+ |
AURKB | down-regulates
phosphorylation
|
DSN1 |
0.64 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-165546 |
Ser100 |
RQSWRRAsMKETNRR |
Homo sapiens |
|
pmid |
sentence |
20471944 |
To determine whether the combinatorial regulation of the kmn network by aurora b observed in vitro is critical to controlling kinetochore-microtubule attachments in vivo, we next investigated the effect of the phosphomimetic (to aspartate) and nonphosphorylatable (to alanine) mutants of dsn1, knl1, and ndc80 in vertebrate cells. We predicted that both types of mutations in critical phosphorylation sites would affect chromosome segregation, since preventing the inactivation of inappropriately attached kinetochores by aurora b (in the nonphosphorylatable mutant) or constitutively inactivating this attachment (in the phosphomimetic mutant). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-165550 |
Ser109 |
KETNRRKsLHPIHQG |
Homo sapiens |
|
pmid |
sentence |
20471944 |
To determine whether the combinatorial regulation of the kmn network by aurora b observed in vitro is critical to controlling kinetochore-microtubule attachments in vivo, we next investigated the effect of the phosphomimetic (to aspartate) and nonphosphorylatable (to alanine) mutants of dsn1, knl1, and ndc80 in vertebrate cells. We predicted that both types of mutations in critical phosphorylation sites would affect chromosome segregation, since preventing the inactivation of inappropriately attached kinetochores by aurora b (in the nonphosphorylatable mutant) or constitutively inactivating this attachment (in the phosphomimetic mutant). |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
AURKB | up-regulates activity
phosphorylation
|
HASPIN |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263137 |
Ser108 |
WKLRARPsLTVTPRR |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
21658950 |
Here, we show that Aurora B phosphorylates Haspin to promote generation of H3T3ph and that Aurora B kinase activity is required for normal chromosomal localization of the CPC, indicating an intimate linkage between Aurora B and Haspin functions in mitosis. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263138 |
Ser143 |
PPFPSRDsGRLSPDL |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
21658950 |
Here, we show that Aurora B phosphorylates Haspin to promote generation of H3T3ph and that Aurora B kinase activity is required for normal chromosomal localization of the CPC, indicating an intimate linkage between Aurora B and Haspin functions in mitosis. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262656 |
Ser143 |
PPFPSRDsGRLSPDL |
Homo sapiens |
|
pmid |
sentence |
21658950 |
Phosphorylation by Aurora B is required for full Haspin activity toward H3T3 in mitosis |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263139 |
Ser93 |
RVPKDRPsLTVTPKR |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
21658950 |
Here, we show that Aurora B phosphorylates Haspin to promote generation of H3T3ph and that Aurora B kinase activity is required for normal chromosomal localization of the CPC, indicating an intimate linkage between Aurora B and Haspin functions in mitosis. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262657 |
Ser93 |
RVPKDRPsLTVTPKR |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
21658950 |
Phosphorylation by Aurora B is required for full Haspin activity toward H3T3 in mitosis |
|
Publications: |
5 |
Organism: |
Homo Sapiens |
+ |
AURKB | up-regulates activity
phosphorylation
|
H3-3A |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-118890 |
Ser11 |
TKQTARKsTGGKAPR |
Homo sapiens |
|
pmid |
sentence |
14583461 |
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. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-70420 |
Ser11 |
TKQTARKsTGGKAPR |
Homo sapiens |
|
pmid |
sentence |
10464286 |
Phosphorylation at ser-11 (h3s10ph) by aurkb is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-98293 |
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: |
3 |
Organism: |
Homo Sapiens |
+ |
AURKB | up-regulates activity
phosphorylation
|
H3C1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-118894 |
Ser11 |
TKQTARKsTGGKAPR |
Homo sapiens |
|
pmid |
sentence |
14583461 |
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. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-98297 |
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: |
2 |
Organism: |
Homo Sapiens |
+ |
AURKB | down-regulates
phosphorylation
|
KIF2C |
0.72 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-155894 |
Ser111 |
KESLRSRsTRMSTVS |
Homo sapiens |
|
pmid |
sentence |
17567953 |
