| + |
AURKA | up-regulates 
phosphorylation
|
TP53 |
0.771 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-199939 |
Ser106 |
SQKTYQGsYGFRLGF |
Homo sapiens |
|
| pmid |
sentence |
| 23201157 |
Ser-106 phosphorylation of p53 decreases its interaction with mdm2 and prolongs the half-life of p53 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | up-regulates activity
phosphorylation
|
SPIN1 |
0.245 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273549 |
Ser109 |
LNKDERVsALEVLPD |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 22258766 |
The Ser84 and Ser99 amino acids within SPINDLIN1 were further identified as the key functional sites in WNT/TCF-4 signaling activation. Mutation of these two sites of SPINDLIN1 abolished its effects on promoting WNT/TCF-4 signaling and cancer cell proliferation. We further found that Aurora-A could interact with and phosphorylate SPINDLIN1 at its key functional sites, Ser84 and Ser99, suggesting that phosphorylation of SPINDLIN1 is involved in its oncogenic function. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273550 |
Ser124 |
RVATSRIsDAHLADT |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 22258766 |
The Ser84 and Ser99 amino acids within SPINDLIN1 were further identified as the key functional sites in WNT/TCF-4 signaling activation. Mutation of these two sites of SPINDLIN1 abolished its effects on promoting WNT/TCF-4 signaling and cancer cell proliferation. We further found that Aurora-A could interact with and phosphorylate SPINDLIN1 at its key functional sites, Ser84 and Ser99, suggesting that phosphorylation of SPINDLIN1 is involved in its oncogenic function. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
AURKA |
phosphorylation
|
H3C1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-118886 |
Ser11 |
TKQTARKsTGGKAPR |
Mus musculus |
|
| pmid |
sentence |
| 12234980 |
In the present study, chromosome number instability and increased tumor invasiveness were noted in constitutively AIM-1-overexpressing cells in vivo. Increased mitotic Ser-10 phosphorylation was also observed in various colorectal tumor cells with high AIM-1 expression levels. These data suggest that increased H3 histone phosphorylation as a result of AIM-1 overexpression is a major precipitating factor of chromosome instability and, thus, may play a role in carcinogenesis. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
AURKA | up-regulates activity
phosphorylation
|
H3C1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98289 |
Ser11 |
TKQTARKsTGGKAPR |
Homo sapiens |
|
| pmid |
sentence |
| 12588998 |
Phosphorylation at ser-11 (h3s10ph) by aurkb is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. Phosphorylation at ser-11 (h3s10ph) by aurkb is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | up-regulates activity
phosphorylation
|
SPAG5 |
0.525 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276648 |
Ser115 |
ISSTPKTsEEAVDPL |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 25009111 |
We report here that Astrin acts as a mitotic phosphoprotein, and Aurora-A phosphorylates Astrin at Ser(115). The phosphorylation-deficient mutant Astrin S115A abnormally activates spindle assembly checkpoint and delays mitosis progression, decreases spindle stability, and induces chromosome misalignment. Mechanistic analyses reveal that Astrin phosphorylation mimicking mutant S115D, instead of S115A, binds and induces ubiquitination and degradation of securin, which sequentially activates Separase, an enzyme required for the separation of sister chromatids. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | up-regulates activity
phosphorylation
|
TPX2 |
0.963 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265089 |
Ser121 |
PAQPQRRsLRLSAQK |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 26240182 |
Here we show that TPX2, a microtubule-bundling protein and activator of Aurora A, plays an important role. TPX2 was phosphorylated by Aurora A during mitosis. Its phospho-null mutant caused short metaphase spindles coupled with low microtubule flux rate. Interestingly, phosphorylation of TPX2 regulated its interaction with CLASP1 but not Kif2a.|This suggests that TPX2 phosphorylation positively regulates the function of CLASP1.| This is in accord with a phosphoproteomics study that identified S121 and S125 as potential phosphorylation sites for Aurora A in mitotic HeLa cells |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265088 |
Ser125 |
QRRSLRLsAQKDLEQ |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 26240182 |
Here we show that TPX2, a microtubule-bundling protein and activator of Aurora A, plays an important role. TPX2 was phosphorylated by Aurora A during mitosis. Its phospho-null mutant caused short metaphase spindles coupled with low microtubule flux rate. Interestingly, phosphorylation of TPX2 regulated its interaction with CLASP1 but not Kif2a.|This suggests that TPX2 phosphorylation positively regulates the function of CLASP1.| This is in accord with a phosphoproteomics study that identified S121 and S125 as potential phosphorylation sites for Aurora A in mitotic HeLa cells |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
AURKA | down-regulates activity 
phosphorylation
|
PIN1 |
0.257 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202487 |
Ser16 |
PGWEKRMsRSSGRVY |
Homo sapiens |
|
| pmid |
sentence |
| 23970419 |
Here, we found that aurora a can interact with and phosphorylate pin1 at ser16, which suppresses the g2/m function of pin1 by disrupting its binding ability and mitotic entry. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | up-regulates activity
phosphorylation
|
LDHB |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277493 |
Ser162 |
PKHRVIGsGCNLDSA |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 31804482 |
Aurora-A-mediated phosphorylation of LDHB serine 162 significantly increases its activity in reducing pyruvate to lactate, which efficiently promotes NAD+ regeneration, glycolytic flux, lactate production and bio-synthesis with glycolytic intermediates. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | up-regulates activity
phosphorylation
|
FANCA |
0.48 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277263 |
Ser165 |
