| Function: |
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. |
| Tissue Specificity: |
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. |
| Sequence Similarities: |
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily. |
| Post-Translational Modification: |
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. |
| Cellular locations: |
Cytoplasm > Cytoskeleton > Microtubule organizing center > Centrosome. Cytoplasm > Cytoskeleton > Spindle pole. Cytoplasm > Cytoskeleton > Cilium basal body. Cytoplasm > Cytoskeleton > Microtubule organizing center > Centrosome > Centriole.
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:9606188, PubMed:17229885, PubMed:21225229). 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). |
| Database Links: |
Entrez Gene: 6790?HumanEntrez Gene: 20878?MouseOmim: 603072?HumanSwissProt: O14965?HumanSwissProt: P97477?MouseUnigene: 250822?HumanUnigene: 249363?Mouse |
| Synonyms: |
AIK AntibodyARK-1 AntibodyARK1 AntibodyAURA AntibodyAurka AntibodyAurora 2 AntibodyAurora A AntibodyAurora kinase A AntibodyAurora-related kinase 1 AntibodyAurora/IPL1 like kinase AntibodyAurora/IPL1-related kinase 1 AntibodyAURORA2 AntibodyBreast tumor-amplified kinase AntibodyBTAK AntibodyhARK1 AntibodyIAK AntibodyIPL1 related kinase AntibodyMGC34538 AntibodyOTTHUMP00000031340 AntibodyOTTHUMP00000031341 AntibodyOTTHUMP00000031342 AntibodyOTTHUMP00000031343 AntibodyOTTHUMP00000031344 AntibodyOTTHUMP00000031345 AntibodyOTTHUMP00000166071 AntibodyOTTHUMP00000166072 AntibodyPPP1R47 AntibodyProtein phosphatase 1, regulatory subunit 47 AntibodySerine/threonine kinase 15 AntibodySerine/threonine kinase 6 AntibodySerine/threonine-protein kinase 15 AntibodySerine/threonine-protein kinase 6 AntibodySerine/threonine-protein kinase aurora-A AntibodySTK15 AntibodySTK6 AntibodySTK6_HUMAN AntibodySTK7 Antibody |
| Information: |
Target information shown above is from the UniProt Consortium. |
