEDX-ray3.05A123-401[»]
4DEEX-ray2.30A123-401[»]
4DHFX-ray2.80A/B126-391[»]
4J8MX-ray1.85A123-401[»]
4J8NX-ray3.14A/B/C/D123-401[»]
4JAIX-ray3.20A122-396[»]
4JAJX-ray2.70A122-396[»]
4JBOX-ray2.49A123-401[»]
4JBPX-ray2.45A123-401[»]
4JBQX-ray2.30A123-401[»]
4O0SX-ray2.50A122-403[»]
4O0UX-ray2.60A122-403[»]
4O0WX-ray2.60A122-403[»]
4PRJX-ray2.80A124-391[»]
4UTDX-ray2.36A122-403[»]
4UYNX-ray1.90A125-399[»]
4UZDX-ray3.20A/B125-399[»]
4UZHX-ray2.00A125-399[»]
4ZS0X-ray3.00A122-403[»]
4ZTQX-ray2.80A122-403[»]
4ZTRX-ray2.85A122-403[»]
4ZTSX-ray2.90A122-403[»]
5AADX-ray3.10A122-403[»]
5AAEX-ray3.11A122-403[»]
5AAFX-ray2.78A122-403[»]
5AAGX-ray2.85A122-403[»]
5DN3X-ray2.05A125-391[»]
5DNRX-ray1.95A125-391[»]
5DOSX-ray2.98A126-390[»]
5DPVX-ray2.29A126-390[»]
5DR2X-ray2.46A128-390[»]
5DR6X-ray2.53A126-390[»]
5DR9X-ray2.47A126-390[»]
5DRDX-ray2.13A126-390[»]
5DT0X-ray2.15A126-390[»]
5DT3X-ray2.33A126-390[»]
5DT4X-ray2.86A126-390[»]
5EW9X-ray2.18A123-390[»]
5L8JX-ray1.68A122-403[»]
5L8KX-ray1.79A122-403[»]
5L8LX-ray1.67A122-403[»]
ProteinModelPortaliO14965.
SMRiO14965.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO14965.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini133 – 383Protein kinasePROSITE-ProRule annotationAdd BLAST251

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni280 – 293Activation segmentAdd BLAST14

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

eggNOGiKOG0580. Eukaryota.
ENOG410XNRB. LUCA.
HOVERGENiHBG108519.
InParanoidiO14965.
KOiK11481.
OrthoDBiEOG091G0EU2.
PhylomeDBiO14965.
TreeFamiTF105331.

Family and domain databases

InterProiIPR030616. Aur.
IPR030611. AURKA.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24350. PTHR24350. 1 hit.
PTHR24350:SF5. PTHR24350:SF5. 1 hit.
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]

Sequencei

Sequence statusi: Complete.

O14965-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDRSKENCIS GPVKATAPVG GPKRVLVTQQ FPCQNPLPVN SGQAQRVLCP
60 70 80 90 100
SNSSQRVPLQ AQKLVSSHKP VQNQKQKQLQ ATSVPHPVSR PLNNTQKSKQ
110 120 130 140 150
PLPSAPENNP EEELASKQKN EESKKRQWAL EDFEIGRPLG KGKFGNVYLA
160 170 180 190 200
REKQSKFILA LKVLFKAQLE KAGVEHQLRR EVEIQSHLRH PNILRLYGYF
210 220 230 240 250
HDATRVYLIL EYAPLGTVYR ELQKLSKFDE QRTATYITEL ANALSYCHSK
260 270 280 290 300
RVIHRDIKPE NLLLGSAGEL KIADFGWSVH APSSRRTTLC GTLDYLPPEM
310 320 330 340 350
IEGRMHDEKV DLWSLGVLCY EFLVGKPPFE ANTYQETYKR ISRVEFTFPD
360 370 380 390 400
FVTEGARDLI SRLLKHNPSQ RPMLREVLEH PWITANSSKP SNCQNKESAS

KQS
Length:403
Mass (Da):45,809
Last modified:January 27, 2003 - v2
Checksum:i125F3594834CD157
GO