HSMFSRLsFCQELWK |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 27398318 |
E detected interactions between Aurora A kinase and FANCA protein, one of the components of the FA nuclear core complex. These results suggest that S165 phosphorylation by Aurora A kinase is required for proper activation of the FA/BRCA pathway in response to DNA damage. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | up-regulates
phosphorylation
|
CETN2 |
0.495 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-174686 |
Ser170 |
LRIMKKTsLY |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 21731694 |
Our studies show that aurora a phosphorylates centrin at serine 170 in vitro and that the serine 170 phosphorylation affects the stability of centrin by regulating its interaction with apc/c. finally we demonstrated that phosphorylation of centrin serine 170 is an absolute requirement for aurora a-mediated centriole amplification. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | up-regulates
phosphorylation
|
MAPRE3 |
0.453 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187657 |
Ser176 |
MQTSGRLsNVAPPCI |
Homo sapiens |
|
| pmid |
sentence |
| 19696028 |
Aurora-a and aurora-b phosphorylate eb3 at ser-176 in a spatial and cell cycle-specific manner, respectively during mitosis two kinases, aurora-a and aurora-b, phosphorylate eb3 at ser-176, and the resulting phosphorylation disrupts the eb3-siah-1 complex. Indeed, eb3 is stabilized during mitosis and facilitates cell cycle progression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | down-regulates activity
phosphorylation
|
POU6F1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273546 |
Ser197 |
KLDITPKsAQKLKPV |
in vitro |
|
| pmid |
sentence |
| 31665313 |
Here, we report that Aurora kinase A phosphorylates mPOU at Ser197 and inhibit its DNA-binding ability. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
AURKA | up-regulates
phosphorylation
|
FADD |
0.35 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176739 |
Ser203 |
MSWNSDAsTSEAS |
Homo sapiens |
|
| pmid |
sentence |
| 21978935 |
Here, we report that aur-a phosphorylates s203 of the fas associated with death domain protein (fadd)phosphorylation of s203 by aur-a serves to prime fadd for plk1-mediated phosphorylation at s194 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | down-regulates
phosphorylation
|
RASSF1 |
0.46 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-155815 |
Ser207 |
TSVRRRTsFYLPKDA |
Homo sapiens |
|
| pmid |
sentence |
| 17563743 |
Aurora-a appears to phosphorylate rassf1a at threonine202 and/or serine203 that reside within the known microtubule-binding domain of rassf1a. Substitutions of these residues with glutamic acid at both positions, mimicking constitutive phosphorylation of rassf1a, disrupt rassf1a interactions with microtubules and abolish its ability to induce m-phase cell cycle arrest. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-155819 |
Thr206 |
GTSVRRRtSFYLPKD |
Homo sapiens |
|
| pmid |
sentence |
| 17563743 |
AuroraT-a appears to phosphorylate rassf1a at threonine202 and/or serine203 that reside within the known microtubule-binding domain of rassf1a. Substitutions of these residues with glutamic acid at both positions, mimicking constitutive phosphorylation of rassf1a, disrupt rassf1a interactions with microtubules and abolish its ability to induce m-phase cell cycle arrest. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
AURKA | down-regulates
phosphorylation
|
TP53 |
0.771 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-129809 |
Ser215 |
DRNTFRHsVVVPYEP |
Homo sapiens |
|
| pmid |
sentence |
| 15469940 |
Here we show that p53 is phosphorylated by the mitotic kinase aurora-a at serine 215. Unlike most identified phosphorylation sites of p53 that positively associate with p53 function (brooks, c. L., and gu, w. (2003) curr. Opin. Cell biol. 15, 164-171), the phosphorylation of p53 by aurora-a at ser-215 abrogates p53 dna binding and transactivation activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | up-regulates
phosphorylation
|
MBD3 |
0.289 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-93693 |
Ser24 |
REEVPRRsGLSAGHR |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 12354758 |
These results suggest that the biochemical changes of mbd3 may be intimately related to the targeting of mbd3 to centrosomes. aurora-a phosphorylates mbd3 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-93697 |
Ser85 |
RQRVRYDsSNQVKGK |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 12354758 |
These results suggest that the biochemical changes of mbd3 may be intimately related to the targeting of mbd3 to centrosomes. aurora-a phosphorylates mbd3 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
AURKA | up-regulates activity
phosphorylation
|
KCTD12 |
0.277 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273544 |
Ser243 |
ITVCGKTsLAKEVFG |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 28869606 |
In addition, Aurora A phosphorylated KCTD12 at serine 243, thereby initiating a positive feedback loop necessary for KCTD12 to exert its cancer-promoting effects. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | down-regulates quantity by destabilization
phosphorylation
|
NDEL1 |
0.587 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263159 |
Ser251 |
LTPSARIsALNIVGD |
Mus musculus |
|
| pmid |
sentence |
| 17060449 |
Here, we show that Aurora-A phosphorylates NDEL1 at Ser251 at the beginning of mitotic entry. Interestingly, NDEL1 phosphorylated by Aurora-A was rapidly downregulated thereafter by ubiquitination-mediated protein degradation. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
AURKA | down-regulates activity
phosphorylation
|
FAF1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-180887 |
Ser289 |
ITDVHMVsDSDGDDF |
Homo sapiens |
|
| pmid |
sentence |
| 18790738 |
This study reports that aurora-a (aur-a) phosphorylates fas-associated factor-1 (faf1) at ser-289 and ser-29 our findings support the negative feedback regulation of aur-a via phosphorylation of the death-promoting protein, faf1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-180891 |
Ser291 |
DVHMVSDsDGDDFED |
Homo sapiens |
|
| pmid |
sentence |
| 18790738 |
