AURKA (Aurora kinase A) is a mitotic serine/threonine kinase concentrated at centrosomes and spindle-pole microtubules from late G2 to anaphase. Activated by autophosphorylation in its activation loop and by cofactors such as TPX2, BORA and Ajuba, it drives centrosome maturation and separation, bipolar spindle assembly, and mitotic entry. Among other routes, it initiates CDK1 activation at centrosomes and activates PLK1. It phosphorylates many substrates, including TPX2, TACC3, NDEL1, CDC25B, BRCA1, p53 and HURP. Outside mitosis it acts at the ciliary basal body, where NEDD9-activated AURKA phosphorylates HDAC6 to disassemble the primary cilium, and it phosphorylates RALA to promote mitotic mitochondrial fission. AURKA is frequently amplified and overexpressed in cancers.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000086 G2/M transition of mitotic cell cycle | TAS Reactome:R-HSA-69275 | ACCEPT | Summary: G2/M transition of mitotic cell cycle (TAS). AURKA contributes to mitotic progression, initiating CDK1 activation at centrosomes and acting through many mitotic substrates. Core process. Reactome event: 'G2/M Transition'. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the"] [file:human/AURKA/AURKA-uniprot.txt "CC CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates"] [file:human/AURKA/AURKA-uniprot.txt "CC centrosome separation as well as maturation, chromosomal alignment,"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the file:human/AURKA/AURKA-uniprot.txt CC CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates file:human/AURKA/AURKA-uniprot.txt CC centrosome separation as well as maturation, chromosomal alignment, |
| GO:0000212 meiotic spindle organization | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: Meiotic spindle organization (IEA). In mouse oocytes, AURKA inhibition with MLN8237 shortens the meiotic spindle and disrupts acentriolar MTOC organization. AURKA activity is therefore needed for meiotic spindle-pole focusing. This is mammalian ortholog evidence, and the mitotic roles remain the core ones, so it is kept as non-core. Reason: [PMID:31895686 "Taken together, our current data reveal a critical role for AURKA activity in regulating microtubule dynamics, spindle pole focusing, and the maintenance of oocyte aMTOC organization at assembled meiotic spindles."] [PMID:31895686 "MI oocytes treated with MLN8237 showed similar alterations, exhibiting significantly shorter spindles with highly focused poles, as well as loss of aMTOC organization with bright CEP215 and increased chromosome misalignment (Supplemental Fig. 1)."] Supporting Evidence: PMID:31895686 Taken together, our current data reveal a critical role for AURKA activity in regulating microtubule dynamics, spindle pole focusing, and the maintenance of oocyte aMTOC organization at assembled meiotic spindles. PMID:31895686 MI oocytes treated with MLN8237 showed similar alterations, exhibiting significantly shorter spindles with highly focused poles, as well as loss of aMTOC organization with bright CEP215 and increased chromosome misalignment (Supplemental Fig. 1). |
| GO:0000226 microtubule cytoskeleton organization | IEA GO_REF:0000002 | ACCEPT | Summary: Microtubule cytoskeleton organization (IEA). AURKA drives mitotic spindle assembly, centrosome maturation and separation, and spindle-pole organization. Core process. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC the establishment of mitotic spindle, centrosome duplication,"] [file:human/AURKA/AURKA-uniprot.txt "CC centrosome separation as well as maturation, chromosomal alignment,"] [file:human/AURKA/AURKA-uniprot.txt "CC Associates with the centrosome and the spindle microtubules during"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC the establishment of mitotic spindle, centrosome duplication, file:human/AURKA/AURKA-uniprot.txt CC centrosome separation as well as maturation, chromosomal alignment, file:human/AURKA/AURKA-uniprot.txt CC Associates with the centrosome and the spindle microtubules during |
| GO:0000278 mitotic cell cycle | IEA GO_REF:0000002 | ACCEPT | Summary: Mitotic cell cycle (IEA). AURKA contributes to mitotic progression, initiating CDK1 activation at centrosomes and acting through many mitotic substrates. Core process. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the"] [file:human/AURKA/AURKA-uniprot.txt "CC CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates"] [file:human/AURKA/AURKA-uniprot.txt "CC centrosome separation as well as maturation, chromosomal alignment,"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the file:human/AURKA/AURKA-uniprot.txt CC CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates file:human/AURKA/AURKA-uniprot.txt CC centrosome separation as well as maturation, chromosomal alignment, |
| GO:0000278 mitotic cell cycle | TAS PMID:9153231 Cell cycle-dependent expression and spindle pole localizatio... | ACCEPT | Summary: Mitotic cell cycle (TAS). AURKA contributes to mitotic progression, initiating CDK1 activation at centrosomes and acting through many mitotic substrates. Core process. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the"] [file:human/AURKA/AURKA-uniprot.txt "CC CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates"] [file:human/AURKA/AURKA-uniprot.txt "CC centrosome separation as well as maturation, chromosomal alignment,"] [PMID:9153231 "In HeLa cells, the endogenous levels of aik mRNA and protein contents are tightly regulated during cell cycle progression."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the file:human/AURKA/AURKA-uniprot.txt CC CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates file:human/AURKA/AURKA-uniprot.txt CC centrosome separation as well as maturation, chromosomal alignment, PMID:9153231 In HeLa cells, the endogenous levels of aik mRNA and protein contents are tightly regulated during cell cycle progression. |
| GO:0000776 kinetochore | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Kinetochore (IBA). Inherited from the Aurora family node, where the kinetochore/centromere localization belongs to Aurora-B. AURKA's main sites are centrosomes and spindle poles. Kept as non-core. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC Associates with the centrosome and the spindle microtubules during"] [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000681968 SUPPORTS TRANSFER Aurora family node; the term reflects mainly Aurora-B biology, so it is kept as non-core for Aurora-A. Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC Associates with the centrosome and the spindle microtubules during file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing |
| GO:0000922 spindle pole | IBA GO_REF:0000033 | ACCEPT | Summary: Spindle pole (IBA). AURKA concentrates at centrosomes from early prophase to telophase and on spindle-pole microtubules from prophase to anaphase. Core location. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] [file:human/AURKA/AURKA-uniprot.txt "CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638,"] [file:human/AURKA/AURKA-uniprot.txt "CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885,"] Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000681968 SUPPORTS TRANSFER Aurora family node; conserved Aurora-A function, with human AURKA among the experimentally annotated members. Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing file:human/AURKA/AURKA-uniprot.txt CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638, file:human/AURKA/AURKA-uniprot.txt CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885, |
| GO:0000922 spindle pole | IEA GO_REF:0000044 | ACCEPT | Summary: Spindle pole (IEA). AURKA concentrates at centrosomes from early prophase to telophase and on spindle-pole microtubules from prophase to anaphase. Core location. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] [file:human/AURKA/AURKA-uniprot.txt "CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638,"] [file:human/AURKA/AURKA-uniprot.txt "CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885,"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing file:human/AURKA/AURKA-uniprot.txt CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638, file:human/AURKA/AURKA-uniprot.txt CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885, |
| GO:0004672 protein kinase activity | IDA PMID:14580337 Structural basis of Aurora-A activation by TPX2 at the mitot... | ACCEPT | Summary: Protein kinase activity (IDA). AURKA is a mitotic serine/threonine kinase with demonstrated serine and threonine phosphotransferase activity on many substrates. Core function. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +"] [file:human/AURKA/AURKA-uniprot.txt "CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B,"] [PMID:14580337 "It is activated by phosphorylation and by the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + file:human/AURKA/AURKA-uniprot.txt CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, PMID:14580337 It is activated by phosphorylation and by the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. |
| GO:0004672 protein kinase activity | IDA PMID:19801554 A cancer-associated aurora A mutant is mislocalized and misr... | ACCEPT | Summary: Protein kinase activity (IDA). AURKA is a mitotic serine/threonine kinase with demonstrated serine and threonine phosphotransferase activity on many substrates. Core function. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +"] [file:human/AURKA/AURKA-uniprot.txt "CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B,"] [PMID:19801554 "In this study we show that Aurora A kinase activity is altered in different ways in three somatic cancer-associated mutations located within the catalytic domain; Aurora A(V174M) shows constitutively increased kinase activity, Aurora A(S155R) activity is decreased primarily due to misregulation, and Aurora A(S361*) activity is ablated due to loss of structural integrity."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + file:human/AURKA/AURKA-uniprot.txt CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, PMID:19801554 In this study we show that Aurora A kinase activity is altered in different ways in three somatic cancer-associated mutations located within the catalytic domain; Aurora A(V174M) shows constitutively increased kinase activity, Aurora A(S155R) activity is decreased primarily due to misregulation, and Aurora A(S361*) activity is ablated due to loss of structural integrity. |
| GO:0004672 protein kinase activity | IDA PMID:21600873 Identification of Ski as a target for Aurora A kinase. | ACCEPT | Summary: Protein kinase activity (IDA). AURKA is a mitotic serine/threonine kinase with demonstrated serine and threonine phosphotransferase activity on many substrates. Core function. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +"] [file:human/AURKA/AURKA-uniprot.txt "CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B,"] [PMID:21600873 "Here, we show that Aurora A kinase is able to phosphorylate Ski in vitro."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + file:human/AURKA/AURKA-uniprot.txt CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, PMID:21600873 Here, we show that Aurora A kinase is able to phosphorylate Ski in vitro. |
| GO:0004672 protein kinase activity | IEA GO_REF:0000002 | ACCEPT | Summary: Protein kinase activity (IEA). AURKA is a mitotic serine/threonine kinase with demonstrated serine and threonine phosphotransferase activity on many substrates. Core function. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +"] [file:human/AURKA/AURKA-uniprot.txt "CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B,"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + file:human/AURKA/AURKA-uniprot.txt CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, |
| GO:0004674 protein serine/threonine kinase activity | EXP PMID:13678582 Aurora-A and an interacting activator, the LIM protein Ajuba... | ACCEPT | Summary: Protein serine/threonine kinase activity (EXP). AURKA is a mitotic serine/threonine kinase with demonstrated serine and threonine phosphotransferase activity on many substrates. Core function. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +"] [file:human/AURKA/AURKA-uniprot.txt "CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B,"] [PMID:13678582 "In vitro analyses revealed that Ajuba induces the autophosphorylation and consequent activation of Aurora-A."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + file:human/AURKA/AURKA-uniprot.txt CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, PMID:13678582 In vitro analyses revealed that Ajuba induces the autophosphorylation and consequent activation of Aurora-A. |
| GO:0004674 protein serine/threonine kinase activity | EXP PMID:18566290 Bora and the kinase Aurora a cooperatively activate the kina... | ACCEPT | Summary: Protein serine/threonine kinase activity (EXP). AURKA is a mitotic serine/threonine kinase with demonstrated serine and threonine phosphotransferase activity on many substrates. Core function. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +"] [file:human/AURKA/AURKA-uniprot.txt "CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B,"] [PMID:18566290 "Mechanistically, Bora interacts with Plk1 and controls the accessibility of its activation loop for phosphorylation and activation by Aur-A."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + file:human/AURKA/AURKA-uniprot.txt CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, PMID:18566290 Mechanistically, Bora interacts with Plk1 and controls the accessibility of its activation loop for phosphorylation and activation by Aur-A. |
