AURKA
entrez
6790
canonical
uniprot
O14965
canonical
ensembl
ENSG00000087586
resolver
ensp
ENSP00000216911
resolver
ensp
ENSP00000321591
resolver
ensp
ENSP00000360407
resolver
ensp
ENSP00000379247
resolver
ensp
ENSP00000379249
resolver
ensp
ENSP00000379250
resolver
ensp
ENSP00000379251
resolver
ensp
ENSP00000562491
resolver
ensp
ENSP00000562492
resolver
ensp
ENSP00000562495
resolver
ensp
ENSP00000562496
resolver
ensp
ENSP00000600791
resolver
ensp
ENSP00000600792
resolver
ensp
ENSP00000600794
resolver
ensp
ENSP00000600795
resolver
ensp
ENSP00000600799
resolver
ensp
ENSP00000600800
resolver
ensp
ENSP00000600801
resolver
ensp
ENSP00000600802
resolver
ensp
ENSP00000600803
resolver
ensp
ENSP00000600806
resolver
ensp
ENSP00000600811
resolver
ensp
ENSP00000636881
resolver
ensp
ENSP00000636882
resolver
enst
ENST00000312783
resolver
enst
ENST00000347343
resolver
enst
ENST00000371356
resolver
enst
ENST00000395911
resolver
enst
ENST00000395913
resolver
enst
ENST00000395914
resolver
enst
ENST00000395915
resolver
enst
ENST00000892432
resolver
enst
ENST00000892433
resolver
enst
ENST00000892436
resolver
enst
ENST00000892437
resolver
enst
ENST00000930732
resolver
enst
ENST00000930733
resolver
enst
ENST00000930735
resolver
enst
ENST00000930736
resolver
enst
ENST00000930740
resolver
enst
ENST00000930741
resolver
enst
ENST00000930742
resolver
enst
ENST00000930743
resolver
enst
ENST00000930744
resolver
enst
ENST00000930747
resolver
enst
ENST00000930752
resolver
enst
ENST00000966822
resolver
enst
ENST00000966823
resolver
genesymbol
AURKA
resolver
genesymbol_syn
AIK
resolver
genesymbol_syn
AIRK1
resolver
genesymbol_syn
ARK1
resolver
genesymbol_syn
AURA
resolver
genesymbol_syn
AYK1
resolver
genesymbol_syn
BTAK
resolver
genesymbol_syn
IAK1
resolver
genesymbol_syn
STK15
resolver
genesymbol_syn
STK6
resolver
hgnc
HGNC:11393
resolver
uniprot
E1P5F9
resolver
uniprot
O60445
resolver
uniprot
O75873
resolver
uniprot
Q9BQD6
resolver
uniprot
Q9UPG5
resolver
uniprot_entry
AURKA_HUMAN
resolver
uniprot_sec
E1P5F9
resolver
uniprot_sec
O60445
resolver
uniprot_sec
O75873
resolver
uniprot_sec
Q9BQD6
resolver
uniprot_sec
Q9UPG5
resolver
activity_regulation
ACTIVITY 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. Activated during the early phase of cilia disassembly in the presence of CIMAP3. Inhibited by the small molecule inhibitor VX-680 (PubMed:28218735). {ECO:0000269|PubMed:11039908, ECO:0000269|PubMed:12390251, ECO:0000269|PubMed:17360485, ECO:0000269|PubMed:28218735}.