This study reports that aurora-a (aur-a) phosphorylates fas-associated factor-1 (faf1) at ser-289 and ser-29 our findings support the negative feedback regulation of aur-a via phosphorylation of the death-promoting protein, faf1 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
AURKA | up-regulates activity
phosphorylation
|
NEDD9 |
0.588 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262654 |
Ser296 |
PVARRHQsLSPNHPP |
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 16184168 |
HEF1 interacts with AurA and is required for the activation of AurA kinase. Together, these data suggest a model in which an initial interaction of HEF1 with AurA prior to mitotic entry activates AurA, which then phosphorylates HEF1, promoting dissociation of the two proteins. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | up-regulates activity
phosphorylation
|
LIMK1 |
0.265 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276399 |
Ser307 |
DRSPGAGsLGSPASQ |
in vitro |
|
| pmid |
sentence |
| 22214762 |
Here, we report a novel functional cooperativity between Aur-A and LIMK1 through mutual phosphorylation. LIMK1 is recruited to the centrosomes during early prophase and then to the spindle poles, where it colocalizes with Aur-A. Aur-A physically associates with LIMK1 and activates it through phosphorylation, which is important for its centrosomal and spindle pole localization. Aur-A also acts as a substrate of LIMK1, and the function of LIMK1 is important for its specific localization and regulation of spindle morphology. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
AURKA | up-regulates
phosphorylation
|
BRCA1 |
0.663 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123065 |
Ser308 |
KAEFCNKsKQPGLAR |
Homo sapiens |
|
| pmid |
sentence |
| 14990569 |
Previous studies have shown that the brca1 breast cancer tumor suppressor also localizes to the centrosome and that brca1 inactivation results in loss of the g(2)-m checkpoint. We demonstrate here that aurora-a physically binds to and phosphorylates brca1. We propose that brca1 phosphorylation by aurora-a plays a role in g(2) to m transition of cell cycle |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | up-regulates activity
phosphorylation
|
TP53 |
0.771 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120836 |
Ser315 |
LPNNTSSsPQPKKKP |
Homo sapiens |
|
| pmid |
sentence |
| 24173284 |
The N-terminus of E2F1 can interact directly with a region towards the C-terminus of p53, resulting in increased nuclear retention of p53 and p53-mediated transcription and apoptosis. This is inhibited by competition between p53 and cyclin A at the binding site within E2F19,10. The interaction between p53 and E2F1 is enhanced by phosphorylation of p53 on Ser315, a residue within the E2F1 binding region that is phosphorylated by cell cycle kinases such as cdk1, cdk2, cdk9 and Aurora kinase A |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | up-regulates activity
phosphorylation
|
WDR62 |
0.359 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271712 |
Ser32 |
VPARRGQsSPPPAPP |
in vitro |
|
| pmid |
sentence |
| 25501809 |
AURKA activity promotes WDR62 spindle localization|We next purified recombinant full-length WDR62 (GST–WDR62-FL) for in vitro kinase assays with active AURKA and demonstrated that WDR62 was a direct phosphorylation target of AURKA|In addition, our quantitative phosphoproteomic analysis of in-vitro-phosphorylated WDR62 identified S32 and S33 as significantly phosphorylated in the presence of active AURKA|Alanine replacement of the five putative phosphorylation sites (S32/S33/S49/T50/S52-AAAAA) of WDR62 attenuated interphase microtubule association induced by AURKA coexpression |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271713 |
Ser33 |
PARRGQSsPPPAPPI |
in vitro |
|
| pmid |
sentence |
| 25501809 |
AURKA activity promotes WDR62 spindle localization|We next purified recombinant full-length WDR62 (GST–WDR62-FL) for in vitro kinase assays with active AURKA and demonstrated that WDR62 was a direct phosphorylation target of AURKA|In addition, our quantitative phosphoproteomic analysis of in-vitro-phosphorylated WDR62 identified S32 and S33 as significantly phosphorylated in the presence of active AURKA|Alanine replacement of the five putative phosphorylation sites (S32/S33/S49/T50/S52-AAAAA) of WDR62 attenuated interphase microtubule association induced by AURKA coexpression |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
AURKA | down-regulates quantity by destabilization
phosphorylation
|
SKI |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276918 |
Ser326 |
RRVPRVSsEPPASIR |
in vitro |
|
| pmid |
sentence |
| 26138431 |
Here we show that AURKA phosphorylates in vitro the transcripcional co-repressor Ski on aminoacids Ser326 and Ser383. Phosphorylations on these aminoacids decreased Ski protein half-life |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276917 |
Ser383 |
LSAFRPWsPAVSASE |
in vitro |
|
| pmid |
sentence |
| 26138431 |
Here we show that AURKA phosphorylates in vitro the transcripcional co-repressor Ski on aminoacids Ser326 and Ser383. Phosphorylations on these aminoacids decreased Ski protein half-life |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
AURKA | up-regulates activity
phosphorylation
|
SOX8 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273548 |
Ser327 |
SAPSASAsPTETGPP |
Homo sapiens |
Immature Ovarian Follicle |
| pmid |
sentence |
| 32550913 |
We showed for the first time that Aurora-A interacts directly with SOX8 and phosphorylates the protein at Ser327 to further regulate the SOX8/FOXK1 axis, which modulates cell senescence and glycolysis, ultimately leading to cisplatin resistance. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA |
phosphorylation
|
TACC3 |
0.934 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263697 |
Ser34 |
PEVTGRSsVLRVSQK |
in vitro |
|
| pmid |
sentence |
| 26134678 |
To address whether the phosphorylation state of TACC3 influenced Aurora-A binding and activation, we generated TACC3 variants in which all three Aurora-A phosphorylation sites (S34, S552 and S558)| The SA mutant had strongly reduced levels of phosphorylation compared to the individual mutations| |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263698 |
Ser552 |
GTSSFKEsALRKQSL |