Sequence cautioni

The sequence BAA23592 differs from that shown. Reason: Frameshift at positions 105, 125, 129, 235 and 241.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03084011G → R.Corresponds to variant rs6069717dbSNPEnsembl.1
Natural variantiVAR_03084131F → I.5 PublicationsCorresponds to variant rs2273535dbSNPEnsembl.1
Natural variantiVAR_04112750P → L.1 PublicationCorresponds to variant rs34572020dbSNPEnsembl.1
Natural variantiVAR_03084257V → I.4 PublicationsCorresponds to variant rs1047972dbSNPEnsembl.1
Natural variantiVAR_061745104S → L.Corresponds to variant rs2230743dbSNPEnsembl.1
Natural variantiVAR_041128155S → R in a colorectal adenocarcinoma sample; somatic mutation; reduces interaction with TPX2. 2 Publications1
Natural variantiVAR_041129174V → M in a metastatic melanoma sample; somatic mutation; constitutively enhanced kinase activity. 2 Publications1
Natural variantiVAR_041130373M → V.1 PublicationCorresponds to variant rs33923703dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D84212 mRNA. Translation: BAA23592.1. Frameshift.
AF008551 mRNA. Translation: AAC12708.1.
AF011467 Genomic DNA. Translation: AAC23448.1.
AF011468 mRNA. Translation: AAC63902.1.
AF195947
, AF195942, AF195943, AF195944, AF195945, AF195946 Genomic DNA. Translation: AAF29508.1.
AL121914 Genomic DNA. Translation: CAC12717.1.
CH471077 Genomic DNA. Translation: EAW75550.1.
CH471077 Genomic DNA. Translation: EAW75551.1.
CH471077 Genomic DNA. Translation: EAW75552.1.
CH471077 Genomic DNA. Translation: EAW75553.1.
CH471077 Genomic DNA. Translation: EAW75554.1.
CH471077 Genomic DNA. Translation: EAW75555.1.
CH471077 Genomic DNA. Translation: EAW75556.1.
CH471077 Genomic DNA. Translation: EAW75557.1.
CH471077 Genomic DNA. Translation: EAW75558.1.
CH471077 Genomic DNA. Translation: EAW75559.1.
CH471077 Genomic DNA. Translation: EAW75561.1.
CH471077 Genomic DNA. Translation: EAW75562.1.
BC001280 mRNA. Translation: AAH01280.1.
BC002499 mRNA. Translation: AAH02499.1.
BC006423 mRNA. Translation: AAH06423.1.
BC027464 mRNA. Translation: AAH27464.1.
CCDSiCCDS13451.1.
PIRiJC5974.
RefSeqiNP_001310232.1. NM_001323303.1.
NP_001310233.1. NM_001323304.1.
NP_001310234.1. NM_001323305.1.
NP_003591.2. NM_003600.3.
NP_940835.1. NM_198433.2.
NP_940836.1. NM_198434.2.
NP_940837.1. NM_198435.2.
NP_940838.1. NM_198436.2.
NP_940839.1. NM_198437.2.
XP_016883524.1. XM_017028035.1.
UniGeneiHs.250822.