| GO:0004674 protein serine/threonine kinase activity | EXP PMID:21807936 PHLDA1 is a crucial negative regulator and effector of Auror... | ACCEPT | Summary: Protein serine/threonine kinase activity (EXP). AURKA is a mitotic serine/threonine kinase with demonstrated serine and threonine phosphotransferase activity on many substrates. Core function. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +"] [file:human/AURKA/AURKA-uniprot.txt "CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B,"] [PMID:21807936 "A chemical genetic approach was used to identify the malignant targets of Aurora A, which revealed pleckstrin-homology-like domain protein PHLDA1 as an Aurora A substrate."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + file:human/AURKA/AURKA-uniprot.txt CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, PMID:21807936 A chemical genetic approach was used to identify the malignant targets of Aurora A, which revealed pleckstrin-homology-like domain protein PHLDA1 as an Aurora A substrate. |
| GO:0004674 protein serine/threonine kinase activity | IEA GO_REF:0000003 | ACCEPT | Summary: Protein serine/threonine kinase activity (IEA). AURKA is a mitotic serine/threonine kinase with demonstrated serine and threonine phosphotransferase activity on many substrates. Core function. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +"] [file:human/AURKA/AURKA-uniprot.txt "CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B,"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + file:human/AURKA/AURKA-uniprot.txt CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, |
| GO:0004674 protein serine/threonine kinase activity | IMP PMID:28218735 Aurora kinase A regulates Survivin stability through targeti... | ACCEPT | Summary: Protein serine/threonine kinase activity (IMP). AURKA is a mitotic serine/threonine kinase with demonstrated serine and threonine phosphotransferase activity on many substrates. Core function. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +"] [file:human/AURKA/AURKA-uniprot.txt "CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B,"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + file:human/AURKA/AURKA-uniprot.txt CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, |
| GO:0004674 protein serine/threonine kinase activity | TAS Reactome:R-HSA-8853419 | ACCEPT | Summary: Protein serine/threonine kinase activity (TAS). AURKA is a mitotic serine/threonine kinase with demonstrated serine and threonine phosphotransferase activity on many substrates. Core function. Reactome event: 'TPX2 promotes AURKA autophosphorylation'. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +"] [file:human/AURKA/AURKA-uniprot.txt "CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B,"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + file:human/AURKA/AURKA-uniprot.txt CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, |
| GO:0004712 protein serine/threonine/tyrosine kinase activity | IEA GO_REF:0000117 | MODIFY | Summary: Protein serine/threonine/tyrosine kinase activity (IEA). AURKA is a serine/threonine kinase: UniProt records serine and threonine phosphotransferase reactions only, and no tyrosine kinase activity is reported. The dual-specificity term overstates it. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +"] [file:human/AURKA/AURKA-uniprot.txt "CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the"] Proposed replacements: protein serine/threonine kinase activity Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + file:human/AURKA/AURKA-uniprot.txt CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the |
| GO:0004712 protein serine/threonine/tyrosine kinase activity | TAS PMID:19774610 Aurora A, centrosome structure, and the centrosome cycle. | MODIFY | Summary: Protein serine/threonine/tyrosine kinase activity (TAS). AURKA is a serine/threonine kinase: UniProt records serine and threonine phosphotransferase reactions only, and no tyrosine kinase activity is reported. The dual-specificity term overstates it. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +"] [file:human/AURKA/AURKA-uniprot.txt "CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the"] [PMID:19774610 "The aurora kinases A, B, and C are serine/threonine kinases that are active during mitosis."] Proposed replacements: protein serine/threonine kinase activity Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + file:human/AURKA/AURKA-uniprot.txt CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the PMID:19774610 The aurora kinases A, B, and C are serine/threonine kinases that are active during mitosis. |
| GO:0005515 protein binding | IPI PMID:12244051 Aurora-A kinase interacting protein (AIP), a novel negative ... | REMOVE | Summary: Protein binding (IPI) with AURKAIP1. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:14580337 Structural basis of Aurora-A activation by TPX2 at the mitot... | REMOVE | Summary: Protein binding (IPI) with TPX2. TPX2 is AURKA's spindle activator and targeting factor; activation is captured by the kinase and spindle terms. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:15987997 Phosphorylation and stabilization of HURP by Aurora-A: impli... | REMOVE | Summary: Protein binding (IPI) with DLGAP5. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:16890155 Mitotic activation of the kinase Aurora-A requires its bindi... | REMOVE | Summary: Protein binding (IPI) with BORA. BORA is an AURKA substrate and cofactor for PLK1 activation. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:17604723 HEF1-dependent Aurora A activation induces disassembly of th... | REMOVE | Summary: Protein binding (IPI) with HDAC6. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:17726514 Interphase nucleo-cytoplasmic shuttling and localization of ... | REMOVE | Summary: Protein binding (IPI) with SIRT2. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:17939994 A role for IkappaB kinase 2 in bipolar spindle assembly. | MODIFY | Summary: Protein binding (IPI) with IKBKB (IKK2). IKK2 antagonizes Aurora-A signalling in mitosis, and its depletion deregulates Aurora-A stability. The partner is a protein kinase, so protein kinase binding is the informative term, as for PLK1. Reason: [PMID:17939994 "These data support a function for IKK2 as an antagonist of Aurora A signaling during mitosis."] [file:human/AURKA/AURKA-uniprot.txt "CC O14965; O14920: IKBKB; NbExp=2; IntAct=EBI-448680, EBI-81266;"] Proposed replacements: protein kinase binding Supporting Evidence: PMID:17939994 These data support a function for IKK2 as an antagonist of Aurora A signaling during mitosis. file:human/AURKA/AURKA-uniprot.txt CC O14965; O14920: IKBKB; NbExp=2; IntAct=EBI-448680, EBI-81266; |
| GO:0005515 protein binding | IPI PMID:18361916 Astrin regulates Aurora-A localization. | REMOVE | Summary: Protein binding (IPI) with SPAG5. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:18521620 Plk1 regulates mitotic Aurora A function through betaTrCP-de... | REMOVE | Summary: Protein binding (IPI) with BORA. BORA is an AURKA substrate and cofactor for PLK1 activation. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:18615013 Polo-like kinase-1 is activated by aurora A to promote check... | MODIFY | Summary: Protein binding (IPI) with PLK1. AURKA (with BORA) phosphorylates PLK1 to activate it. Protein kinase binding is the informative term. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3,"] Proposed replacements: protein kinase binding Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3, |
| GO:0005515 protein binding | IPI PMID:18615013 Polo-like kinase-1 is activated by aurora A to promote check... | REMOVE | Summary: Protein binding (IPI) with BORA. BORA is an AURKA substrate and cofactor for PLK1 activation. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:18662907 Modulation of kinase-inhibitor interactions by auxiliary pro... | REMOVE | Summary: Protein binding (IPI) with TPX2. TPX2 is AURKA's spindle activator and targeting factor; activation is captured by the kinase and spindle terms. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:18663142 Building a spindle of the correct length in human cells requ... | REMOVE | Summary: Protein binding (IPI) with Tpx2. TPX2 is AURKA's spindle activator and targeting factor; activation is captured by the kinase and spindle terms. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:19111882 Stabilization of N-Myc is a critical function of Aurora A in... | MODIFY | Summary: Protein binding (IPI) with MYCN (N-Myc). The AURKA catalytic domain binds a site flanking Myc Box I of N-Myc, independently of phosphorylation. This shields N-Myc from SCF-FBXW7 degradation in neuroblastoma, a function described as kinase-independent. N-Myc is a transcription factor, so transcription factor binding is the informative term; the stabilization output is captured by GO:0031647. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC MYCN; interaction is phospho-independent and triggers AURKA activation;"] [PMID:27837025 "However, N-Myc protein (the product of the MYCN oncogene) is stabilized in neuroblastoma by the protein kinase Aurora-A in a manner that is sensitive to certain Aurora-A-selective inhibitors."] [PMID:25175806 "Proteolytic degradation of MYCN protein is regulated in part by a kinase-independent function of Aurora A."] Proposed replacements: transcription factor binding Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC MYCN; interaction is phospho-independent and triggers AURKA activation; PMID:27837025 However, N-Myc protein (the product of the MYCN oncogene) is stabilized in neuroblastoma by the protein kinase Aurora-A in a manner that is sensitive to certain Aurora-A-selective inhibitors. PMID:25175806 Proteolytic degradation of MYCN protein is regulated in part by a kinase-independent function of Aurora A. |
| GO:0005515 protein binding | IPI PMID:19357306 A single amino acid change converts Aurora-A into Aurora-B-l... | REMOVE | Summary: Protein binding (IPI) with BIRC5. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:19357306 A single amino acid change converts Aurora-A into Aurora-B-l... | REMOVE | Summary: Protein binding (IPI) with INCENP. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:19357306 A single amino acid change converts Aurora-A into Aurora-B-l... | REMOVE | Summary: Protein binding (IPI) with INCENP. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:19357306 A single amino acid change converts Aurora-A into Aurora-B-l... | REMOVE | Summary: Protein binding (IPI) with TPX2. TPX2 is AURKA's spindle activator and targeting factor; activation is captured by the kinase and spindle terms. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:19801554 A cancer-associated aurora A mutant is mislocalized and misr... | REMOVE | Summary: Protein binding (IPI) with TPX2. TPX2 is AURKA's spindle activator and targeting factor; activation is captured by the kinase and spindle terms. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:20360068 Systematic analysis of human protein complexes identifies ch... | REMOVE | Summary: Protein binding (IPI) with TPX2. TPX2 is AURKA's spindle activator and targeting factor; activation is captured by the kinase and spindle terms. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:20460379 Solution structure of human growth arrest and DNA damage 45a... | REMOVE | Summary: Protein binding (IPI) with GADD45A. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:20596670 Functional characterization of AIBp, a novel Aurora-A bindin... | REMOVE | Summary: Protein binding (IPI) with AUNIP. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:20643351 Pitchfork regulates primary cilia disassembly and left-right... | REMOVE | Summary: Protein binding (IPI) with CIMAP3. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:20643351 Pitchfork regulates primary cilia disassembly and left-right... | REMOVE | Summary: Protein binding (IPI) with Cimap3. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:21242313 The nuclear scaffold protein SAF-A is required for kinetocho... | REMOVE | Summary: Protein binding (IPI) with HNRNPU. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:21821029 Aurora-A phosphorylates hnRNPK and disrupts its interaction ... | REMOVE | Summary: Protein binding (IPI) with HNRNPK. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:22014574 SIRT2 maintains genome integrity and suppresses tumorigenesi... | REMOVE | Summary: Protein binding (IPI) with Sirt2. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:22110403 Interplay between BRCA1 and RHAMM regulates epithelial apico... | REMOVE | Summary: Protein binding (IPI) with TPX2. TPX2 is AURKA's spindle activator and targeting factor; activation is captured by the kinase and spindle terms. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:22305495 Protein tyrosine phosphatase receptor delta acts as a neurob... | REMOVE | Summary: Protein binding (IPI) with PTPRD. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:22306998 Novel E3 ligase component FBXL7 ubiquitinates and degrades A... | REMOVE | Summary: Protein binding (IPI) with Fbxl7. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:22340593 Aurora kinase-A inactivates DNA damage-induced apoptosis and... | REMOVE | Summary: Protein binding (IPI) with TP73. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:23213400 The CUL3-KLHL18 ligase regulates mitotic entry and ubiquityl... | REMOVE | Summary: Protein binding (IPI) with KLHL18. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:23213400 The CUL3-KLHL18 ligase regulates mitotic entry and ubiquityl... | REMOVE | Summary: Protein binding (IPI) with CUL3. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:23520446 Protein phosphorylation profiling using an in situ proximity... | REMOVE | Summary: Protein binding (IPI) with EGFR. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:23792191 Small molecule inhibitors of aurora-a induce proteasomal deg... | MODIFY | Summary: Protein binding (IPI) with MYCN (N-Myc). The AURKA catalytic domain binds a site flanking Myc Box I of N-Myc, independently of phosphorylation. This shields N-Myc from SCF-FBXW7 degradation in neuroblastoma, a function described as kinase-independent. N-Myc is a transcription factor, so transcription factor binding is the informative term; the stabilization output is captured by GO:0031647. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC MYCN; interaction is phospho-independent and triggers AURKA activation;"] [PMID:27837025 "However, N-Myc protein (the product of the MYCN oncogene) is stabilized in neuroblastoma by the protein kinase Aurora-A in a manner that is sensitive to certain Aurora-A-selective inhibitors."] [PMID:25175806 "Proteolytic degradation of MYCN protein is regulated in part by a kinase-independent function of Aurora A."] Proposed replacements: transcription factor binding Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC MYCN; interaction is phospho-independent and triggers AURKA activation; PMID:27837025 However, N-Myc protein (the product of the MYCN oncogene) is stabilized in neuroblastoma by the protein kinase Aurora-A in a manner that is sensitive to certain Aurora-A-selective inhibitors. PMID:25175806 Proteolytic degradation of MYCN protein is regulated in part by a kinase-independent function of Aurora A. |
| GO:0005515 protein binding | IPI PMID:24574519 NEDD9 regulates actin dynamics through cortactin deacetylati... | REMOVE | Summary: Protein binding (IPI) with CTTN and NEDD9. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:24857377 Phosphorylation of multifunctional nucleolar protein nucleop... | REMOVE | Summary: Protein binding (IPI) with NPM1. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:24996188 Depletion of IK causes mitotic arrest through aberrant regul... | REMOVE | Summary: Protein binding (IPI) with IK. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:25175806 Drugging MYCN through an allosteric transition in Aurora kin... | MODIFY | Summary: Protein binding (IPI) with MYCN (N-Myc). The AURKA catalytic domain binds a site flanking Myc Box I of N-Myc, independently of phosphorylation. This shields N-Myc from SCF-FBXW7 degradation in neuroblastoma, a function described as kinase-independent. N-Myc is a transcription factor, so transcription factor binding is the informative term; the stabilization output is captured by GO:0031647. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC MYCN; interaction is phospho-independent and triggers AURKA activation;"] [PMID:27837025 "However, N-Myc protein (the product of the MYCN oncogene) is stabilized in neuroblastoma by the protein kinase Aurora-A in a manner that is sensitive to certain Aurora-A-selective inhibitors."] [PMID:25175806 "Proteolytic degradation of MYCN protein is regulated in part by a kinase-independent function of Aurora A."] Proposed replacements: transcription factor binding Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC MYCN; interaction is phospho-independent and triggers AURKA activation; PMID:27837025 However, N-Myc protein (the product of the MYCN oncogene) is stabilized in neuroblastoma by the protein kinase Aurora-A in a manner that is sensitive to certain Aurora-A-selective inhibitors. PMID:25175806 Proteolytic degradation of MYCN protein is regulated in part by a kinase-independent function of Aurora A. |
| GO:0005515 protein binding | IPI PMID:25986610 Phosphorylation of SAF-A/hnRNP-U Serine 59 by Polo-Like Kina... | REMOVE | Summary: Protein binding (IPI) with HNRNPU. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:27728805 N-Myc Induces an EZH2-Mediated Transcriptional Program Drivi... | MODIFY | Summary: Protein binding (IPI) with MYCN (N-Myc). The AURKA catalytic domain binds a site flanking Myc Box I of N-Myc, independently of phosphorylation. This shields N-Myc from SCF-FBXW7 degradation in neuroblastoma, a function described as kinase-independent. N-Myc is a transcription factor, so transcription factor binding is the informative term; the stabilization output is captured by GO:0031647. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC MYCN; interaction is phospho-independent and triggers AURKA activation;"] [PMID:27837025 "However, N-Myc protein (the product of the MYCN oncogene) is stabilized in neuroblastoma by the protein kinase Aurora-A in a manner that is sensitive to certain Aurora-A-selective inhibitors."] [PMID:25175806 "Proteolytic degradation of MYCN protein is regulated in part by a kinase-independent function of Aurora A."] Proposed replacements: transcription factor binding Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC MYCN; interaction is phospho-independent and triggers AURKA activation; PMID:27837025 However, N-Myc protein (the product of the MYCN oncogene) is stabilized in neuroblastoma by the protein kinase Aurora-A in a manner that is sensitive to certain Aurora-A-selective inhibitors. PMID:25175806 Proteolytic degradation of MYCN protein is regulated in part by a kinase-independent function of Aurora A. |
| GO:0005515 protein binding | IPI PMID:27837025 Structural basis of N-Myc binding by Aurora-A and its destab... | MODIFY | Summary: Protein binding (IPI) with MYCN (N-Myc). The AURKA catalytic domain binds a site flanking Myc Box I of N-Myc, independently of phosphorylation. This shields N-Myc from SCF-FBXW7 degradation in neuroblastoma, a function described as kinase-independent. N-Myc is a transcription factor, so transcription factor binding is the informative term; the stabilization output is captured by GO:0031647. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC MYCN; interaction is phospho-independent and triggers AURKA activation;"] [PMID:27837025 "Here we identify a direct interaction between the catalytic domain of Aurora-A and a site flanking Myc Box I that also binds SCFFbxW7 We determined the crystal structure of the complex between Aurora-A and this region of N-Myc to 1.72-Γ
resolution."] [PMID:25175806 "Proteolytic degradation of MYCN protein is regulated in part by a kinase-independent function of Aurora A."] Proposed replacements: transcription factor binding Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC MYCN; interaction is phospho-independent and triggers AURKA activation; PMID:27837025 Here we identify a direct interaction between the catalytic domain of Aurora-A and a site flanking Myc Box I that also binds SCFFbxW7 We determined the crystal structure of the complex between Aurora-A and this region of N-Myc to 1.72-Γ
resolution. PMID:25175806 Proteolytic degradation of MYCN protein is regulated in part by a kinase-independent function of Aurora A. |
| GO:0005515 protein binding | IPI PMID:27837025 Structural basis of N-Myc binding by Aurora-A and its destab... | REMOVE | Summary: Protein binding (IPI) with TPX2. TPX2 is AURKA's spindle activator and targeting factor; activation is captured by the kinase and spindle terms. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:28218735 Aurora kinase A regulates Survivin stability through targeti... | REMOVE | Summary: Protein binding (IPI) with FOXP1. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Protein binding (IPI) with TPX2. TPX2 is AURKA's spindle activator and targeting factor; activation is captured by the kinase and spindle terms. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Protein binding (IPI) with TPX2. TPX2 is AURKA's spindle activator and targeting factor; activation is captured by the kinase and spindle terms. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | REMOVE | Summary: Protein binding (IPI) with EGFR. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | REMOVE | Summary: Protein binding (IPI) with BRAF. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:38729556 SOX9 is regulated by AURKA in response to Helicobacter pylor... | REMOVE | Summary: Protein binding (IPI) with EIF4E. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | ACCEPT | Summary: ATP binding (IEA). ATP binding: AURKA is an active protein kinase (Rhea Ser/Thr phosphotransfer reactions); its catalytic domain has also been crystallized with adenosine bound in the ATP site. Accepted. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +"] [PMID:12237287 "We report the first crystal structure of Aurora-2 kinase in complex with adenosine."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + PMID:12237287 We report the first crystal structure of Aurora-2 kinase in complex with adenosine. |
| GO:0005634 nucleus | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Nucleus (IBA). A nuclear pool of AURKA exists. In breast cancer cells, nuclear AURKA binds hnRNP K and transactivates the MYC promoter independently of its kinase activity. Its core sites are the centrosome and spindle, so this is kept as non-core. Reason: [PMID:26782714 "Instead, AURKA preferentially interacts with heterogeneous nuclear ribonucleoprotein K (hnRNP K) in the nucleus and acts as a transcription factor in a complex that induces a shift in MYC promoter usage and activates the MYC promoter."] [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000681967 SUPPORTS TRANSFER Aurora family node; the term reflects mainly Aurora-B biology, so it is kept as non-core for Aurora-A. Supporting Evidence: PMID:26782714 Instead, AURKA preferentially interacts with heterogeneous nuclear ribonucleoprotein K (hnRNP K) in the nucleus and acts as a transcription factor in a complex that induces a shift in MYC promoter usage and activates the MYC promoter. file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing |
| GO:0005634 nucleus | IDA PMID:20531406 A human B-cell interactome identifies MYB and FOXM1 as maste... | KEEP AS NON CORE | Summary: Nucleus (IDA). A nuclear pool of AURKA exists. In breast cancer cells, nuclear AURKA binds hnRNP K and transactivates the MYC promoter independently of its kinase activity. Its core sites are the centrosome and spindle, so this is kept as non-core. Reason: [PMID:26782714 "Instead, AURKA preferentially interacts with heterogeneous nuclear ribonucleoprotein K (hnRNP K) in the nucleus and acts as a transcription factor in a complex that induces a shift in MYC promoter usage and activates the MYC promoter."] [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] [PMID:20531406 "High-resolution confocal imaging showed that these proteins are co-localized either in the nucleus or perinuclearly (Figure 6C)."] Supporting Evidence: PMID:26782714 Instead, AURKA preferentially interacts with heterogeneous nuclear ribonucleoprotein K (hnRNP K) in the nucleus and acts as a transcription factor in a complex that induces a shift in MYC promoter usage and activates the MYC promoter. file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing PMID:20531406 High-resolution confocal imaging showed that these proteins are co-localized either in the nucleus or perinuclearly (Figure 6C). |