in vitro |
|
| pmid |
sentence |
| 26134678 |
In humans, Aurora-A phosphorylates TACC3 on three residues (S34, S552 and S558); these sites are conserved in Maskin and the S558 equivalent site is also present in D-TACC [26,27,30]. In mammalian cells, phosphorylation of S558 promotes accumulation of TACC3 on spindle MTs |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
AURKA | up-regulates
phosphorylation
|
CDC25B |
0.711 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-139396 |
Ser353 |
VQNKRRRsVTPPEEQ |
Homo sapiens |
|
| pmid |
sentence |
| 16082213 |
We show that bypass of the g2/m checkpoint by the chk1 kinase inhibitor ucn-01 results in the activation of aurora-a and phosphorylation of cdc25b on s353 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | up-regulates
phosphorylation
|
LATS2 |
0.388 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-175939 |
Ser380 |
ATLARRDsLQKPGLE |
Homo sapiens |
|
| pmid |
sentence |
| 21822051 |
In the present study, aurora a was demonstrated to phosphorylate lats2 on serine 380 (s380) during mitosistogether, the results suggest that the aurora a-lats1/2-aurora b axis might be a novel pathway that regulates accurate mitotic progression by ensuring the proper mitotic localization of lats2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124830 |
Ser83 |
ALREIRYsLLPFANE |
Homo sapiens |
|
| pmid |
sentence |
| 15147269 |
On the basis of these observations, we conclude that s83 of lats2 is a phosphorylation target of aurora-a and this phosphorylation plays a role of the centrosomal localization of lats2. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
AURKA | up-regulates activity
phosphorylation
|
NEDD1 |
0.539 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272965 |
Ser405 |
FDDTGKSsLGDMFSP |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 31028180 |
Microtubule nucleation during central spindle assembly requires NEDD1 phosphorylation on serine 405 by Aurora A| In the absence of Aurora A, the HURP (also known as DLGAP5) and NEDD1 proteins that are involved in nucleation of microtubules fail to concentrate in the midzone. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA |
phosphorylation
|
WWC1 |
0.253 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176359 |
Ser539 |
TSLSPRSsLSSPSPP |
Homo sapiens |
|
| pmid |
sentence |
| 21878642 |
We identified the highly conserved ser(539) as the primary phosphorylation site for aurora kinases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | up-regulates activity
phosphorylation
|
TACC3 |
0.934 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262655 |
Ser558 |
ESALRKQsLYLKFDP |
Homo sapiens |
HCT-116 Cell |
| pmid |
sentence |
| 17545617 |
We show that this conserved serine on human TACC3 (Ser(558)) is also phosphorylated by Aurora A. Moreover, phosphorylation of TACC3 by Aurora A in human cells is essential for its proper localization to centrosomes and proximal mitotic spindles. Inhibition of Aurora A with the selective small molecule inhibitor MLN8054 in cultured human tumor cells resulted in mislocalization of TACC3 away from mitotic spindles in a concentration-dependent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | up-regulates quantity by stabilization
phosphorylation
|
NSD2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275512 |
Ser56 |
SKAQLSSsLQEGVMQ |
|
|
| pmid |
sentence |
| 35389552 |
Mechanistically, Aurora A phosphorylated NSD2 at S56 residue to protect the protein from cleavage and degradation, thus methylation of Aurora A and phosphorylation of NSD2 bilaterally formed a positive regulating loop. |
|
| Publications: |
1 |
| + |
AURKA | up-regulates
phosphorylation
|
MAP9 |
0.333 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-158210 |
Ser625 |
RKQKKRHsFLESEAL |
Homo sapiens |
|
| pmid |
sentence |
| 17925329 |
Asap is a novel substrate of the oncogenic mitotic kinase aurora-a: phosphorylation on ser625 is essential to spindle formation and mitosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | up-regulates quantity by stabilization
phosphorylation
|
DLGAP5 |
0.741 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262649 |
Ser627 |
VKLFSGLsVSSEGPS |
Homo sapiens |
|
| pmid |
sentence |
| 15987997 |
Phosphorylation and stabilization of HURP by Aurora-A. Four phosphorylated residues were identified, namely, HURP-S627, -S725, -S757, and -S830, with 65% amino acid sequence coverage. we propose here that Aurora-A may phosphorylate HURP and this probably attenuates the negative impact of cdk1 phosphorylation and by inhibiting subsequent proteasome activity and this will generate a longer HURP half-life. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262650 |
Ser725 |
CLSSERMsLPLLAGG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15987997 |
Phosphorylation and stabilization of HURP by Aurora-A. Four phosphorylated residues were identified, namely, HURP-S627, -S725, -S757, and -S830, with 65% amino acid sequence coverage. we propose here that Aurora-A may phosphorylate HURP and this probably attenuates the negative impact of cdk1 phosphorylation and by inhibiting subsequent proteasome activity and this will generate a longer HURP half-life. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262651 |
Ser757 |
EGMELNSsITSQDVL |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15987997 |
Phosphorylation and stabilization of HURP by Aurora-A. Four phosphorylated residues were identified, namely, HURP-S627, -S725, -S757, and -S830, with 65% amino acid sequence coverage. we propose here that Aurora-A may phosphorylate HURP and this probably attenuates the negative impact of cdk1 phosphorylation and by inhibiting subsequent proteasome activity and this will generate a longer HURP half-life. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262652 |
Ser830 |
QEHARHIsFGGNLIT |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15987997 |
Phosphorylation and stabilization of HURP by Aurora-A. Four phosphorylated residues were identified, namely, HURP-S627, -S725, -S757, and -S830, with 65% amino acid sequence coverage. we propose here that Aurora-A may phosphorylate HURP and this probably attenuates the negative impact of cdk1 phosphorylation and by inhibiting subsequent proteasome activity and this will generate a longer HURP half-life. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