Genome annotation databases

EnsembliENST00000312783; ENSP00000321591; ENSG00000087586.
ENST00000347343; ENSP00000216911; ENSG00000087586.
ENST00000371356; ENSP00000360407; ENSG00000087586.
ENST00000395911; ENSP00000379247; ENSG00000087586.
ENST00000395913; ENSP00000379249; ENSG00000087586.
ENST00000395914; ENSP00000379250; ENSG00000087586.
ENST00000395915; ENSP00000379251; ENSG00000087586.
GeneIDi6790.
KEGGihsa:6790.
UCSCiuc002xxe.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D84212 mRNA. Translation: BAA23592.1. Frameshift.
AF008551 mRNA. Translation: AAC12708.1.
AF011467 Genomic DNA. Translation: AAC23448.1.
AF011468 mRNA. Translation: AAC63902.1.
AF195947
, AF195942, AF195943, AF195944, AF195945, AF195946 Genomic DNA. Translation: AAF29508.1.
AL121914 Genomic DNA. Translation: CAC12717.1.
CH471077 Genomic DNA. Translation: EAW75550.1.
CH471077 Genomic DNA. Translation: EAW75551.1.
CH471077 Genomic DNA. Translation: EAW75552.1.
CH471077 Genomic DNA. Translation: EAW75553.1.
CH471077 Genomic DNA. Translation: EAW75554.1.
CH471077 Genomic DNA. Translation: EAW75555.1.
CH471077 Genomic DNA. Translation: EAW75556.1.
CH471077 Genomic DNA. Translation: EAW75557.1.
CH471077 Genomic DNA. Translation: EAW75558.1.
CH471077 Genomic DNA. Translation: EAW75559.1.
CH471077 Genomic DNA. Translation: EAW75561.1.
CH471077 Genomic DNA. Translation: EAW75562.1.
BC001280 mRNA. Translation: AAH01280.1.
BC002499 mRNA. Translation: AAH02499.1.
BC006423 mRNA. Translation: AAH06423.1.
BC027464 mRNA. Translation: AAH27464.1.
CCDSiCCDS13451.1.
PIRiJC5974.
RefSeqiNP_001310232.1. NM_001323303.1.
NP_001310233.1. NM_001323304.1.
NP_001310234.1. NM_001323305.1.
NP_003591.2. NM_003600.3.
NP_940835.1. NM_198433.2.
NP_940836.1. NM_198434.2.
NP_940837.1. NM_198435.2.
NP_940838.1. NM_198436.2.
NP_940839.1. NM_198437.2.
XP_016883524.1. XM_017028035.1.
UniGeneiHs.250822.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MQ4X-ray1.90A125-391[»]
1MUOX-ray2.90A107-403[»]
1OL5X-ray2.50A122-403[»]
1OL6X-ray3.00A122-403[»]
1OL7X-ray2.75A122-403[»]
2BMCX-ray2.60A/B/C/D/E/F100-403[»]
2C6DX-ray2.20A124-398[»]
2C6EX-ray2.10A/B123-401[»]
2DWBX-ray2.50A122-403[»]
2J4ZX-ray2.00A/B100-403[»]
2J50X-ray3.00A/B126-403[»]
2NP8X-ray2.25A125-391[»]
2W1CX-ray3.24A122-389[»]
2W1DX-ray2.97A122-389[»]
2W1EX-ray2.93A122-389[»]
2W1FX-ray2.85A122-389[»]
2W1GX-ray2.71A122-389[»]
2WQEX-ray2.50A127-388[»]
2WTVX-ray2.40A/B/C/D122-403[»]
2WTWX-ray3.30A122-403[»]
2X6DX-ray2.80A122-403[»]
2X6EX-ray3.35A122-403[»]
2X81X-ray2.91A126-391[»]
2XNEX-ray2.80A122-392[»]
2XNGX-ray2.60A122-403[»]
2XRUX-ray2.90A126-403[»]
3COHX-ray2.70A/B124-391[»]
3E5AX-ray2.30A125-391[»]
3EFWX-ray2.29A/B125-391[»]
3FDNX-ray1.90A123-401[»]
3H0YX-ray2.50A124-391[»]
3H0ZX-ray2.92A/B/C124-391[»]
3H10X-ray2.20A/B/D124-391[»]
3HA6X-ray2.36A125-391[»]
3K5UX-ray2.35A123-401[»]
3LAUX-ray2.10A125-399[»]
3M11X-ray2.75A123-401[»]
3MYGX-ray2.40A125-391[»]
3NRMX-ray3.05A126-403[»]
3O50X-ray2.00A/B125-391[»]
3O51X-ray3.20A125-391[»]
3P9JX-ray2.80A125-391[»]
3QBNX-ray3.50A124-403[»]
3R21X-ray2.90A126-391[»]
3R22X-ray2.90A126-391[»]
3UNZX-ray2.80A/B123-401[»]
3UO4X-ray2.45A123-401[»]
3UO5X-ray2.70A123-401[»]
3UO6X-ray2.80A/B123-401[»]
3UODX-ray2.50A123-401[»]
3UOHX-ray2.80A/B123-401[»]
3UOJX-ray2.90A/B123-401[»]
3UOKX-ray2.95A/B123-401[»]
3UOLX-ray2.40A/B123-401[»]
3UP2X-ray2.30A123-401[»]
3UP7X-ray3.05A123-401[»]
3VAPX-ray2.66A125-391[»]
3W10X-ray2.70A126-403[»]
3W16X-ray2.80A126-403[»]
3W18X-ray2.50A/B126-403[»]
3W2CX-ray2.45A/C/E/G128-388[»]
4B0GX-ray2.50A122-403[»]
4BN1X-ray2.50A122-403[»]
4BYIX-ray2.60A122-403[»]
4BYJX-ray2.75A122-403[»]
4C3PX-ray2.69A/D122-403[»]
4C3RX-ray2.79A122-403[»]
4CEGX-ray2.10A122-403[»]
4DEAX-ray2.45A123-401[»]
4DEBX-ray3.05A123-401[»]
4DEDX-ray3.05A123-401[»]
4DEEX-ray2.30A123-401[»]
4DHFX-ray2.80A/B126-391[»]
4J8MX-ray1.85A123-401[»]
4J8NX-ray3.14A/B/C/D123-401[»]
4JAIX-ray3.20A122-396[»]
4JAJX-ray2.70A122-396[»]
4JBOX-ray2.49A123-401[»]
4JBPX-ray2.45A123-401[»]
4JBQX-ray2.30A123-401[»]
4O0SX-ray2.50A122-403[»]
4O0UX-ray2.60A122-403[»]
4O0WX-ray2.60A122-403[»]
4PRJX-ray2.80A124-391[»]
4UTDX-ray2.36A122-403[»]
4UYNX-ray1.90A125-399[»]
4UZDX-ray3.20A/B125-399[»]
4UZHX-ray2.00A125-399[»]
4ZS0X-ray3.00A122-403[»]
4ZTQX-ray2.80A122-403[»]
4ZTRX-ray2.85A122-403[»]
4ZTSX-ray2.90A122-403[»]
5AADX-ray3.10A122-403[»]
5AAEX-ray3.11A122-403[»]
5AAFX-ray2.78A122-403[»]
5AAGX-ray2.85A122-403[»]
5DN3X-ray2.05A125-391[»]
5DNRX-ray1.95A125-391[»]
5DOSX-ray2.98A126-390[»]
5DPVX-ray2.29A126-390[»]
5DR2X-ray2.46A128-390[»]
5DR6X-ray2.53A126-390[»]
5DR9X-ray2.47A126-390[»]
5DRDX-ray2.13A126-390[»]
5DT0X-ray2.15A126-390[»]
5DT3X-ray2.33A126-390[»]
5DT4X-ray2.86A126-390[»]
5EW9X-ray2.18A123-390[»]
5L8JX-ray1.68A122-403[»]
5L8KX-ray1.79A122-403[»]
5L8LX-ray1.67A122-403[»]
ProteinModelPortaliO14965.
SMRiO14965.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112666. 279 interactors.
DIPiDIP-33068N.
IntActiO14965. 98 interactors.
MINTiMINT-254096.
STRINGi9606.ENSP00000216911.