| GO:0005634 nucleus | TAS PMID:9153231 Cell cycle-dependent expression and spindle pole localizatio... | KEEP AS NON CORE | Summary: Nucleus (TAS). A nuclear pool of AURKA exists. In breast cancer cells, nuclear AURKA binds hnRNP K and transactivates the MYC promoter independently of its kinase activity. Its core sites are the centrosome and spindle, so this is kept as non-core. Reason: [PMID:26782714 "Instead, AURKA preferentially interacts with heterogeneous nuclear ribonucleoprotein K (hnRNP K) in the nucleus and acts as a transcription factor in a complex that induces a shift in MYC promoter usage and activates the MYC promoter."] [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] Supporting Evidence: PMID:26782714 Instead, AURKA preferentially interacts with heterogeneous nuclear ribonucleoprotein K (hnRNP K) in the nucleus and acts as a transcription factor in a complex that induces a shift in MYC promoter usage and activates the MYC promoter. file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6791235 | KEEP AS NON CORE | Summary: Nucleoplasm (TAS). A nucleoplasmic pool of AURKA exists. In breast cancer cells, nuclear AURKA binds hnRNP K and transactivates the MYC promoter independently of its kinase activity. Its core sites are the centrosome and spindle, so this is kept as non-core. Reactome event: 'GADD45A binds AURKA'. Reason: [PMID:26782714 "Instead, AURKA preferentially interacts with heterogeneous nuclear ribonucleoprotein K (hnRNP K) in the nucleus and acts as a transcription factor in a complex that induces a shift in MYC promoter usage and activates the MYC promoter."] [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] Supporting Evidence: PMID:26782714 Instead, AURKA preferentially interacts with heterogeneous nuclear ribonucleoprotein K (hnRNP K) in the nucleus and acts as a transcription factor in a complex that induces a shift in MYC promoter usage and activates the MYC promoter. file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6805103 | KEEP AS NON CORE | Summary: Nucleoplasm (TAS). A nucleoplasmic pool of AURKA exists. In breast cancer cells, nuclear AURKA binds hnRNP K and transactivates the MYC promoter independently of its kinase activity. Its core sites are the centrosome and spindle, so this is kept as non-core. Reactome event: 'AURKA phosphorylates TP53'. Reason: [PMID:26782714 "Instead, AURKA preferentially interacts with heterogeneous nuclear ribonucleoprotein K (hnRNP K) in the nucleus and acts as a transcription factor in a complex that induces a shift in MYC promoter usage and activates the MYC promoter."] [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] Supporting Evidence: PMID:26782714 Instead, AURKA preferentially interacts with heterogeneous nuclear ribonucleoprotein K (hnRNP K) in the nucleus and acts as a transcription factor in a complex that induces a shift in MYC promoter usage and activates the MYC promoter. file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing |
| GO:0005813 centrosome | IBA GO_REF:0000033 | ACCEPT | Summary: Centrosome (IBA). AURKA concentrates at centrosomes from early prophase to telophase and on spindle-pole microtubules from prophase to anaphase. Core location. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] [file:human/AURKA/AURKA-uniprot.txt "CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638,"] [file:human/AURKA/AURKA-uniprot.txt "CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885,"] Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN001219008 SUPPORTS TRANSFER Aurora family node; conserved Aurora-A function, with human AURKA among the experimentally annotated members. Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing file:human/AURKA/AURKA-uniprot.txt CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638, file:human/AURKA/AURKA-uniprot.txt CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885, |
| GO:0005813 centrosome | IDA GO_REF:0000052 | ACCEPT | Summary: Centrosome (IDA). AURKA concentrates at centrosomes from early prophase to telophase and on spindle-pole microtubules from prophase to anaphase. Core location. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] [file:human/AURKA/AURKA-uniprot.txt "CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638,"] [file:human/AURKA/AURKA-uniprot.txt "CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885,"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing file:human/AURKA/AURKA-uniprot.txt CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638, file:human/AURKA/AURKA-uniprot.txt CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885, |
| GO:0005813 centrosome | IDA PMID:17726514 Interphase nucleo-cytoplasmic shuttling and localization of ... | ACCEPT | Summary: Centrosome (IDA). AURKA concentrates at centrosomes from early prophase to telophase and on spindle-pole microtubules from prophase to anaphase. Core location. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] [file:human/AURKA/AURKA-uniprot.txt "CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638,"] [file:human/AURKA/AURKA-uniprot.txt "CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885,"] [PMID:17726514 "During early prophase, endogenous SIRT2 became enriched at the centrosome demonstrated by its colocalization with Aurora A, a mitotic regulatory kinase also found on the centrosomes (Figure 4B and C) [35]."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing file:human/AURKA/AURKA-uniprot.txt CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638, file:human/AURKA/AURKA-uniprot.txt CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885, PMID:17726514 During early prophase, endogenous SIRT2 became enriched at the centrosome demonstrated by its colocalization with Aurora A, a mitotic regulatory kinase also found on the centrosomes (Figure 4B and C) [35]. |
| GO:0005813 centrosome | IDA PMID:21399614 Novel asymmetrically localizing components of human centroso... | ACCEPT | Summary: Centrosome (IDA). AURKA concentrates at centrosomes from early prophase to telophase and on spindle-pole microtubules from prophase to anaphase. Core location. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] [file:human/AURKA/AURKA-uniprot.txt "CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638,"] [file:human/AURKA/AURKA-uniprot.txt "CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885,"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing file:human/AURKA/AURKA-uniprot.txt CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638, file:human/AURKA/AURKA-uniprot.txt CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885, |
| GO:0005813 centrosome | IDA PMID:21600873 Identification of Ski as a target for Aurora A kinase. | ACCEPT | Summary: Centrosome (IDA). AURKA concentrates at centrosomes from early prophase to telophase and on spindle-pole microtubules from prophase to anaphase. Core location. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] [file:human/AURKA/AURKA-uniprot.txt "CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638,"] [file:human/AURKA/AURKA-uniprot.txt "CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885,"] [PMID:21600873 "In vivo, Aurora A and Ski co-localized at the centrosomes and co-immunoprecipitated."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing file:human/AURKA/AURKA-uniprot.txt CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638, file:human/AURKA/AURKA-uniprot.txt CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885, PMID:21600873 In vivo, Aurora A and Ski co-localized at the centrosomes and co-immunoprecipitated. |
| GO:0005813 centrosome | IDA PMID:23213400 The CUL3-KLHL18 ligase regulates mitotic entry and ubiquityl... | ACCEPT | Summary: Centrosome (IDA). AURKA concentrates at centrosomes from early prophase to telophase and on spindle-pole microtubules from prophase to anaphase. Core location. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] [file:human/AURKA/AURKA-uniprot.txt "CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638,"] [file:human/AURKA/AURKA-uniprot.txt "CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885,"] [PMID:23213400 "Aurora-A localizes at the centrosome and activates Plk1 with Bora, leading to the activation of Cdk1 and in turn mitotic entry (Hirota et al., 2003; Macurek et al., 2008; Seki et al., 2008)."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing file:human/AURKA/AURKA-uniprot.txt CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638, file:human/AURKA/AURKA-uniprot.txt CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885, PMID:23213400 Aurora-A localizes at the centrosome and activates Plk1 with Bora, leading to the activation of Cdk1 and in turn mitotic entry (Hirota et al., 2003; Macurek et al., 2008; Seki et al., 2008). |
| GO:0005813 centrosome | IDA PMID:25657325 CENP-32 is required to maintain centrosomal dominance in bip... | ACCEPT | Summary: Centrosome (IDA). AURKA concentrates at centrosomes from early prophase to telophase and on spindle-pole microtubules from prophase to anaphase. Core location. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] [file:human/AURKA/AURKA-uniprot.txt "CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638,"] [file:human/AURKA/AURKA-uniprot.txt "CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885,"] [PMID:25657325 "Compared to control cells, CENP-32 siRNA cells exhibited a weaker (but still positive) staining of Aurora A on the detached centrosomes and a stronger diffuse signal on spindle microtubules (Figure 2, A and E)."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing file:human/AURKA/AURKA-uniprot.txt CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638, file:human/AURKA/AURKA-uniprot.txt CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885, PMID:25657325 Compared to control cells, CENP-32 siRNA cells exhibited a weaker (but still positive) staining of Aurora A on the detached centrosomes and a stronger diffuse signal on spindle microtubules (Figure 2, A and E). |
| GO:0005813 centrosome | IDA PMID:30538148 Human nuclear RNAi-defective 2 (NRDE2) is an essential RNA s... | ACCEPT | Summary: Centrosome (IDA). AURKA concentrates at centrosomes from early prophase to telophase and on spindle-pole microtubules from prophase to anaphase. Core location. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] [file:human/AURKA/AURKA-uniprot.txt "CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638,"] [file:human/AURKA/AURKA-uniprot.txt "CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885,"] [PMID:30538148 "Second, we confirmed that the centrosomal localization of both active AURKA (Fig. 5B) and total AURKA (Supplemental Fig. 10A) was similarly reduced."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing file:human/AURKA/AURKA-uniprot.txt CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638, file:human/AURKA/AURKA-uniprot.txt CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885, PMID:30538148 Second, we confirmed that the centrosomal localization of both active AURKA (Fig. 5B) and total AURKA (Supplemental Fig. 10A) was similarly reduced. |
| GO:0005813 centrosome | IEA GO_REF:0000044 | ACCEPT | Summary: Centrosome (IEA). AURKA concentrates at centrosomes from early prophase to telophase and on spindle-pole microtubules from prophase to anaphase. Core location. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] [file:human/AURKA/AURKA-uniprot.txt "CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638,"] [file:human/AURKA/AURKA-uniprot.txt "CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885,"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing file:human/AURKA/AURKA-uniprot.txt CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638, file:human/AURKA/AURKA-uniprot.txt CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885, |
| GO:0005813 centrosome | TAS PMID:19774610 Aurora A, centrosome structure, and the centrosome cycle. | ACCEPT | Summary: Centrosome (TAS). AURKA concentrates at centrosomes from early prophase to telophase and on spindle-pole microtubules from prophase to anaphase. Core location. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] [file:human/AURKA/AURKA-uniprot.txt "CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638,"] [file:human/AURKA/AURKA-uniprot.txt "CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885,"] [PMID:19774610 "Aurora A is associated with centrosomes, being localized at the centrosome just prior to the onset of mitosis and for the duration of mitosis."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing file:human/AURKA/AURKA-uniprot.txt CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638, file:human/AURKA/AURKA-uniprot.txt CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885, PMID:19774610 Aurora A is associated with centrosomes, being localized at the centrosome just prior to the onset of mitosis and for the duration of mitosis. |
| GO:0005814 centriole | IEA GO_REF:0000044 | ACCEPT | Summary: Centriole (IEA). AURKA associates with both the pericentriolar material and the centrioles, part of its core centrosomal localization. Accepted. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC material (PCM) and centrioles (PubMed:22014574). The localization to"] [file:human/AURKA/AURKA-uniprot.txt "CC Associates with the centrosome and the spindle microtubules during"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC material (PCM) and centrioles (PubMed:22014574). The localization to file:human/AURKA/AURKA-uniprot.txt CC Associates with the centrosome and the spindle microtubules during |
| GO:0005819 spindle | TAS PMID:19774610 Aurora A, centrosome structure, and the centrosome cycle. | ACCEPT | Summary: Spindle (TAS). AURKA associates with the spindle and spindle-pole microtubules during mitosis. Core location. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC Associates with the centrosome and the spindle microtubules during"] [file:human/AURKA/AURKA-uniprot.txt "CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885,"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC Associates with the centrosome and the spindle microtubules during file:human/AURKA/AURKA-uniprot.txt CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885, |