AURKA | up-regulates quantity by stabilization
phosphorylation
|
AURKAIP1 |
0.669 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262648 |
Ser70 |
MLVPRKMsVSPLESW |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 17957726 |
AIP is phosphorylated on Serine 70 by Aurora‐A but not Aurora‐B and expression of phosphorylation mimic mutant of AIP results in prolonged protein stability compared to unphosphorylatable mutant. Phosphorylation of AIP Prolongs its Protein Stability |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | down-regulates quantity by destabilization
phosphorylation
|
BCL2L11 |
0.384 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276247 |
Ser93 |
SSLLSRSsSGYFSFD |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 23912711 |
We observed that BimEL is phosphorylated by Aurora A early in mitosis and reversed by PP2A after mitotic exit. Aurora A phosphorylation stimulated binding of BimEL to the F-box protein beta-transducin repeat containing E3 ubiquitin protein ligase and promoted ubiquitination and degradation of BimEL. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276248 |
Ser94 |
SLLSRSSsGYFSFDT |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 23912711 |
We observed that BimEL is phosphorylated by Aurora A early in mitosis and reversed by PP2A after mitotic exit. Aurora A phosphorylation stimulated binding of BimEL to the F-box protein beta-transducin repeat containing E3 ubiquitin protein ligase and promoted ubiquitination and degradation of BimEL. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276246 |
Ser98 |
RSSSGYFsFDTDRSP |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 23912711 |
We observed that BimEL is phosphorylated by Aurora A early in mitosis and reversed by PP2A after mitotic exit. Aurora A phosphorylation stimulated binding of BimEL to the F-box protein beta-transducin repeat containing E3 ubiquitin protein ligase and promoted ubiquitination and degradation of BimEL. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
AURKA | down-regulates quantity by destabilization
phosphorylation
|
PHLDA1 |
0.423 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273545 |
Ser95 |
PLCLLRVsLLCALRA |
Homo sapiens |
MDA-MB-157 Cell |
| pmid |
sentence |
| 21807936 |
Aurora A directly phosphorylates PHLDA1 leading to its degradation. Aurora A phosphorylates PHLDA1 at Ser 98. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | down-regulates activity
phosphorylation
|
ARHGEF2 |
0.339 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276061 |
Ser960 |
SRLSPPHsPRDFTRM |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 17488622 |
The mitotic kinases Aurora A/B and Cdk1/Cyclin B phosphorylate GEF-H1, thereby inhibiting GEF-H1 catalytic activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | up-regulates
phosphorylation
|
PARD3 |
0.358 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-188398 |
Ser962 |
SSRSGREsVSTASDQ |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 19812038 |
Aurora a interacts directly with the atypical protein kinase c binding domain of par3 and phosphorylates it at serine 962. The phosphorylation of par3 at serine 962 contributes to its function in the establishment of neuronal polarity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | up-regulates
phosphorylation
|
PLK1 |
0.649 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179422 |
Thr210 |
YDGERKKtLCGTPNY |
Homo sapiens |
|
| pmid |
sentence |
| 18615013 |
We find that aurora a (aurka) can directly phosphorylate plk1 on thr 210;activation of plk1 requires phosphorylation of a conserved threonine residue (thr 210). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | up-regulates activity
phosphorylation
|
ALDH1A1 |
0.381 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276750 |
Thr267 |
KSNLKRVtLELGGKS |
in vitro |
|
| pmid |
sentence |
| 28193222 |
AURKA phosphorylates ALDH1A1 at three critical residues which exert a multifaceted regulation over its level, enzymatic activity, and quaternary structure. While all three phosphorylation sites contribute to its increased stability, T267 phosphorylation primarily regulates ALDH1A1 activity. AURKA-mediated phosphorylation rapidly dissociates tetrameric ALDH1A1 into a highly active monomeric species. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276748 |
Thr442 |
KDIDKAItISSALQA |
in vitro |
|
| pmid |
sentence |
| 28193222 |
AURKA phosphorylates ALDH1A1 at three critical residues which exert a multifaceted regulation over its level, enzymatic activity, and quaternary structure. While all three phosphorylation sites contribute to its increased stability, T267 phosphorylation primarily regulates ALDH1A1 activity. AURKA-mediated phosphorylation rapidly dissociates tetrameric ALDH1A1 into a highly active monomeric species. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276749 |
Thr493 |
YTEVKTVtVKISQKN |
in vitro |
|
| pmid |
sentence |
| 28193222 |
AURKA phosphorylates ALDH1A1 at three critical residues which exert a multifaceted regulation over its level, enzymatic activity, and quaternary structure. While all three phosphorylation sites contribute to its increased stability, T267 phosphorylation primarily regulates ALDH1A1 activity. AURKA-mediated phosphorylation rapidly dissociates tetrameric ALDH1A1 into a highly active monomeric species. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
AURKA | up-regulates
phosphorylation
|
AURKA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-205106 |
Thr288 |
APSSRRTtLCGTLDY |
Homo sapiens |
|
| pmid |
sentence |
| 24867643 |
The upstream pak1 kinase can phosphorylate aurora a at t288, autophosphorylation appears to be the essential mode of activation. Our experiments suggest that phosphorylation of t288 is important for regulation of the aurora2 kinase both for its activity and its stability |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK1 | up-regulates
phosphorylation
|
AURKA |
0.392 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-205110 |
Thr288 |
APSSRRTtLCGTLDY |
Homo sapiens |
|
| pmid |
sentence |
| 24867643 |