Here, we show that the binding of mcak to chromosome arms is also regulated by aurora b and that aurora b-dependent chromosome arm and centromere localization is regulated by distinct two-site phosphoregulatory mechanisms. Mcak association with chromosome arms is promoted by phosphorylation of t95 on mcak, whereas phosphorylation of s196 on mcak promotes dissociation from the arms. Although targeting of mcak to centromeres requires phosphorylation of s110 on mcak, dephosphorylation of t95 on mcak increases the binding of mcak to centromeres. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-155898 |
Ser192 |
VNSVRRKsCLVKEVE |
Homo sapiens |
|
pmid |
sentence |
17567953 |
Here, we show that the binding of mcak to chromosome arms is also regulated by aurora b and that aurora b-dependent chromosome arm and centromere localization is regulated by distinct two-site phosphoregulatory mechanisms. Mcak association with chromosome arms is promoted by phosphorylation of t95 on mcak, whereas phosphorylation of s196 on mcak promotes dissociation from the arms. Although targeting of mcak to centromeres requires phosphorylation of s110 on mcak, dephosphorylation of t95 on mcak increases the binding of mcak to centromeres. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
AURKB | down-regulates
phosphorylation
|
DES |
0.526 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-100107 |
Ser12 |
YSSSQRVsSYRRTFG |
in vitro |
|
pmid |
sentence |
12686604 |
We report here that aurora-b phosphorylates gfap and desmin in vitro, and this phosphorylation leads to a reduction in filament forming ability. In the present study, we found aurora-b phosphorylates desmin at ser-11, thr-16, and ser-59, in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-100111 |
Ser60 |
VYQVSRTsGGAGGLG |
in vitro |
|
pmid |
sentence |
12686604 |
We report here that aurora-b phosphorylates gfap and desmin in vitro, and this phosphorylation leads to a reduction in filament forming ability. In the present study, we found aurora-b phosphorylates desmin at ser-11, thr-16, and ser-59, in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-100115 |
Thr17 |
RVSSYRRtFGGAPGF |
in vitro |
|
pmid |
sentence |
12686604 |
We report here that aurora-b phosphorylates gfap and desmin in vitro, and this phosphorylation leads to a reduction in filament forming ability. In the present study, we found aurora-b phosphorylates desmin at ser-11, thr-16, and ser-59, in vitro. |
|
Publications: |
3 |
Organism: |
In Vitro |
+ |
AURKB | down-regulates activity
phosphorylation
|
CDCA5 |
0.614 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276123 |
Ser126 |
NPEAESSsKEGELDA |
in vitro |
|
pmid |
sentence |
23901111 |
Here we show that the mitotic kinases Aurora B and Cyclin-dependent kinase 1 (Cdk1) destabilize interactions between Sororin and the cohesin subunit precocious dissociation of sisters protein 5 (Pds5) by phosphorylating Sororin, leading to release of acetylated cohesin from chromosome arms and loss of cohesion. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276114 |
Ser139 |
DARDLEMsKKVRRSY |
in vitro |
|
pmid |
sentence |
23901111 |
Here we show that the mitotic kinases Aurora B and Cyclin-dependent kinase 1 (Cdk1) destabilize interactions between Sororin and the cohesin subunit precocious dissociation of sisters protein 5 (Pds5) by phosphorylating Sororin, leading to release of acetylated cohesin from chromosome arms and loss of cohesion. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276113 |
Ser164 |
TSTPGRRsCFGFEGL |
in vitro |
|
pmid |
sentence |
23901111 |
Here we show that the mitotic kinases Aurora B and Cyclin-dependent kinase 1 (Cdk1) destabilize interactions between Sororin and the cohesin subunit precocious dissociation of sisters protein 5 (Pds5) by phosphorylating Sororin, leading to release of acetylated cohesin from chromosome arms and loss of cohesion. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276116 |
Ser33 |
LRRSQRKsGSELPSI |
in vitro |
|
pmid |
sentence |
23901111 |
Here we show that the mitotic kinases Aurora B and Cyclin-dependent kinase 1 (Cdk1) destabilize interactions between Sororin and the cohesin subunit precocious dissociation of sisters protein 5 (Pds5) by phosphorylating Sororin, leading to release of acetylated cohesin from chromosome arms and loss of cohesion. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276119 |
Ser83 |
PRRSPRIsFFLEKEN |
in vitro |
|
pmid |
sentence |
23901111 |
Here we show that the mitotic kinases Aurora B and Cyclin-dependent kinase 1 (Cdk1) destabilize interactions between Sororin and the cohesin subunit precocious dissociation of sisters protein 5 (Pds5) by phosphorylating Sororin, leading to release of acetylated cohesin from chromosome arms and loss of cohesion. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276117 |
