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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 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.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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei143 – 1431ATP; via amide nitrogen
Binding sitei162 – 1621ATP
Active sitei256 – 2561Proton acceptorPROSITE-ProRule annotation1 Publication
Binding sitei274 – 2741ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi210 – 2134ATP

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

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-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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi162 – 1621K → R: Loss of kinase activity. 2 Publications
Mutagenesisi165 – 1651F → A: Decreases the interaction with phosphatase type 1 isoforms. 1 Publication
Mutagenesisi198 – 1981G → 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 Publication
Mutagenesisi205 – 2051R → A: Reduces ubiquitination and proteasomal degradation. 1 Publication
Mutagenesisi274 – 2741D → N: Abolishes autophosphorylation. 1 Publication
Mutagenesisi287 – 2871T → A: No direct effect on catalytic activity. 1 Publication
Mutagenesisi287 – 2871T → E: Enhances interaction with TPX2. 1 Publication
Mutagenesisi288 – 2881T → D: Mimics phosphorylation state and increases kinase activity. 1 Publication
Mutagenesisi346 – 3461F → A: Decreases the interaction with phosphatase type 1 isoforms. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

MalaCardsiAURKA.
PharmGKBiPA36201.

Chemistry

ChEMBLiCHEMBL3430911.
GuidetoPHARMACOLOGYi1936.

Polymorphism and mutation databases

BioMutaiAURKA.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 403403Aurora kinase APRO_0000086692Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei41 – 411PhosphoserineCombined sources
Modified residuei51 – 511Phosphoserine1 Publication
Modified residuei287 – 2871Phosphothreonine2 Publications
Modified residuei288 – 2881Phosphothreonine7 Publications
Modified residuei342 – 3421Phosphoserine; by PKA and PAK1 Publication

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.
PhosphoSiteiO14965.

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 interactions.
DIPiDIP-33068N.
IntActiO14965. 97 interactions.
MINTiMINT-254096.
STRINGi9606.ENSP00000216911.

Chemistry

BindingDBiO14965.

Structurei

Secondary structure

1
403
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi130 – 1323Combined sources
Beta strandi133 – 14210Combined sources
Beta strandi145 – 1528Combined sources
Turni153 – 1553Combined sources
Beta strandi158 – 1658Combined sources
Helixi166 – 1727Combined sources
Helixi175 – 18713Combined sources
Beta strandi191 – 1933Combined sources
Beta strandi196 – 2016Combined sources
Beta strandi203 – 2108Combined sources
Beta strandi214 – 2174Combined sources
Helixi218 – 2258Combined sources
Helixi230 – 24920Combined sources
Helixi259 – 2613Combined sources
Beta strandi262 – 2643Combined sources
Beta strandi266 – 2683Combined sources
Beta strandi270 – 2723Combined sources
Beta strandi277 – 2793Combined sources
Turni283 – 2853Combined sources
Beta strandi287 – 2893Combined sources
Helixi290 – 2923Combined sources
Helixi293 – 2953Combined sources
Helixi298 – 3014Combined sources
Turni302 – 3043Combined sources
Helixi307 – 3093Combined sources
Helixi310 – 32415Combined sources
Helixi334 – 3429Combined sources
Beta strandi350 – 3523Combined sources
Helixi354 – 36310Combined sources
Helixi368 – 3703Combined sources
Helixi374 – 3785Combined sources
Helixi381 – 3866Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
5AADX-ray3.10A122-403[»]
5AAEX-ray3.11A122-403[»]
5AAFX-ray2.78A122-403[»]
5AAGX-ray2.85A122-403[»]
5EW9X-ray2.18A123-390[»]
ProteinModelPortaliO14965.
SMRiO14965. Positions 76-394.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO14965.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini133 – 383251Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni280 – 29314Activation segmentAdd
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

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111G → R.
Corresponds to variant rs6069717 [ dbSNP | Ensembl ].
VAR_030840
Natural varianti31 – 311F → I.5 Publications
Corresponds to variant rs2273535 [ dbSNP | Ensembl ].
VAR_030841
Natural varianti50 – 501P → L.1 Publication
Corresponds to variant rs34572020 [ dbSNP | Ensembl ].
VAR_041127
Natural varianti57 – 571V → I.4 Publications
Corresponds to variant rs1047972 [ dbSNP | Ensembl ].
VAR_030842
Natural varianti104 – 1041S → L.
Corresponds to variant rs2230743 [ dbSNP | Ensembl ].
VAR_061745
Natural varianti155 – 1551S → R in a colorectal adenocarcinoma sample; somatic mutation; reduces interaction with TPX2. 2 Publications
VAR_041128
Natural varianti174 – 1741V → M in a metastatic melanoma sample; somatic mutation; constitutively enhanced kinase activity. 2 Publications
VAR_041129
Natural varianti373 – 3731M → V.1 Publication
Corresponds to variant rs33923703 [ dbSNP | Ensembl ].
VAR_041130

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.
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.
UniGeneiHs.250822.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
5AADX-ray3.10A122-403[»]
5AAEX-ray3.11A122-403[»]
5AAFX-ray2.78A122-403[»]
5AAGX-ray2.85A122-403[»]
5EW9X-ray2.18A123-390[»]
ProteinModelPortaliO14965.
SMRiO14965. Positions 76-394.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112666. 279 interactions.
DIPiDIP-33068N.
IntActiO14965. 97 interactions.
MINTiMINT-254096.
STRINGi9606.ENSP00000216911.

Chemistry

BindingDBiO14965.
ChEMBLiCHEMBL3430911.
GuidetoPHARMACOLOGYi1936.

PTM databases

iPTMnetiO14965.
PhosphoSiteiO14965.

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.
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

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-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: September 7, 2016
This is version 190 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.