The upstream pak1 kinase can phosphorylate aurora a at t288, autophosphorylation appears to be the essential mode of activation. Our experiments suggest that phosphorylation of t288 is important for regulation of the aurora2 kinase both for its activity and its stability |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKACA | up-regulates activity
phosphorylation
|
AURKA |
0.49 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250337 |
Thr288 |
APSSRRTtLCGTLDY |
in vitro |
|
| pmid |
sentence |
| 11039908 |
Aurora2 is regulated by phosphorylation. phosphorylation occurs on a conserved residue, Threonine 288, within the activation loop of the catalytic domain of the kinase and results in a significant increase in the enzymatic activity. Threonine 288 resides within a consensus motif for the cAMP dependent kinase and can be phosphorylated by PKA in vitro. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
AURKA | up-regulates quantity
phosphorylation
|
SECISBP2L |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273547 |
Thr573 |
IAKLKRPtALKKVIL |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 31314582 |
To explore the underlying mechanisms, we found that SLAN, a potential tumor suppressor, served as a substrate of Aurora-A and knockdown of SLAN induced immature cytokinesis. Aurora-A phosphorylates SLAN at T573 under the help of the scaffold protein 14-3-3η. Intriguingly, SLAN T573D or T573E inactivated and T573A activated the key cytokinesis regulator RhoA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | up-regulates activity
phosphorylation
|
KIF4A |
0.429 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265993 |
Thr799 |
PPKLRRRtFSLTEVR |
in vitro |
|
| pmid |
sentence |
| 31881080 |
We show that Aurora A phosphorylates the condensin I-dependent pool of KIF4A and thus actively promotes chromosome congression from the spindle poles to the metaphase plate. In vitro kinase assays showed that recombinant KIF4A can be phosphorylated by Aurora A and that this activity is inhibited by the specific Aurora A inhibitor MLN8537 (Fig. 7 C). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
AURKA | up-regulates activity
phosphorylation
|
TIFA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273551 |
Thr9 |
TSFEDADtEETVTCL |
Homo sapiens |
Acute Myeloid Leukemia Cell |
| pmid |
sentence |
| 28069801 |
Here, we report that Aurora A is essential for Thr9 phosphorylation of the TRAF-interacting protein TIFA, triggering activation of the NF-κB survival pathway in AML. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Cullin 3-RBX1-Skp1 | up-regulates activity
monoubiquitination
|
AURKA |
0.419 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272023 |
|
|
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 23213400 |
We identify Aurora-A as a KLHL18-interacting partner. Overexpression of KLHL18 and CUL3 promotes Aurora-A ubiquitylation in vivo, and the CUL3-KLHL18-ROC1 ligase ubiquitylates Aurora-A in vitro. Our study reveals that the CUL3-KLHL18 ligase is required for timely entry into mitosis, as well as for the activation of Aurora-A at centrosomes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PP1 | down-regulates
dephosphorylation
|
AURKA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264651 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11551964 |
Pp1 is shown to dephosphorylate active stk15 and abolish its activity in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AMG 900 | down-regulates
chemical inhibition
|
AURKA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189492 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | up-regulates activity
phosphorylation
|
INCENP |
0.714 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252047 |
|
|
Drosophila melanogaster |
|
| pmid |
sentence |
| 16824953 |
INCENP is phosphorylated by Aurora B and activates the kinase in a positive feedback loop |
|
| Publications: |
1 |
Organism: |
Drosophila Melanogaster |
| + |
BORA | up-regulates
binding
|
AURKA |
0.717 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-148661 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16890155 |
Both drosophila and human bora can bind to aurora-a and activate the kinase in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CEP192 | up-regulates activity
binding
|
AURKA |
0.787 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266406 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26012549 |
These findings demonstrated that Cep192 mediates the AurA-Plk1 interaction and that the formation of the Cep192-AurA-Plk1 complex could be important for activating AurA and Plk1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ENMD-2076 | down-regulates
chemical inhibition
|
AURKA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-191466 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | up-regulates activity
phosphorylation
|
SGO1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252046 |
|
|
in vitro |
|
| pmid |
sentence |
| 16824953 |
Loss of INCENP/Aurora B in Mitosis Correlates with Delocalization of MEI-S332|MEI-S332 Is Phosphorylated by Aurora B In Vitro|Of these, MEI-S332S124,125,126A was a poor substrate for Aurora B kinase in vitro |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
NEDD9 | up-regulates activity
binding
|
AURKA |
0.588 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262653 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16184168 |
HEF1 interacts with AurA and is required for the activation of AurA kinase. Together, these data suggest a model in which an initial interaction of HEF1 with AurA prior to mitotic entry activates AurA, which then phosphorylates HEF1, promoting dissociation of the two proteins. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | down-regulates activity
phosphorylation
|
KNSTRN |
0.264 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252052 |
|
|
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 22535524 |
The protein astrin has been shown to remove Kif2b from kinetochores in metaphase through competitive binding of CLASP1 (Manning et al., 2010 blue right-pointing triangle). During prometaphase, Aurora B kinase activity prevents astrin from localizing to kinetochores (Manning et al., 2010 blue right-pointing triangle; Schmidt et al., 2010 blue right-pointing triangle). This permits Kif2b to localize to kinetochores to destabilize k-MT attachments to execute error correction through Plk1-dependent recruitment and activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