Chemistry databases

BindingDBiO14965.
ChEMBLiCHEMBL4722.
GuidetoPHARMACOLOGYi1936.

PTM databases

iPTMnetiO14965.
PhosphoSitePlusiO14965.

Polymorphism and mutation databases

BioMutaiAURKA.

Proteomic databases

EPDiO14965.
MaxQBiO14965.
PaxDbiO14965.
PeptideAtlasiO14965.
PRIDEiO14965.

Protocols and materials databases

DNASUi6790.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000312783; ENSP00000321591; ENSG00000087586.
ENST00000347343; ENSP00000216911; ENSG00000087586.
ENST00000371356; ENSP00000360407; ENSG00000087586.
ENST00000395911; ENSP00000379247; ENSG00000087586.
ENST00000395913; ENSP00000379249; ENSG00000087586.
ENST00000395914; ENSP00000379250; ENSG00000087586.
ENST00000395915; ENSP00000379251; ENSG00000087586.
GeneIDi6790.
KEGGihsa:6790.
UCSCiuc002xxe.1. human.

Organism-specific databases

CTDi6790.
DisGeNETi6790.
GeneCardsiAURKA.
H-InvDBHIX0015930.
HGNCiHGNC:11393. AURKA.
HPAiCAB001454.
HPA002636.
MalaCardsiAURKA.
MIMi603072. gene.
neXtProtiNX_O14965.
PharmGKBiPA36201.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0580. Eukaryota.
ENOG410XNRB. LUCA.
HOVERGENiHBG108519.
InParanoidiO14965.
KOiK11481.
OrthoDBiEOG091G0EU2.
PhylomeDBiO14965.
TreeFamiTF105331.

Enzyme and pathway databases

BioCyciZFISH:HS01581-MONOMER.
BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-6804114. TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-HSA-8854518. AURKA Activation by TPX2.
R-HSA-8854521. Interaction between PHLDA1 and AURKA.
SignaLinkiO14965.
SIGNORiO14965.

Miscellaneous databases

EvolutionaryTraceiO14965.
GeneWikiiAurora_A_kinase.
GenomeRNAii6790.
PROiO14965.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000087586.
CleanExiHS_AURKA.
ExpressionAtlasiO14965. baseline and differential.
GenevisibleiO14965. HS.

Family and domain databases

InterProiIPR030616. Aur.
IPR030611. AURKA.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24350. PTHR24350. 1 hit.
PTHR24350:SF5. PTHR24350:SF5. 1 hit.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiAURKA_HUMAN
AccessioniPrimary (citable) accession number: O14965
Secondary accession number(s): E1P5F9
, O60445, O75873, Q9BQD6, Q9UPG5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 27, 2003
Last sequence update: January 27, 2003
Last modified: November 30, 2016
This is version 193 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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.

Caution

Authors initially considered AURKA/STK6 and STK15 as 2 different proteins (PubMed:9771714). It is clear that they are the same protein.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.