uniprot
proteins
amino_acid_sequence
MDRSKENCISGPVKATAPVGGPKRVLVTQQFPCQNPLPVNSGQAQRVLCPSNSSQRIPLQAQKLVSSHKPVQNQKQKQLQATSVPHPVSRPLNNTQKSKQPLPSAPENNPEEELASKQKNEESKKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLEHPWITANSSKPSNCQNKESASKQS
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: Mitotic serine/threonine kinase that contributes to the regulation of cell cycle progression (PubMed:11039908, PubMed:12390251, PubMed:17125279, PubMed:17360485, PubMed:18615013, PubMed:26246606). 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 (PubMed:14523000, PubMed:26246606). Required for normal spindle positioning during mitosis and for the localization of NUMA1 and DCTN1 to the cell cortex during metaphase (PubMed:27335426). Required for initial activation of CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3, p53/TP53 and TPX2 (PubMed:11551964, PubMed:14702041, PubMed:15128871, PubMed:15147269, PubMed:15987997, PubMed:17604723, PubMed:18056443, PubMed:18615013). Phosphorylates MCRS1 which is required for MCRS1-mediated kinetochore fiber assembly and mitotic progression (PubMed:27192185). Regulates KIF2A tubulin depolymerase activity (PubMed:19351716). Important for microtubule formation and/or stabilization (PubMed:18056443). Required for normal axon formation (PubMed:19812038). Plays a role in microtubule remodeling during neurite extension (PubMed:19668197). 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 destabilizing p53/TP53 (PubMed:14702041). Phosphorylates its own inhibitors, the protein phosphatase type 1 (PP1) isoforms, to inhibit their activity (PubMed:11551964). Inhibits cilia outgrowth (By similarity). Required for cilia disassembly via phosphorylation of HDAC6 and subsequent deacetylation of alpha-tubulin (PubMed:17604723, PubMed:20643351). Regulates protein levels of the anti-apoptosis protein BIRC5 by suppressing the expression of the SCF(FBXL7) E3 ubiquitin-protein ligase substrate adapter FBXL7 through the phosphorylation of the transcription factor FOXP1 (PubMed:28218735). {ECO:0000250|UniProtKB:A0A8I3S724, ECO:0000269|PubMed:11039908, ECO:0000269|PubMed:11551964, ECO:0000269|PubMed:12390251, ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:14523000, ECO:0000269|PubMed:14702041, ECO:0000269|PubMed:15128871, ECO:0000269|PubMed:15147269, ECO:0000269|PubMed:15987997, ECO:0000269|PubMed:17125279, ECO:0000269|PubMed:17360485, ECO:0000269|PubMed:17604723, ECO:0000269|PubMed:18056443, ECO:0000269|PubMed:18615013, ECO:0000269|PubMed:19351716, ECO:0000269|PubMed:19668197, ECO:0000269|PubMed:19812038, ECO:0000269|PubMed:20643351, ECO:0000269|PubMed:26246606, ECO:0000269|PubMed:27192185, ECO:0000269|PubMed:27335426, ECO:0000269|PubMed:28218735}.
uniprot
proteins
mass_dalton
45823
uniprot
proteins
mutagenesis
MUTAGEN 162; /note="K->R: Loss of kinase activity."; /evidence="ECO:0000269|PubMed:14702041"; MUTAGEN 165; /note="F->A: Decreases the interaction with phosphatase type 1 isoforms."; /evidence="ECO:0000269|PubMed:11551964"; MUTAGEN 198; /note="G->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."; /evidence="ECO:0000269|PubMed:19357306"; MUTAGEN 205; /note="R->A: Reduces ubiquitination and proteasomal degradation."; /evidence="ECO:0000269|PubMed:10851084"; MUTAGEN 274; /note="D->N: Abolishes cilia disassembly and kinase activity."; /evidence="ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:17604723"; MUTAGEN 287; /note="T->A: No direct effect on catalytic activity."; /evidence="ECO:0000269|PubMed:19668197"; MUTAGEN 287; /note="T->E: Enhances interaction with TPX2."; /evidence="ECO:0000269|PubMed:19668197"; MUTAGEN 288; /note="T->A: Reduces cilia disassembly and kinase activity."; /evidence="ECO:0000269|PubMed:17604723"; MUTAGEN 288; /note="T->D: Mimics phosphorylation state and increases kinase activity."; /evidence="ECO:0000269|PubMed:11039908"; MUTAGEN 290; /note="C->A: Enhances stability; when associated with A-393."; /evidence="ECO:0000269|PubMed:27837025"; MUTAGEN 334; /note="Y->A: Reduces binding to MYCN."; /evidence="ECO:0000269|PubMed:27837025"; MUTAGEN 335; /note="Q->A: Reduces binding to MYCN."; /evidence="ECO:0000269|PubMed:27837025"; MUTAGEN 346; /note="F->A: Decreases the interaction with phosphatase type 1 isoforms."; /evidence="ECO:0000269|PubMed:11551964"; MUTAGEN 393; /note="C->A: Enhances stability; when associated with A-290."; /evidence="ECO:0000269|PubMed:27837025
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000269|PubMed:11039908, ECO:0000269|PubMed:11551964, ECO:0000269|PubMed:12390251, ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:16246726, ECO:0000269|PubMed:17229885, ECO:0000269|PubMed:18662907, ECO:0000269|PubMed:19668197}.; PTM: Ubiquitinated by the E3 ubiquitin-protein ligase complex SCF(FBXL7) during mitosis, leading to its degradation by the proteasome (By similarity). 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 (PubMed:10851084, PubMed:11039908). Ubiquitinated by the CUL3-KLHL18 ligase leading to its activation at the centrosome which is required for initiating mitotic entry (PubMed:23213400). Ubiquitination mediated by CUL3-KLHL18 ligase does not lead to its degradation by the proteasome (PubMed:23213400). {ECO:0000250|UniProtKB:P97477, ECO:0000269|PubMed:10851084, ECO:0000269|PubMed:11039908, ECO:0000269|PubMed:23213400}.