APC-c | down-regulates quantity by destabilization
polyubiquitination
|
AURKA |
0.42 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272612 |
|
|
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 12023018 |
We previously showed that human Aurora-A is turned over through the anaphase promoting complex/cyclosome (APC/C)–ubiquitin–proteasome pathway. The association of two distinct WD40 repeat proteins known as Cdc20 and Cdh1, respectively, sequentially activates the APC/C. The present study shows that Aurora-A degradation is dependent on hCdh1 in vivo, not on hCdc20, and that Aurora-A is targeted for proteolysis through distinct structural features of the destruction box, the KEN box motifs and its kinase activity. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
UBXN2B | down-regulates activity
binding
|
AURKA |
0.309 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265042 |
|
|
Caenorhabditis elegans |
|
| pmid |
sentence |
| 23649807 |
The UBXN-2/p37/p47 adaptors of CDC-48/p97 regulate mitosis by limiting the centrosomal recruitment of Aurora A.|We found that UBXN-2 and CDC-48 coimmunoprecipitated with AIR-1 from embryonic extracts |
|
| Publications: |
1 |
Organism: |
Caenorhabditis Elegans |
| + |
CCT129202 | down-regulates
chemical inhibition
|
AURKA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-190877 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KLHL18 | up-regulates activity
binding
|
AURKA |
0.375 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272021 |
|
|
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 23213400 |
We identify Aurora-A as a KLHL18-interacting partner. Overexpression of KLHL18 and CUL3 promotes Aurora-A ubiquitylation in vivo, and the CUL3-KLHL18-ROC1 ligase ubiquitylates Aurora-A in vitro. Our study reveals that the CUL3-KLHL18 ligase is required for timely entry into mitosis, as well as for the activation of Aurora-A at centrosomes.We also noticed that overexpression of both CUL3 and KLHL18 stimulated mono-ubiquitylation of Aurora-A as well (Fig. 8A,B). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
[4-[2-(1H-indazol-3-yl)ethenyl]phenyl]-(1-piperazinyl)methanone | down-regulates activity
chemical inhibition
|
AURKA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258232 |
|
|
in vitro |
|
| pmid |
sentence |
| 22037378 |
Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. | The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PF-03814735 | down-regulates
chemical inhibition
|
AURKA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-205950 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PHA-680632 | down-regulates
chemical inhibition
|
AURKA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-206097 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FZR1 | down-regulates quantity by destabilization
binding
|
AURKA |
0.542 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272610 |
|
|
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 12023018 |
We previously showed that human Aurora-A is turned over through the anaphase promoting complex/cyclosome (APC/C)–ubiquitin–proteasome pathway. The association of two distinct WD40 repeat proteins known as Cdc20 and Cdh1, respectively, sequentially activates the APC/C. The present study shows that Aurora-A degradation is dependent on hCdh1 in vivo, not on hCdc20, and that Aurora-A is targeted for proteolysis through distinct structural features of the destruction box, the KEN box motifs and its kinase activity. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
VCP | down-regulates activity
binding
|
AURKA |
0.319 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265044 |
|
|
Caenorhabditis elegans |
|
| pmid |
sentence |
| 23649807 |
The UBXN-2/p37/p47 adaptors of CDC-48/p97 regulate mitosis by limiting the centrosomal recruitment of Aurora A.|We found that UBXN-2 and CDC-48 coimmunoprecipitated with AIR-1 from embryonic extracts |
|
| Publications: |
1 |
Organism: |
Caenorhabditis Elegans |
| + |
4-[[9-chloro-7-(2,6-difluorophenyl)-5H-pyrimido[5,4-d][2]benzazepin-2-yl]amino]benzoic acid | down-regulates activity
chemical inhibition
|
AURKA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258250 |
|
|
in vitro |
|
| pmid |
sentence |
| 22037378 |
Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. | The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
3-[4-[4-[2-[3-[(dimethylamino)methyl]phenyl]-1H-pyrrolo[2,3-b]pyridin-4-yl]-1-ethyl-3-pyrazolyl]phenyl]-1,1-dimethylurea | down-regulates activity
chemical inhibition
|
AURKA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262225 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19567821 |
The protein kinases, Aurora A, B, and C have critical roles in the regulation of mitosis and are frequently overexpressed or amplified in human tumors. GSK1070916, is a novel ATP competitive inhibitor that is highly potent and selective for Aurora B/C kinases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
N-[5-[(2R)-2-methoxy-1-oxo-2-phenylethyl]-4,6-dihydro-1H-pyrrolo[3,4-c]pyrazol-3-yl]-4-(4-methyl-1-piperazinyl)benzamide | down-regulates
chemical inhibition
|
AURKA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-191274 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA |
phosphorylation
|
Histone H3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265356 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 12234980 |
In the present study, chromosome number instability and increased tumor invasiveness were noted in constitutively AIM-1-overexpressing cells in vivo. Increased mitotic Ser-10 phosphorylation was also observed in various colorectal tumor cells with high AIM-1 expression levels. These data suggest that increased H3 histone phosphorylation as a result of AIM-1 overexpression is a major precipitating factor of chromosome instability and, thus, may play a role in carcinogenesis. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PPP1CA | down-regulates
dephosphorylation
|
AURKA |
0.446 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-110411 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11551964 |