Thr151 |
RSYSRLEtLGSASTS |
in vitro |
|
pmid |
sentence |
23901111 |
Here we show that the mitotic kinases Aurora B and Cyclin-dependent kinase 1 (Cdk1) destabilize interactions between Sororin and the cohesin subunit precocious dissociation of sisters protein 5 (Pds5) by phosphorylating Sororin, leading to release of acetylated cohesin from chromosome arms and loss of cohesion. |
|
Publications: |
6 |
Organism: |
In Vitro |
+ |
AURKB | down-regulates activity
phosphorylation
|
GFAP |
0.449 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-100165 |
Ser13 |
ITSAARRsYVSSGEM |
in vitro |
|
pmid |
sentence |
12686604 |
We report here that aurora-b phosphorylates gfap and desmin in vitro, and this phosphorylation leads to a reduction in filament forming ability. The sites phosphorylated by aurora-b;thr-7/ser-13/ser-38 of gfap, and thr-16 of desmin are common with those related to rho-associated kinase (rho-kinase), which has been reported to phosphorylate gfap and desmin at cleavage furrow during cytokinesis. We identified ser-59 of desmin to be a specific site phosphorylated by aurora-b in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-100169 |
Ser38 |
LGPGTRLsLARMPPP |
in vitro |
|
pmid |
sentence |
12686604 |
We report here that aurora-b phosphorylates gfap and desmin in vitro, and this phosphorylation leads to a reduction in filament forming ability. The sites phosphorylated by aurora-b;thr-7/ser-13/ser-38 of gfap, and thr-16 of desmin are common with those related to rho-associated kinase (rho-kinase), which has been reported to phosphorylate gfap and desmin at cleavage furrow during cytokinesis. We identified ser-59 of desmin to be a specific site phosphorylated by aurora-b in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-100173 |
Thr7 |
tSAARRSY |
in vitro |
|
pmid |
sentence |
12686604 |
We report here that aurora-b phosphorylates gfap and desmin in vitro, and this phosphorylation leads to a reduction in filament forming ability. The sites phosphorylated by aurora-b;thr-7/ser-13/ser-38 of gfap, and thr-16 of desmin are common with those related to rho-associated kinase (rho-kinase), which has been reported to phosphorylate gfap and desmin at cleavage furrow during cytokinesis. We identified ser-59 of desmin to be a specific site phosphorylated by aurora-b in vitro. |
|
Publications: |
3 |
Organism: |
In Vitro |
+ |
AURKB |
phosphorylation
|
MYBBP1A |
0.399 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-163903 |
Ser1303 |
ARKKARLsLVIRSPS |
Homo sapiens |
|
pmid |
sentence |
20177074 |
We identified mybbp1a as a novel aurora b substrate and serine 1303 as the major phosphorylation site |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AURKB | up-regulates activity
phosphorylation
|
TP53BP1 |
0.421 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264411 |
Ser1342 |
GPLRGKTsGTEPADF |
Homo sapiens |
U2-OS Cell |
pmid |
sentence |
28415769 |
Here we report for the first time that tumor suppressor p53-binding protein 1 (53BP1) is phosphorylated at serine 1342 (S1342) by Aurora kinase B both in vitro and in human cells, which is required for optimal recruitment of 53BP1 at kinetochores. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AURKB | down-regulates
phosphorylation
|
NSUN2 |
0.709 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-152001 |
Ser139 |
SRKILRKsPHLEKFH |
Homo sapiens |
|
pmid |
sentence |
17215513 |
Aurora-b phosphorylated nsun2 at ser139. Aurora-b-phosphorylation and the phosphorylation-mimic mutation (s139e) suppressed methyltransferase activities of nsun2. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AURKB | up-regulates
phosphorylation
|
ATM |
0.444 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-177280 |
Ser1403 |
CHKTKLKsILEILSK |
Homo sapiens |
|
pmid |
sentence |
22099307 |
Aurora-b mediated atm serine 1403 phosphorylation is required for mitotic atm activation and the spindle checkpoint |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AURKB | up-regulates activity
phosphorylation
|
RACGAP1 |
0.772 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250586 |
Ser144 |
NAGNKRLsTIDESGS |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
14744859 |
It was found that the 5A fragment in which five Ser/Thr residues were substituted with Ala (S144A/T145A/S185A/T186A/S187A) fully prevented phosphorylation (Fig. 5B), confirming that Aurora B primarily phosphorylates five Ser/Thr residues in the basic region of MgcRacGAP. | the strong phosphorylation of the basic region of MgcRacGAP by Aurora B kinase was demonstrated, and this phosphorylation prevents the inhibition of MgcRacGAP GAP activity by PRC1 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250587 |