uniprot
proteins
protein_family
Aurora subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Ser/Thr protein kinase family
uniprot
proteins
pubmed
10851084
uniprot
proteins
pubmed
11039908
uniprot
proteins
pubmed
11551964
uniprot
proteins
pubmed
11780052
uniprot
proteins
pubmed
11790771
uniprot
proteins
pubmed
12237287
uniprot
proteins
pubmed
12390251
uniprot
proteins
pubmed
12467573
uniprot
proteins
pubmed
12576638
uniprot
proteins
pubmed
13678582
uniprot
proteins
pubmed
14523000
uniprot
proteins
pubmed
14580337
uniprot
proteins
pubmed
14603251
uniprot
proteins
pubmed
14625535
uniprot
proteins
pubmed
14702041
uniprot
proteins
pubmed
14990569
uniprot
proteins
pubmed
15128871
uniprot
proteins
pubmed
15147269
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15867347
uniprot
proteins
pubmed
15966895
uniprot
proteins
pubmed
15987997
uniprot
proteins
pubmed
16011022
uniprot
proteins
pubmed
16246726
uniprot
proteins
pubmed
16337122
uniprot
proteins
pubmed
16762494
uniprot
proteins
pubmed
16890155
uniprot
proteins
pubmed
17125279
uniprot
proteins
pubmed
17229885
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17360485
uniprot
proteins
pubmed
17488622
uniprot
proteins
pubmed
17604723
uniprot
proteins
pubmed
17726514
uniprot
proteins
pubmed
18056443
uniprot
proteins
pubmed
18615013
uniprot
proteins
pubmed
18662907
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19140666
uniprot
proteins
pubmed
19351716
uniprot
proteins
pubmed
19357306
uniprot
proteins
pubmed
19402633
uniprot
proteins
pubmed
19668197
uniprot
proteins
pubmed
19774610
uniprot
proteins
pubmed
19801554
uniprot
proteins
pubmed
19812038
uniprot
proteins
pubmed
20460379
uniprot
proteins
pubmed
20596670
uniprot
proteins
pubmed
20643351
uniprot
proteins
pubmed
21225229
uniprot
proteins
pubmed
21242313
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22014574
uniprot
proteins
pubmed
22753416
uniprot
proteins
pubmed
23213400
uniprot
proteins
pubmed
24574519
uniprot
proteins
pubmed
25657325
uniprot
proteins
pubmed
25986610
uniprot
proteins
pubmed
26246606
uniprot
proteins
pubmed
26341884
uniprot
proteins
pubmed
27192185
uniprot
proteins
pubmed
27335426
uniprot
proteins
pubmed
27837025
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28218735
uniprot
proteins
pubmed
30538148
uniprot
proteins
pubmed
9153231
uniprot
proteins
pubmed
9514916
uniprot
proteins
pubmed
9606188
uniprot
proteins
pubmed
9771714
uniprot
proteins
sequence_length
403
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:12576638, ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:17229885, ECO:0000269|PubMed:17726514, ECO:0000269|PubMed:19357306, ECO:0000269|PubMed:21225229, ECO:0000269|PubMed:22014574, ECO:0000269|PubMed:23213400, ECO:0000269|PubMed:25657325, ECO:0000269|PubMed:30538148, ECO:0000269|PubMed:9153231}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638, ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:17726514, ECO:0000269|PubMed:19351716, ECO:0000269|PubMed:25657325, ECO:0000269|PubMed:26246606, ECO:0000269|PubMed:9153231, ECO:0000269|PubMed:9606188}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:P97477}. Cell projection, neuron projection {ECO:0000250|UniProtKB:P97477}. Cell projection, cilium {ECO:0000269|PubMed:17604723}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:17604723}. Basolateral cell membrane {ECO:0000250|UniProtKB:F1PNY0}. Note=Detected at the neurite hillock in developing neurons (By similarity). Localizes at the centrosome in mitotic cells from early prophase until telophase, but also localizes to the spindle pole MTs from prophase to anaphase (PubMed:17229885, PubMed:21225229, PubMed:9606188). Colocalized with SIRT2 at centrosome (PubMed:22014574). Moves to the midbody during both telophase and cytokinesis (PubMed:17726514). Associates with both the pericentriolar material (PCM) and centrioles (PubMed:22014574). The localization to the spindle poles is regulated by AAAS (PubMed:26246606). {ECO:0000250|UniProtKB:P97477, ECO:0000269|PubMed:17229885, ECO:0000269|PubMed:17726514, ECO:0000269|PubMed:21225229, ECO:0000269|PubMed:22014574, ECO:0000269|PubMed:26246606, ECO:0000269|PubMed:9606188}.
uniprot
proteins