Pp1 is shown to dephosphorylate active stk15 and abolish its activity in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CYC-116 | down-regulates
chemical inhibition
|
AURKA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-191221 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
4-[[9-chloro-7-(2-fluoro-6-methoxyphenyl)-5H-pyrimido[5,4-d][2]benzazepin-2-yl]amino]-2-methoxybenzoic acid | down-regulates
chemical inhibition
|
AURKA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-194527 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
4-(3-chloro-2-fluorophenoxy)-1-[[6-(2-thiazolylamino)-2-pyridinyl]methyl]-1-cyclohexanecarboxylic acid | down-regulates
chemical inhibition
|
AURKA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-194411 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDR2 | up-regulates quantity by expression 
transcriptional regulation
|
AURKA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252023 |
|
|
|
|
| pmid |
sentence |
| 20383333 |
Additionally, cdr2 knockdown lead to a decrease (Table 3) in four other transcripts (AURKA, CENPE, SPC25 and TTK), which are involved in kinetochore and spindle biology |
|
| Publications: |
1 |
| + |
ZM447439 | down-regulates
chemical inhibition
|
AURKA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-207920 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AT9283 | down-regulates
chemical inhibition
|
AURKA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-190011 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
N-[4-[[4-(4-methyl-1-piperazinyl)-6-[(5-methyl-1H-pyrazol-3-yl)amino]-2-pyrimidinyl]thio]phenyl]cyclopropanecarboxamide | down-regulates
chemical inhibition
|
AURKA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-207666 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CCT137690 | down-regulates
chemical inhibition
|
AURKA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-190892 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
4-[[5-amino-1-[(2,6-difluorophenyl)-oxomethyl]-1,2,4-triazol-3-yl]amino]benzenesulfonamide | down-regulates
chemical inhibition
|
AURKA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-193531 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
N-(2-chlorophenyl)-4-[[2-[4-[2-(4-ethyl-1-piperazinyl)-2-oxoethyl]anilino]-5-fluoro-4-pyrimidinyl]amino]benzamide | down-regulates
chemical inhibition
|
AURKA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-190029 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | down-regulates activity
phosphorylation
|
GSK3B/Axin/APC |
0.348 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-227923 |
|
|
Homo sapiens |
MKN-45 Cell |
| pmid |
sentence |
| 19060929 |
The recombinant human aurka protein phosphorylated the gsk-3beta protein at ser 9 in a concentration-dependent manner, in vitro. The phosphorylation of beta-catenin (ser33/37/thr41) by gsk-3beta is known to target beta-catenin towards degradation. In line with our findings, the increase in phospho-gsk-3beta level was accompanied by a significant decrease in beta-catenin phosphorylation (ser33/37/thr41) and accumulation of beta-catenin protein. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SNS-314 Mesylate | down-regulates
chemical inhibition
|
AURKA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-207099 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
4-[[9-chloro-7-(2,6-difluorophenyl)-5H-pyrimido[5,4-d][2]benzazepin-2-yl]amino]benzoic acid | down-regulates
chemical inhibition
|
AURKA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-194518 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
anthra[1,9-cd]pyrazol-6(2H)-one | down-regulates
chemical inhibition
|
AURKA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-170611 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21159646 |
In comparison, in the same assay conditions, the previously reported mps1 inhibitor sp600125 (13) was 10-fold less potent than nms-p715 on mps1 and, in addition, it was highly unspecific, being more active on at least 12 kinases including mitotic kinases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CHFR | down-regulates quantity by destabilization
polyubiquitination
|
AURKA |
0.483 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271463 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17442268 |
Chfr, a mitotic stress checkpoint, plays an important role in cell cycle progression, tumor suppression and the processes that require the E3 ubiquitin ligase activity mediated by the RING finger domain. Chfr stimulates the formation of polyubiquitin chains by ub-conjugating enzymes, and induces the proteasome-dependent degradation of a number of cellular proteins including Plk1 and Aurora A. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
N-[4-[[4-(4-methyl-1-piperazinyl)-6-[(5-methyl-1H-pyrazol-3-yl)amino]-2-pyrimidinyl]thio]phenyl]cyclopropanecarboxamide | down-regulates activity
chemical inhibition
|
AURKA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258303 |
|
|
in vitro |
|
| pmid |
sentence |
| 22037378 |
Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. | The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
INCENP | up-regulates activity
binding
|
AURKA |
0.714 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252048 |
|
|
Drosophila melanogaster |
|
| pmid |
sentence |
| 16824953 |
INCENP is phosphorylated by Aurora B and activates the kinase in a positive feedback loop |
|
| Publications: |
1 |
Organism: |
Drosophila Melanogaster |
| + |
LIMK1 | up-regulates activity
phosphorylation
|
AURKA |
0.265 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276400 |
|
|
in vitro |
|
| pmid |
sentence |
| 22214762 |
Here, we report a novel functional cooperativity between Aur-A and LIMK1 through mutual phosphorylation. LIMK1 is recruited to the centrosomes during early prophase and then to the spindle poles, where it colocalizes with Aur-A. Aur-A physically associates with LIMK1 and activates it through phosphorylation, which is important for its centrosomal and spindle pole localization. Aur-A also acts as a substrate of LIMK1, and the function of LIMK1 is important for its specific localization and regulation of spindle morphology. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
AURKA
- 
- 