| GO:0005819 spindle | TAS PMID:9153231 Cell cycle-dependent expression and spindle pole localizatio... | ACCEPT | Summary: Spindle (TAS). AURKA associates with the spindle and spindle-pole microtubules during mitosis. Core location. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC Associates with the centrosome and the spindle microtubules during"] [file:human/AURKA/AURKA-uniprot.txt "CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885,"] [PMID:9153231 "Immunofluorescence studies using a specific antibody have shown that Aik is localized to the spindle pole during mitosis, especially from prophase through anaphase."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC Associates with the centrosome and the spindle microtubules during file:human/AURKA/AURKA-uniprot.txt CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885, PMID:9153231 Immunofluorescence studies using a specific antibody have shown that Aik is localized to the spindle pole during mitosis, especially from prophase through anaphase. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-174088 | KEEP AS NON CORE | Summary: Cytosol (TAS). AURKA is cytoplasmic outside its centrosomal and spindle pools, and Reactome places its mitotic reactions in the cytosol. A diffuse pool rather than a core site (centrosome and spindle pole); kept as non-core. Reactome event: 'Association of cell cycle proteins with the APC/C:Cdh1 complex'. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing |
| GO:0005829 cytosol | TAS Reactome:R-HSA-174105 | KEEP AS NON CORE | Summary: Cytosol (TAS). AURKA is cytoplasmic outside its centrosomal and spindle pools, and Reactome places its mitotic reactions in the cytosol. A diffuse pool rather than a core site (centrosome and spindle pole); kept as non-core. Reactome event: 'Degradation of multiubiquitinated cell cycle proteins'. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing |
| GO:0005829 cytosol | TAS Reactome:R-HSA-174195 | KEEP AS NON CORE | Summary: Cytosol (TAS). AURKA is cytoplasmic outside its centrosomal and spindle pools, and Reactome places its mitotic reactions in the cytosol. A diffuse pool rather than a core site (centrosome and spindle pole); kept as non-core. Reactome event: 'Ubiquitination of cell cycle proteins targeted by the APC/C:Cdh1complex'. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2574840 | KEEP AS NON CORE | Summary: Cytosol (TAS). AURKA is cytoplasmic outside its centrosomal and spindle pools, and Reactome places its mitotic reactions in the cytosol. A diffuse pool rather than a core site (centrosome and spindle pole); kept as non-core. Reactome event: 'AJUBA facilitates AURKA autophosphorylation'. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2574845 | KEEP AS NON CORE | Summary: Cytosol (TAS). AURKA is cytoplasmic outside its centrosomal and spindle pools, and Reactome places its mitotic reactions in the cytosol. A diffuse pool rather than a core site (centrosome and spindle pole); kept as non-core. Reactome event: 'AJUBA binds centrosome-associated AURKA'. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing |
| GO:0005829 cytosol | TAS Reactome:R-HSA-3000310 | KEEP AS NON CORE | Summary: Cytosol (TAS). AURKA is cytoplasmic outside its centrosomal and spindle pools, and Reactome places its mitotic reactions in the cytosol. A diffuse pool rather than a core site (centrosome and spindle pole); kept as non-core. Reactome event: 'AURKA phosphorylates PLK1'. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing |
| GO:0005829 cytosol | TAS Reactome:R-HSA-3000319 | KEEP AS NON CORE | Summary: Cytosol (TAS). AURKA is cytoplasmic outside its centrosomal and spindle pools, and Reactome places its mitotic reactions in the cytosol. A diffuse pool rather than a core site (centrosome and spindle pole); kept as non-core. Reactome event: 'BORA binds PLK1 and AURKA'. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8853405 | KEEP AS NON CORE | Summary: Cytosol (TAS). AURKA is cytoplasmic outside its centrosomal and spindle pools, and Reactome places its mitotic reactions in the cytosol. A diffuse pool rather than a core site (centrosome and spindle pole); kept as non-core. Reactome event: 'TPX2 binds AURKA at centrosomes'. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8853419 | KEEP AS NON CORE | Summary: Cytosol (TAS). AURKA is cytoplasmic outside its centrosomal and spindle pools, and Reactome places its mitotic reactions in the cytosol. A diffuse pool rather than a core site (centrosome and spindle pole); kept as non-core. Reactome event: 'TPX2 promotes AURKA autophosphorylation'. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8853429 | KEEP AS NON CORE | Summary: Cytosol (TAS). AURKA is cytoplasmic outside its centrosomal and spindle pools, and Reactome places its mitotic reactions in the cytosol. A diffuse pool rather than a core site (centrosome and spindle pole); kept as non-core. Reactome event: 'PHLDA1 binds AURKA'. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8853444 | KEEP AS NON CORE | Summary: Cytosol (TAS). AURKA is cytoplasmic outside its centrosomal and spindle pools, and Reactome places its mitotic reactions in the cytosol. A diffuse pool rather than a core site (centrosome and spindle pole); kept as non-core. Reactome event: 'AURKA phosphorylates PHLDA1'. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8853496 | KEEP AS NON CORE | Summary: Cytosol (TAS). AURKA is cytoplasmic outside its centrosomal and spindle pools, and Reactome places its mitotic reactions in the cytosol. A diffuse pool rather than a core site (centrosome and spindle pole); kept as non-core. Reactome event: 'SCF:FBXL7 binds AURKA'. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8854041 | KEEP AS NON CORE | Summary: Cytosol (TAS). AURKA is cytoplasmic outside its centrosomal and spindle pools, and Reactome places its mitotic reactions in the cytosol. A diffuse pool rather than a core site (centrosome and spindle pole); kept as non-core. Reactome event: 'SCF-FBXL7 ubiquitinates AURKA'. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8854044 | KEEP AS NON CORE | Summary: Cytosol (TAS). AURKA is cytoplasmic outside its centrosomal and spindle pools, and Reactome places its mitotic reactions in the cytosol. A diffuse pool rather than a core site (centrosome and spindle pole); kept as non-core. Reactome event: 'Proteasome degrades AURKA ubiquitinated by SCF-FBXL7'. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing |
| GO:0005876 spindle microtubule | IDA PMID:19801554 A cancer-associated aurora A mutant is mislocalized and misr... | ACCEPT | Summary: Spindle microtubule (IDA). AURKA associates with spindle microtubules. Accepted. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC Associates with the centrosome and the spindle microtubules during"] [file:human/AURKA/AURKA-uniprot.txt "CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885,"] [PMID:19801554 "We have further characterized the Aurora A(S155R) mutant protein, found that its reduced cellular activity and mislocalization are due to loss of interaction with TPX2, and deciphered the structural basis of the disruption at 2.5 A resolution."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC Associates with the centrosome and the spindle microtubules during file:human/AURKA/AURKA-uniprot.txt CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885, PMID:19801554 We have further characterized the Aurora A(S155R) mutant protein, found that its reduced cellular activity and mislocalization are due to loss of interaction with TPX2, and deciphered the structural basis of the disruption at 2.5 A resolution. |
| GO:0005929 cilium | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Cilium (IEA). UniProt places AURKA in cilia in the HEF1 study, but its documented action is at the basal body. Kept as non-core. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC {ECO:0000269|PubMed:17604723}. Cytoplasm, cytoskeleton, cilium basal"] [PMID:17604723 "Here, we show that interactions between the prometastatic scaffolding protein HEF1/Cas-L/NEDD9 and the oncogenic Aurora A (AurA) kinase at the basal body of cilia causes phosphorylation and activation of HDAC6, a tubulin deacetylase, promoting ciliary disassembly."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC {ECO:0000269|PubMed:17604723}. Cytoplasm, cytoskeleton, cilium basal PMID:17604723 Here, we show that interactions between the prometastatic scaffolding protein HEF1/Cas-L/NEDD9 and the oncogenic Aurora A (AurA) kinase at the basal body of cilia causes phosphorylation and activation of HDAC6, a tubulin deacetylase, promoting ciliary disassembly. |
| GO:0006468 protein phosphorylation | IDA PMID:21600873 Identification of Ski as a target for Aurora A kinase. | ACCEPT | Summary: Protein phosphorylation (IDA). AURKA phosphorylates many mitotic substrates, and its activation loop is autophosphorylated. Core process. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B,"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +"] [file:human/AURKA/AURKA-uniprot.txt "CC event of AURKA activation. Phosphatase inhibitor-2 (PPP1R2) and TPX2"] [PMID:21600873 "Here, we show that Aurora A kinase is able to phosphorylate Ski in vitro."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + file:human/AURKA/AURKA-uniprot.txt CC event of AURKA activation. Phosphatase inhibitor-2 (PPP1R2) and TPX2 PMID:21600873 Here, we show that Aurora A kinase is able to phosphorylate Ski in vitro. |
| GO:0006468 protein phosphorylation | IDA PMID:21820309 A complex of Kif18b and MCAK promotes microtubule depolymeri... | ACCEPT | Summary: Protein phosphorylation (IDA). AURKA phosphorylates many mitotic substrates, and its activation loop is autophosphorylated. Core process. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B,"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +"] [file:human/AURKA/AURKA-uniprot.txt "CC event of AURKA activation. Phosphatase inhibitor-2 (PPP1R2) and TPX2"] [PMID:21820309 "Furthermore, the Kif18b-MCAK interaction is negatively regulated by Aurora kinases through phosphorylation of MCAK, indicating that Aurora kinases regulate MT plus-end stability in mitosis through control of Kif18b-MCAK complex formation."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + file:human/AURKA/AURKA-uniprot.txt CC event of AURKA activation. Phosphatase inhibitor-2 (PPP1R2) and TPX2 PMID:21820309 Furthermore, the Kif18b-MCAK interaction is negatively regulated by Aurora kinases through phosphorylation of MCAK, indicating that Aurora kinases regulate MT plus-end stability in mitosis through control of Kif18b-MCAK complex formation. |
| GO:0006468 protein phosphorylation | TAS PMID:9153231 Cell cycle-dependent expression and spindle pole localizatio... | ACCEPT | Summary: Protein phosphorylation (TAS). AURKA phosphorylates many mitotic substrates, and its activation loop is autophosphorylated. Core process. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B,"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +"] [file:human/AURKA/AURKA-uniprot.txt "CC event of AURKA activation. Phosphatase inhibitor-2 (PPP1R2) and TPX2"] [PMID:9153231 "Its protein kinase activity is also enhanced at mitosis as inferred by exogenous casein phosphorylation."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + file:human/AURKA/AURKA-uniprot.txt CC event of AURKA activation. Phosphatase inhibitor-2 (PPP1R2) and TPX2 PMID:9153231 Its protein kinase activity is also enhanced at mitosis as inferred by exogenous casein phosphorylation. |
| GO:0007051 spindle organization | IEA GO_REF:0000117 | ACCEPT | Summary: Spindle organization (IEA). AURKA drives mitotic spindle assembly, centrosome maturation and separation, and spindle-pole organization. Core process. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC the establishment of mitotic spindle, centrosome duplication,"] [file:human/AURKA/AURKA-uniprot.txt "CC centrosome separation as well as maturation, chromosomal alignment,"] [file:human/AURKA/AURKA-uniprot.txt "CC Associates with the centrosome and the spindle microtubules during"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC the establishment of mitotic spindle, centrosome duplication, file:human/AURKA/AURKA-uniprot.txt CC centrosome separation as well as maturation, chromosomal alignment, file:human/AURKA/AURKA-uniprot.txt CC Associates with the centrosome and the spindle microtubules during |
| GO:0007051 spindle organization | IMP PMID:21820309 A complex of Kif18b and MCAK promotes microtubule depolymeri... | ACCEPT | Summary: Spindle organization (IMP). AURKA drives mitotic spindle assembly, centrosome maturation and separation, and spindle-pole organization. Core process. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC the establishment of mitotic spindle, centrosome duplication,"] [file:human/AURKA/AURKA-uniprot.txt "CC centrosome separation as well as maturation, chromosomal alignment,"] [file:human/AURKA/AURKA-uniprot.txt "CC Associates with the centrosome and the spindle microtubules during"] [PMID:21820309 "RESULTS: Here, we find that simultaneous inhibition of Aurora A and B results in a dramatic decrease in spindle MT stability, and we identify the uncharacterized kinesin-8 Kif18b as a mediator of this effect."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC the establishment of mitotic spindle, centrosome duplication, file:human/AURKA/AURKA-uniprot.txt CC centrosome separation as well as maturation, chromosomal alignment, file:human/AURKA/AURKA-uniprot.txt CC Associates with the centrosome and the spindle microtubules during PMID:21820309 RESULTS: Here, we find that simultaneous inhibition of Aurora A and B results in a dramatic decrease in spindle MT stability, and we identify the uncharacterized kinesin-8 Kif18b as a mediator of this effect. |
