Recombinant human Aurora A protein
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(1 Publication)
Recombinant human Aurora A protein is a Human Full Length protein, in the 2 to 403 aa range, expressed in Baculovirus infected Sf9 cells, with >90%, suitable for Inhib, FuncS.
View Alternative Names
AIK, AIRK1, ARK1, AURA, AYK1, BTAK, IAK1, STK15, STK6, AURKA, Aurora kinase A, Aurora 2, Aurora/IPL1-related kinase 1, Breast tumor-amplified kinase, Ipl1- and aurora-related kinase 1, Serine/threonine-protein kinase 15, Serine/threonine-protein kinase 6, Serine/threonine-protein kinase Ayk1, Serine/threonine-protein kinase aurora-A, ARK-1, Aurora-related kinase 1
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Aurora A plays key roles in the regulation of the cell cycle and mitosis. It functions as part of the Aurora mouse kinase complex associating with other proteins to ensure accurate chromosomal segregation and cytokinesis. Aurora A is involved in centrosome dynamics and interacts with proteins such as 35C1 aiding its localization to the correct cellular structures. The protein’s role in the cell cycle and mitotic checkpoints makes it a subject of interest for researchers examining cancer proliferation.
Pathways
Aurora A integrates into both the mitotic spindle assembly checkpoint and DNA damage repair pathways. Within these pathways Aurora A partners with proteins like APC (Anaphase Promoting Complex) to ensure timely progression through mitosis and safeguard genomic stability. The spindle assembly pathway ensures that spindle fibers correctly attach to chromosomes a process in which Aurora A proves instrumental. Its interaction with other kinases and regulatory molecules in these pathways highlights its regulatory importance in cell proliferation.
Specifications
Form
Liquid
Additional notes
Affinity purified.
General info
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). 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).
Sequence similarities
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily.
Post-translational modifications
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.. 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).
Subcellular localisation
Cytoskeleton
Target data
Publications (1)
Recent publications for all applications. Explore the full list and refine your search
Nature communications 15:10782 PubMed39737931
2024
Applications
Unspecified application
Species
Unspecified reactive species
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