| GO:0007052 mitotic spindle organization | IBA GO_REF:0000033 | ACCEPT | Summary: Mitotic spindle organization (IBA). AURKA drives mitotic spindle assembly, centrosome maturation and separation, and spindle-pole organization. Core process. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC the establishment of mitotic spindle, centrosome duplication,"] [file:human/AURKA/AURKA-uniprot.txt "CC centrosome separation as well as maturation, chromosomal alignment,"] [file:human/AURKA/AURKA-uniprot.txt "CC Associates with the centrosome and the spindle microtubules during"] Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000681967 SUPPORTS TRANSFER Aurora family node; conserved Aurora-A function, with human AURKA among the experimentally annotated members. Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC the establishment of mitotic spindle, centrosome duplication, file:human/AURKA/AURKA-uniprot.txt CC centrosome separation as well as maturation, chromosomal alignment, file:human/AURKA/AURKA-uniprot.txt CC Associates with the centrosome and the spindle microtubules during |
| GO:0007052 mitotic spindle organization | IEA GO_REF:0000002 | ACCEPT | Summary: Mitotic spindle organization (IEA). AURKA drives mitotic spindle assembly, centrosome maturation and separation, and spindle-pole organization. Core process. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC the establishment of mitotic spindle, centrosome duplication,"] [file:human/AURKA/AURKA-uniprot.txt "CC centrosome separation as well as maturation, chromosomal alignment,"] [file:human/AURKA/AURKA-uniprot.txt "CC Associates with the centrosome and the spindle microtubules during"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC the establishment of mitotic spindle, centrosome duplication, file:human/AURKA/AURKA-uniprot.txt CC centrosome separation as well as maturation, chromosomal alignment, file:human/AURKA/AURKA-uniprot.txt CC Associates with the centrosome and the spindle microtubules during |
| GO:0007098 centrosome cycle | IEA GO_REF:0000002 | ACCEPT | Summary: Centrosome cycle (IEA). AURKA controls centrosome duplication, separation and maturation, and initiates CDK1 activation at centrosomes. Core process. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC the establishment of mitotic spindle, centrosome duplication,"] [file:human/AURKA/AURKA-uniprot.txt "CC centrosome separation as well as maturation, chromosomal alignment,"] [file:human/AURKA/AURKA-uniprot.txt "CC CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC the establishment of mitotic spindle, centrosome duplication, file:human/AURKA/AURKA-uniprot.txt CC centrosome separation as well as maturation, chromosomal alignment, file:human/AURKA/AURKA-uniprot.txt CC CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates |
| GO:0007100 mitotic centrosome separation | IEA GO_REF:0000002 | ACCEPT | Summary: Mitotic centrosome separation (IEA). AURKA controls centrosome duplication, separation and maturation, and initiates CDK1 activation at centrosomes. Core process. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC the establishment of mitotic spindle, centrosome duplication,"] [file:human/AURKA/AURKA-uniprot.txt "CC centrosome separation as well as maturation, chromosomal alignment,"] [file:human/AURKA/AURKA-uniprot.txt "CC CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC the establishment of mitotic spindle, centrosome duplication, file:human/AURKA/AURKA-uniprot.txt CC centrosome separation as well as maturation, chromosomal alignment, file:human/AURKA/AURKA-uniprot.txt CC CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates |
| GO:0009611 response to wounding | IDA PMID:19435814 Aurora-A overexpression in mouse liver causes p53-dependent ... | MARK AS OVER ANNOTATED | Summary: Response to wounding (IDA). The basis is transgenic overexpression of human AURKA in mouse liver, which altered cell-cycle entry and caused premitotic arrest during regeneration after hepatectomy. That is an overexpression phenotype, not participation in a wound response. Over-annotation. Reason: [PMID:19435814 "The overexpression of Aurora-A after hepatectomy caused an earlier entry into S phase, a sustaining of DNA synthesis, and premitotic arrest in the regenerating liver."] Supporting Evidence: PMID:19435814 The overexpression of Aurora-A after hepatectomy caused an earlier entry into S phase, a sustaining of DNA synthesis, and premitotic arrest in the regenerating liver. |
| GO:0010389 regulation of G2/M transition of mitotic cell cycle | TAS Reactome:R-HSA-8854518 | ACCEPT | Summary: Regulation of G2/M transition of mitotic cell cycle (TAS). AURKA contributes to mitotic progression, initiating CDK1 activation at centrosomes and acting through many mitotic substrates. Core process. Reactome event: 'AURKA Activation by TPX2'. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the"] [file:human/AURKA/AURKA-uniprot.txt "CC CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates"] [file:human/AURKA/AURKA-uniprot.txt "CC centrosome separation as well as maturation, chromosomal alignment,"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the file:human/AURKA/AURKA-uniprot.txt CC CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates file:human/AURKA/AURKA-uniprot.txt CC centrosome separation as well as maturation, chromosomal alignment, |
| GO:0010629 negative regulation of gene expression | IMP PMID:28218735 Aurora kinase A regulates Survivin stability through targeti... | KEEP AS NON CORE | Summary: Negative regulation of gene expression (IMP). In gastric cancer cells AURKA negatively regulates FOXP1-mediated FBXL7 expression, which lowers FBXL7 and so stabilizes survivin (BIRC5). A context-specific, indirect effect; kept as non-core. Reason: [PMID:28218735 "Overexpression of AURKA exacerbated gastric cancer drug resistance through upregulating the expression of the anti-apoptotic protein Survivin."] [file:human/AURKA/AURKA-uniprot.txt "CC anti-apoptosis protein BIRC5 by suppressing the expression of the"] [PMID:28218735 "We next showed that AURKA was required for FBXL7 transcription and that AURKA negatively regulated FOXP1-mediated FBXL7 expression."] Supporting Evidence: PMID:28218735 Overexpression of AURKA exacerbated gastric cancer drug resistance through upregulating the expression of the anti-apoptotic protein Survivin. file:human/AURKA/AURKA-uniprot.txt CC anti-apoptosis protein BIRC5 by suppressing the expression of the PMID:28218735 We next showed that AURKA was required for FBXL7 transcription and that AURKA negatively regulated FOXP1-mediated FBXL7 expression. |
| GO:0015630 microtubule cytoskeleton | IDA PMID:19801554 A cancer-associated aurora A mutant is mislocalized and misr... | ACCEPT | Summary: Microtubule cytoskeleton (IDA). AURKA associates with centrosomal and spindle microtubules. Accepted. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC Associates with the centrosome and the spindle microtubules during"] [file:human/AURKA/AURKA-uniprot.txt "CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885,"] [PMID:19801554 "We have further characterized the Aurora A(S155R) mutant protein, found that its reduced cellular activity and mislocalization are due to loss of interaction with TPX2, and deciphered the structural basis of the disruption at 2.5 A resolution."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC Associates with the centrosome and the spindle microtubules during file:human/AURKA/AURKA-uniprot.txt CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885, PMID:19801554 We have further characterized the Aurora A(S155R) mutant protein, found that its reduced cellular activity and mislocalization are due to loss of interaction with TPX2, and deciphered the structural basis of the disruption at 2.5 A resolution. |
| GO:0016323 basolateral plasma membrane | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Basolateral plasma membrane (IEA). A minor, epithelial context; the main AURKA sites are centrosome and spindle. Kept as non-core. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC body {ECO:0000269|PubMed:17604723}. Basolateral cell membrane"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC body {ECO:0000269|PubMed:17604723}. Basolateral cell membrane |
| GO:0016323 basolateral plasma membrane | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Basolateral plasma membrane (ISS). A minor, epithelial context; the main AURKA sites are centrosome and spindle. Kept as non-core. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC body {ECO:0000269|PubMed:17604723}. Basolateral cell membrane"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC body {ECO:0000269|PubMed:17604723}. Basolateral cell membrane |
| GO:0018105 peptidyl-serine phosphorylation | IMP PMID:28218735 Aurora kinase A regulates Survivin stability through targeti... | ACCEPT | Summary: Peptidyl-serine phosphorylation (IMP). AURKA phosphorylates many mitotic substrates, and its activation loop is autophosphorylated. Core process. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B,"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +"] [file:human/AURKA/AURKA-uniprot.txt "CC event of AURKA activation. Phosphatase inhibitor-2 (PPP1R2) and TPX2"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + file:human/AURKA/AURKA-uniprot.txt CC event of AURKA activation. Phosphatase inhibitor-2 (PPP1R2) and TPX2 |
| GO:0019901 protein kinase binding | IPI PMID:18615013 Polo-like kinase-1 is activated by aurora A to promote check... | KEEP AS NON CORE | Summary: Protein kinase binding (IPI). AURKA binds and phosphorylates PLK1 (Thr210) to activate it during checkpoint recovery. Accepted as a kinase-substrate binding; non-core. Reason: [PMID:18615013 "Here we show that in human cells PLK1 activation occurs several hours before entry into mitosis, and requires aurora A (AURKA, also known as STK6)-dependent phosphorylation of Thr 210."] [file:human/AURKA/AURKA-uniprot.txt "CC DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3,"] Supporting Evidence: PMID:18615013 Here we show that in human cells PLK1 activation occurs several hours before entry into mitosis, and requires aurora A (AURKA, also known as STK6)-dependent phosphorylation of Thr 210. file:human/AURKA/AURKA-uniprot.txt CC DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3, |
| GO:0030496 midbody | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Midbody (IEA). AURKA contributes to cytokinesis, but the midbody is principally an Aurora-B site. Kept as non-core. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC the establishment of mitotic spindle, centrosome duplication,"] [file:human/AURKA/AURKA-uniprot.txt "CC centrosome separation as well as maturation, chromosomal alignment,"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC the establishment of mitotic spindle, centrosome duplication, file:human/AURKA/AURKA-uniprot.txt CC centrosome separation as well as maturation, chromosomal alignment, |
| GO:0030496 midbody | TAS PMID:19774610 Aurora A, centrosome structure, and the centrosome cycle. | KEEP AS NON CORE | Summary: Midbody (TAS). AURKA contributes to cytokinesis, but the midbody is principally an Aurora-B site. Kept as non-core. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC the establishment of mitotic spindle, centrosome duplication,"] [file:human/AURKA/AURKA-uniprot.txt "CC centrosome separation as well as maturation, chromosomal alignment,"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC the establishment of mitotic spindle, centrosome duplication, file:human/AURKA/AURKA-uniprot.txt CC centrosome separation as well as maturation, chromosomal alignment, |
| GO:0031616 spindle pole centrosome | IDA PMID:19801554 A cancer-associated aurora A mutant is mislocalized and misr... | ACCEPT | Summary: Spindle pole centrosome (IDA). AURKA concentrates at centrosomes from early prophase to telophase and on spindle-pole microtubules from prophase to anaphase. Core location. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] [file:human/AURKA/AURKA-uniprot.txt "CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638,"] [file:human/AURKA/AURKA-uniprot.txt "CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885,"] [PMID:19801554 "We have further characterized the Aurora A(S155R) mutant protein, found that its reduced cellular activity and mislocalization are due to loss of interaction with TPX2, and deciphered the structural basis of the disruption at 2.5 A resolution."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing file:human/AURKA/AURKA-uniprot.txt CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638, file:human/AURKA/AURKA-uniprot.txt CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885, PMID:19801554 We have further characterized the Aurora A(S155R) mutant protein, found that its reduced cellular activity and mislocalization are due to loss of interaction with TPX2, and deciphered the structural basis of the disruption at 2.5 A resolution. |
| GO:0031647 regulation of protein stability | IMP PMID:15987997 Phosphorylation and stabilization of HURP by Aurora-A: impli... | KEEP AS NON CORE | Summary: Regulation of protein stability (IMP). AURKA phosphorylates and stabilizes HURP (DLGAP5), one of several substrate-level effects. Kept as non-core. Reason: [PMID:15987997 "Moreover, Aurora-A phosphorylated HURP in vitro and in vivo."] Supporting Evidence: PMID:15987997 Moreover, Aurora-A phosphorylated HURP in vitro and in vivo. |
| GO:0032091 negative regulation of protein binding | IDA PMID:21820309 A complex of Kif18b and MCAK promotes microtubule depolymeri... | KEEP AS NON CORE | Summary: Negative regulation of protein binding (IDA). Aurora kinases phosphorylate MCAK and so inhibit Kif18b-MCAK complex formation, tuning spindle microtubule dynamics. A downstream consequence of kinase activity; kept as non-core. Reason: [PMID:21820309 "Furthermore, the Kif18b-MCAK interaction is negatively regulated by Aurora kinases through phosphorylation of MCAK, indicating that Aurora kinases regulate MT plus-end stability in mitosis through control of Kif18b-MCAK complex formation."] Supporting Evidence: PMID:21820309 Furthermore, the Kif18b-MCAK interaction is negatively regulated by Aurora kinases through phosphorylation of MCAK, indicating that Aurora kinases regulate MT plus-end stability in mitosis through control of Kif18b-MCAK complex formation. |
| GO:0032133 chromosome passenger complex | IBA GO_REF:0000033 | MARK AS OVER ANNOTATED | Summary: Chromosome passenger complex (IBA). The CPC (INCENP, survivin, borealin and Aurora-B) contains Aurora-B, not Aurora-A. AURKA's interaction with INCENP is not membership of the CPC. The family-level propagation transfers an Aurora-B-specific complex. Over-annotation. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] [file:human/AURKA/AURKA-uniprot.txt "CC Associates with the centrosome and the spindle microtubules during"] Propagation Review Root cause: PROPAGATION BAD Failure modes: WRONG ORTHOLOG OR PARALOG Sources checked: PANTHER:PTN000681967 SUPPORTS SOURCE BUT NOT TARGET Aurora family node; the annotation reflects Aurora-B biology (CPC membership) and does not hold for Aurora-A. Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing file:human/AURKA/AURKA-uniprot.txt CC Associates with the centrosome and the spindle microtubules during |
| GO:0032465 regulation of cytokinesis | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Regulation of cytokinesis (IBA). UniProt lists cytokinesis among AURKA's mitotic roles, but the principal Aurora regulator of cytokinesis is Aurora-B. Kept as non-core. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC the establishment of mitotic spindle, centrosome duplication,"] [file:human/AURKA/AURKA-uniprot.txt "CC centrosome separation as well as maturation, chromosomal alignment,"] Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000681967 SUPPORTS TRANSFER Aurora family node; the term reflects mainly Aurora-B biology, so it is kept as non-core for Aurora-A. Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC the establishment of mitotic spindle, centrosome duplication, file:human/AURKA/AURKA-uniprot.txt CC centrosome separation as well as maturation, chromosomal alignment, |
| GO:0036064 ciliary basal body | IDA GO_REF:0000052 | ACCEPT | Summary: Ciliary basal body (IDA). AURKA acts at the basal body of cilia, where NEDD9 activates it to drive ciliary disassembly. Accepted. Reason: [PMID:17604723 "Here, we show that interactions between the prometastatic scaffolding protein HEF1/Cas-L/NEDD9 and the oncogenic Aurora A (AurA) kinase at the basal body of cilia causes phosphorylation and activation of HDAC6, a tubulin deacetylase, promoting ciliary disassembly."] [file:human/AURKA/AURKA-uniprot.txt "CC {ECO:0000269|PubMed:17604723}. Cytoplasm, cytoskeleton, cilium basal"] Supporting Evidence: PMID:17604723 Here, we show that interactions between the prometastatic scaffolding protein HEF1/Cas-L/NEDD9 and the oncogenic Aurora A (AurA) kinase at the basal body of cilia causes phosphorylation and activation of HDAC6, a tubulin deacetylase, promoting ciliary disassembly. file:human/AURKA/AURKA-uniprot.txt CC {ECO:0000269|PubMed:17604723}. Cytoplasm, cytoskeleton, cilium basal |
| GO:0036064 ciliary basal body | IDA PMID:17604723 HEF1-dependent Aurora A activation induces disassembly of th... | ACCEPT | Summary: Ciliary basal body (IDA). AURKA acts at the basal body of cilia, where NEDD9 activates it to drive ciliary disassembly. Accepted. Reason: [PMID:17604723 "Here, we show that interactions between the prometastatic scaffolding protein HEF1/Cas-L/NEDD9 and the oncogenic Aurora A (AurA) kinase at the basal body of cilia causes phosphorylation and activation of HDAC6, a tubulin deacetylase, promoting ciliary disassembly."] [file:human/AURKA/AURKA-uniprot.txt "CC {ECO:0000269|PubMed:17604723}. Cytoplasm, cytoskeleton, cilium basal"] Supporting Evidence: PMID:17604723 Here, we show that interactions between the prometastatic scaffolding protein HEF1/Cas-L/NEDD9 and the oncogenic Aurora A (AurA) kinase at the basal body of cilia causes phosphorylation and activation of HDAC6, a tubulin deacetylase, promoting ciliary disassembly. file:human/AURKA/AURKA-uniprot.txt CC {ECO:0000269|PubMed:17604723}. Cytoplasm, cytoskeleton, cilium basal |
| GO:0043005 neuron projection | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Neuron projection (IEA). AURKA acts in microtubule remodelling during neurite extension; this is a non-mitotic, context-specific role. Kept as non-core. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC {ECO:0000250|UniProtKB:P97477}. Cell projection, neuron projection"] [file:human/AURKA/AURKA-uniprot.txt "CC (PubMed:19812038). Plays a role in microtubule remodeling during"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC {ECO:0000250|UniProtKB:P97477}. Cell projection, neuron projection file:human/AURKA/AURKA-uniprot.txt CC (PubMed:19812038). Plays a role in microtubule remodeling during |
| GO:0045840 positive regulation of mitotic nuclear division | TAS PMID:19774610 Aurora A, centrosome structure, and the centrosome cycle. | ACCEPT | Summary: Positive regulation of mitotic nuclear division (TAS). AURKA contributes to mitotic progression, initiating CDK1 activation at centrosomes and acting through many mitotic substrates. Core process. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the"] [file:human/AURKA/AURKA-uniprot.txt "CC CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates"] [file:human/AURKA/AURKA-uniprot.txt "CC centrosome separation as well as maturation, chromosomal alignment,"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the file:human/AURKA/AURKA-uniprot.txt CC CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates file:human/AURKA/AURKA-uniprot.txt CC centrosome separation as well as maturation, chromosomal alignment, |
| GO:0045931 positive regulation of mitotic cell cycle | ISS GO_REF:0000024 | ACCEPT | Summary: Positive regulation of mitotic cell cycle (ISS). AURKA contributes to mitotic progression, initiating CDK1 activation at centrosomes and acting through many mitotic substrates. Core process. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the"] [file:human/AURKA/AURKA-uniprot.txt "CC CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates"] [file:human/AURKA/AURKA-uniprot.txt "CC centrosome separation as well as maturation, chromosomal alignment,"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the file:human/AURKA/AURKA-uniprot.txt CC CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates file:human/AURKA/AURKA-uniprot.txt CC centrosome separation as well as maturation, chromosomal alignment, |
| GO:0046605 regulation of centrosome cycle | TAS PMID:19774610 Aurora A, centrosome structure, and the centrosome cycle. | ACCEPT | Summary: Regulation of centrosome cycle (TAS). AURKA controls centrosome duplication, separation and maturation, and initiates CDK1 activation at centrosomes. Core process. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC the establishment of mitotic spindle, centrosome duplication,"] [file:human/AURKA/AURKA-uniprot.txt "CC centrosome separation as well as maturation, chromosomal alignment,"] [file:human/AURKA/AURKA-uniprot.txt "CC CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates"] [PMID:19774610 "Aurora A is associated with centrosomes, being localized at the centrosome just prior to the onset of mitosis and for the duration of mitosis."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC the establishment of mitotic spindle, centrosome duplication, file:human/AURKA/AURKA-uniprot.txt CC centrosome separation as well as maturation, chromosomal alignment, file:human/AURKA/AURKA-uniprot.txt CC CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates PMID:19774610 Aurora A is associated with centrosomes, being localized at the centrosome just prior to the onset of mitosis and for the duration of mitosis. |
| GO:0046777 protein autophosphorylation | TAS PMID:19774610 Aurora A, centrosome structure, and the centrosome cycle. | ACCEPT | Summary: Protein autophosphorylation (TAS). AURKA phosphorylates many mitotic substrates, and its activation loop is autophosphorylated. Core process. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B,"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +"] [file:human/AURKA/AURKA-uniprot.txt "CC event of AURKA activation. Phosphatase inhibitor-2 (PPP1R2) and TPX2"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + file:human/AURKA/AURKA-uniprot.txt CC event of AURKA activation. Phosphatase inhibitor-2 (PPP1R2) and TPX2 |
| GO:0046982 protein heterodimerization activity | IPI PMID:20460379 Solution structure of human growth arrest and DNA damage 45a... | MARK AS OVER ANNOTATED | Summary: Protein heterodimerization activity (IPI). The NMR study shows the AURKA N-terminal domain contacting the inhibitor GADD45A near GADD45A's own dimerization site. That is an inhibitor-kinase interaction, not formation of an AURKA heterodimer in the sense of the term. Over-annotation. Reason: [PMID:20460379 "NMR analysis shows that Aurora A interacts through its N-terminal domain with a region of human Gadd45Ξ± encompassing the site of dimerization"] Supporting Evidence: PMID:20460379 NMR analysis shows that Aurora A interacts through its N-terminal domain with a region of human Gadd45Ξ± encompassing the site of dimerization |
| GO:0048471 perinuclear region of cytoplasm | IDA PMID:20531406 A human B-cell interactome identifies MYB and FOXM1 as maste... | KEEP AS NON CORE | Summary: Perinuclear region of cytoplasm (IDA). A minor or context-specific pool of AURKA; its main sites are the centrosome and spindle. Kept as non-core. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] [file:human/AURKA/AURKA-uniprot.txt "CC Associates with the centrosome and the spindle microtubules during"] [PMID:20531406 "High-resolution confocal imaging showed that these proteins are co-localized either in the nucleus or perinuclearly (Figure 6C)."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing file:human/AURKA/AURKA-uniprot.txt CC Associates with the centrosome and the spindle microtubules during PMID:20531406 High-resolution confocal imaging showed that these proteins are co-localized either in the nucleus or perinuclearly (Figure 6C). |
| GO:0051233 spindle midzone | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Spindle midzone (IBA). The family node includes Aurora-B, which concentrates at the midzone. AURKA's documented sites are poles and spindle microtubules. Kept as non-core. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC Associates with the centrosome and the spindle microtubules during"] [file:human/AURKA/AURKA-uniprot.txt "CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885,"] Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000681967 SUPPORTS TRANSFER Aurora family node; the term reflects mainly Aurora-B biology, so it is kept as non-core for Aurora-A. Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC Associates with the centrosome and the spindle microtubules during file:human/AURKA/AURKA-uniprot.txt CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885, |
| GO:0051321 meiotic cell cycle | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: Meiotic cell cycle (IEA). Broad family mapping. AURKA activity regulates meiotic spindle and aMTOC organization in mouse oocytes. Kept as non-core. Reason: [PMID:31895686 "Taken together, our current data reveal a critical role for AURKA activity in regulating microtubule dynamics, spindle pole focusing, and the maintenance of oocyte aMTOC organization at assembled meiotic spindles."] Supporting Evidence: PMID:31895686 Taken together, our current data reveal a critical role for AURKA activity in regulating microtubule dynamics, spindle pole focusing, and the maintenance of oocyte aMTOC organization at assembled meiotic spindles. |
| GO:0061523 cilium disassembly | IMP PMID:17604723 HEF1-dependent Aurora A activation induces disassembly of th... | ACCEPT | Summary: Cilium disassembly (IMP). At the ciliary basal body, NEDD9/HEF1-activated AURKA phosphorylates and activates the deacetylase HDAC6 to resorb the cilium. Accepted. Reason: [PMID:17604723 "Here, we show that interactions between the prometastatic scaffolding protein HEF1/Cas-L/NEDD9 and the oncogenic Aurora A (AurA) kinase at the basal body of cilia causes phosphorylation and activation of HDAC6, a tubulin deacetylase, promoting ciliary disassembly."] [file:human/AURKA/AURKA-uniprot.txt "CC outgrowth (By similarity). Required for cilia disassembly via"] Supporting Evidence: PMID:17604723 Here, we show that interactions between the prometastatic scaffolding protein HEF1/Cas-L/NEDD9 and the oncogenic Aurora A (AurA) kinase at the basal body of cilia causes phosphorylation and activation of HDAC6, a tubulin deacetylase, promoting ciliary disassembly. file:human/AURKA/AURKA-uniprot.txt CC outgrowth (By similarity). Required for cilia disassembly via |
| GO:0090068 positive regulation of cell cycle process | IEA GO_REF:0000117 | ACCEPT | Summary: Positive regulation of cell cycle process (IEA). AURKA contributes to mitotic progression, initiating CDK1 activation at centrosomes and acting through many mitotic substrates. Core process. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the"] [file:human/AURKA/AURKA-uniprot.txt "CC CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates"] [file:human/AURKA/AURKA-uniprot.txt "CC centrosome separation as well as maturation, chromosomal alignment,"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the file:human/AURKA/AURKA-uniprot.txt CC CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates file:human/AURKA/AURKA-uniprot.txt CC centrosome separation as well as maturation, chromosomal alignment, |
| GO:0090141 positive regulation of mitochondrial fission | IMP PMID:21822277 RALA and RALBP1 regulate mitochondrial fission at mitosis. | KEEP AS NON CORE | Summary: Positive regulation of mitochondrial fission (IMP). In mitosis AURKA phosphorylates RALA Ser194, relocalizing it to mitochondria with RALBP1 and DRP1 to promote fission. A substrate-level mitotic output; kept as non-core. Reason: [PMID:21822277 "Specifically, the mitotic kinase Aurora A phosphorylates Ser 194 of RALA, relocalizing it to the mitochondria, where it concentrates RALBP1 and DRP1."] Supporting Evidence: PMID:21822277 Specifically, the mitotic kinase Aurora A phosphorylates Ser 194 of RALA, relocalizing it to the mitochondria, where it concentrates RALBP1 and DRP1. |
| GO:0097421 liver regeneration | IDA PMID:19435814 Aurora-A overexpression in mouse liver causes p53-dependent ... | MARK AS OVER ANNOTATED | Summary: Liver regeneration (IDA). The same transgenic overexpression study shows that excess AURKA disturbs the regenerative cell cycle; it does not establish a role for normal AURKA in liver regeneration. Over-annotation. Reason: [PMID:19435814 "The overexpression of Aurora-A after hepatectomy caused an earlier entry into S phase, a sustaining of DNA synthesis, and premitotic arrest in the regenerating liver."] Supporting Evidence: PMID:19435814 The overexpression of Aurora-A after hepatectomy caused an earlier entry into S phase, a sustaining of DNA synthesis, and premitotic arrest in the regenerating liver. |
| GO:0097431 mitotic spindle pole | IDA PMID:25657325 CENP-32 is required to maintain centrosomal dominance in bip... | ACCEPT | Summary: Mitotic spindle pole (IDA). AURKA concentrates at centrosomes from early prophase to telophase and on spindle-pole microtubules from prophase to anaphase. Core location. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing"] [file:human/AURKA/AURKA-uniprot.txt "CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638,"] [file:human/AURKA/AURKA-uniprot.txt "CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885,"] [PMID:25657325 "Compared to control cells, CENP-32 siRNA cells exhibited a weaker (but still positive) staining of Aurora A on the detached centrosomes and a stronger diffuse signal on spindle microtubules (Figure 2, A and E)."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing file:human/AURKA/AURKA-uniprot.txt CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638, file:human/AURKA/AURKA-uniprot.txt CC to the spindle pole MTs from prophase to anaphase (PubMed:17229885, PMID:25657325 Compared to control cells, CENP-32 siRNA cells exhibited a weaker (but still positive) staining of Aurora A on the detached centrosomes and a stronger diffuse signal on spindle microtubules (Figure 2, A and E). |
| GO:0106310 protein serine kinase activity | EXP PMID:12237287 Crystal structure of aurora-2, an oncogenic serine/threonine... | ACCEPT | Summary: Protein serine kinase activity (EXP). AURKA is a mitotic serine/threonine kinase with demonstrated serine and threonine phosphotransferase activity on many substrates. Core function. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +"] [file:human/AURKA/AURKA-uniprot.txt "CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B,"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + file:human/AURKA/AURKA-uniprot.txt CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, |
| GO:0106310 protein serine kinase activity | EXP PMID:16337122 SAR and inhibitor complex structure determination of a novel... | ACCEPT | Summary: Protein serine kinase activity (EXP). AURKA is a mitotic serine/threonine kinase with demonstrated serine and threonine phosphotransferase activity on many substrates. Core function. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +"] [file:human/AURKA/AURKA-uniprot.txt "CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B,"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + file:human/AURKA/AURKA-uniprot.txt CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, |
| GO:0106310 protein serine kinase activity | EXP PMID:19140666 Structure-based drug design of novel Aurora kinase A inhibit... | ACCEPT | Summary: Protein serine kinase activity (EXP). AURKA is a mitotic serine/threonine kinase with demonstrated serine and threonine phosphotransferase activity on many substrates. Core function. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +"] [file:human/AURKA/AURKA-uniprot.txt "CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B,"] [PMID:19140666 "On the basis of this insight, bioisosteric replacement of the ester with amide linkage and changing the ethyl substituent to hydrophobic 3-acetamidophenyl ring led to the identification of 12w with a approximately 450-fold improved Aurora kinase A inhibition potency (IC(50) = 33 nM), compared to 8a."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + file:human/AURKA/AURKA-uniprot.txt CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, PMID:19140666 On the basis of this insight, bioisosteric replacement of the ester with amide linkage and changing the ethyl substituent to hydrophobic 3-acetamidophenyl ring led to the identification of 12w with a approximately 450-fold improved Aurora kinase A inhibition potency (IC(50) = 33 nM), compared to 8a. |
| GO:0106310 protein serine kinase activity | EXP PMID:19402633 A class of 2,4-bisanilinopyrimidine Aurora A inhibitors with... | ACCEPT | Summary: Protein serine kinase activity (EXP). AURKA is a mitotic serine/threonine kinase with demonstrated serine and threonine phosphotransferase activity on many substrates. Core function. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +"] [file:human/AURKA/AURKA-uniprot.txt "CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B,"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + file:human/AURKA/AURKA-uniprot.txt CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, |
| GO:0106310 protein serine kinase activity | EXP PMID:27192185 Aurora-A regulates MCRS1 function during mitosis. | ACCEPT | Summary: Protein serine kinase activity (EXP). AURKA is a mitotic serine/threonine kinase with demonstrated serine and threonine phosphotransferase activity on many substrates. Core function. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +"] [file:human/AURKA/AURKA-uniprot.txt "CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B,"] [PMID:27192185 "We show that MCRS1 is phosphorylated by the Aurora-A kinase in mitosis on Ser35/36."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + file:human/AURKA/AURKA-uniprot.txt CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, PMID:27192185 We show that MCRS1 is phosphorylated by the Aurora-A kinase in mitosis on Ser35/36. |
| GO:0106310 protein serine kinase activity | EXP PMID:27837025 Structural basis of N-Myc binding by Aurora-A and its destab... | ACCEPT | Summary: Protein serine kinase activity (EXP). AURKA is a mitotic serine/threonine kinase with demonstrated serine and threonine phosphotransferase activity on many substrates. Core function. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +"] [file:human/AURKA/AURKA-uniprot.txt "CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B,"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + file:human/AURKA/AURKA-uniprot.txt CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, |
| GO:0106310 protein serine kinase activity | EXP PMID:28218735 Aurora kinase A regulates Survivin stability through targeti... | ACCEPT | Summary: Protein serine kinase activity (EXP). AURKA is a mitotic serine/threonine kinase with demonstrated serine and threonine phosphotransferase activity on many substrates. Core function. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +"] [file:human/AURKA/AURKA-uniprot.txt "CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B,"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + file:human/AURKA/AURKA-uniprot.txt CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, |
| GO:0106310 protein serine kinase activity | IEA GO_REF:0000116 | ACCEPT | Summary: Protein serine kinase activity (IEA). AURKA is a mitotic serine/threonine kinase with demonstrated serine and threonine phosphotransferase activity on many substrates. Core function. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +"] [file:human/AURKA/AURKA-uniprot.txt "CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +"] [file:human/AURKA/AURKA-uniprot.txt "CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B,"] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + file:human/AURKA/AURKA-uniprot.txt CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + file:human/AURKA/AURKA-uniprot.txt CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, |
| GO:0140677 molecular function activator activity | EXP PMID:12237287 Crystal structure of aurora-2, an oncogenic serine/threonine... | UNDECIDED | Summary: Molecular function activator activity (EXP). The cited structure paper reports Aurora-2 bound to adenosine and does not show AURKA activating another molecule's function. AURKA does activate PLK1 and CDK1 pathways through phosphorylation, which is captured by kinase activity. The basis for this row is unclear. Reason: [PMID:12237287 "We report the first crystal structure of Aurora-2 kinase in complex with adenosine."] [file:human/AURKA/AURKA-uniprot.txt "CC CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates"] Supporting Evidence: PMID:12237287 We report the first crystal structure of Aurora-2 kinase in complex with adenosine. file:human/AURKA/AURKA-uniprot.txt CC CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates |
| GO:1901796 regulation of signal transduction by p53 class mediator | TAS Reactome:R-HSA-6804756 | KEEP AS NON CORE | Summary: Regulation of signal transduction by p53 class mediator (TAS). AURKA phosphorylates and destabilizes p53. Non-core relative to its mitotic roles. Reactome event: 'Regulation of TP53 Activity through Phosphorylation'. Reason: [file:human/AURKA/AURKA-uniprot.txt "CC phosphorylating and destabilizing p53/TP53 (PubMed:14702041)."] Supporting Evidence: file:human/AURKA/AURKA-uniprot.txt CC phosphorylating and destabilizing p53/TP53 (PubMed:14702041). |
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Download this section (compressed HTML)Q: Which AURKA functions depend on its catalytic activity and which on scaffolding (for example N-Myc stabilization, or nuclear hnRNP K-dependent MYC transactivation), and are the latter separable in cells?
Q: How do the TPX2 and CEP192 activation routes divide AURKA activity between the spindle and the centrosome?
Q: Does AURKA have a direct role in human oocyte meiotic spindle assembly comparable to that shown in mouse oocytes?
Experiment: Compare kinase-dead and analog-sensitive AURKA alleles in human cells for centrosome, spindle, cilium-disassembly and N-Myc-stabilization phenotypes.
Experiment: Express AURKA variants that cannot bind TPX2 or CEP192 to separate the spindle and centrosomal activation pools.
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