Ser185 |
KKREKRRsTSRQFVD |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
14744859 |
It was found that the 5A fragment in which five Ser/Thr residues were substituted with Ala (S144A/T145A/S185A/T186A/S187A) fully prevented phosphorylation (Fig. 5B), confirming that Aurora B primarily phosphorylates five Ser/Thr residues in the basic region of MgcRacGAP. | the strong phosphorylation of the basic region of MgcRacGAP by Aurora B kinase was demonstrated, and this phosphorylation prevents the inhibition of MgcRacGAP GAP activity by PRC1 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250588 |
Ser187 |
REKRRSTsRQFVDGP |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
14744859 |
It was found that the 5A fragment in which five Ser/Thr residues were substituted with Ala (S144A/T145A/S185A/T186A/S187A) fully prevented phosphorylation (Fig. 5B), confirming that Aurora B primarily phosphorylates five Ser/Thr residues in the basic region of MgcRacGAP. | the strong phosphorylation of the basic region of MgcRacGAP by Aurora B kinase was demonstrated, and this phosphorylation prevents the inhibition of MgcRacGAP GAP activity by PRC1 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-100569 |
Ser387 |
ETGLYRIsGCDRTVK |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
12689593 |
We also report that aurora b phosphorylates mgcracgap on serine residues and that this modification induces latent gap activity toward rhoa in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250589 |
Thr145 |
AGNKRLStIDESGSI |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
14744859 |
It was found that the 5A fragment in which five Ser/Thr residues were substituted with Ala (S144A/T145A/S185A/T186A/S187A) fully prevented phosphorylation (Fig. 5B), confirming that Aurora B primarily phosphorylates five Ser/Thr residues in the basic region of MgcRacGAP. | the strong phosphorylation of the basic region of MgcRacGAP by Aurora B kinase was demonstrated, and this phosphorylation prevents the inhibition of MgcRacGAP GAP activity by PRC1 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250590 |
Thr186 |
KREKRRStSRQFVDG |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
14744859 |
It was found that the 5A fragment in which five Ser/Thr residues were substituted with Ala (S144A/T145A/S185A/T186A/S187A) fully prevented phosphorylation (Fig. 5B), confirming that Aurora B primarily phosphorylates five Ser/Thr residues in the basic region of MgcRacGAP. | the strong phosphorylation of the basic region of MgcRacGAP by Aurora B kinase was demonstrated, and this phosphorylation prevents the inhibition of MgcRacGAP GAP activity by PRC1 |
|
Publications: |
6 |
Organism: |
Homo Sapiens |
+ |
AURKB | up-regulates activity
phosphorylation
|
RPRD1B |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265499 |
Ser145 |
KATEEKKsLKRTFQQ |
|
|
pmid |
sentence |
30518842 |
Mechanistically, we revealed that CREPT/RPRD1B interacted with Aurora B to regulate the expression of Cyclin B1 in gastric cancer cells. Interestingly, Aurora B phosphorylates S145 in a well-conserved motif of CREPT/RPRD1B. We proposed that phosphorylation of CREPT/RPRD1B by Aurora B is required for promoting the transcription of Cyclin B1 |
|
Publications: |
1 |
+ |
AURKB | down-regulates
phosphorylation
|
NDC80 |
0.842 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-165554 |
Ser15 |
SGGAGRLsMQELRSQ |
Homo sapiens |
|
pmid |
sentence |
20471944 |
To determine whether the combinatorial regulation of the kmn network by aurora b observed in vitro is critical to controlling kinetochore-microtubule attachments in vivo, we next investigated the effect of the phosphomimetic (to aspartate) and nonphosphorylatable (to alanine) mutants of dsn1, knl1, and ndc80 in vertebrate cells. We predicted that both types of mutations in critical phosphorylation sites would affect chromosome segregation, since preventing the inactivation of inappropriately attached kinetochores by aurora b (in the nonphosphorylatable mutant) or constitutively inactivating this attachment (in the phosphomimetic mutant). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-165558 |
Ser44 |
KPTFGKLsINKPTSE |
Homo sapiens |
|
pmid |
sentence |
20471944 |
To determine whether the combinatorial regulation of the kmn network by aurora b observed in vitro is critical to controlling kinetochore-microtubule attachments in vivo, we next investigated the effect of the phosphomimetic (to aspartate) and nonphosphorylatable (to alanine) mutants of dsn1, knl1, and ndc80 in vertebrate cells. We predicted that both types of mutations in critical phosphorylation sites would affect chromosome segregation, since preventing the inactivation of inappropriately attached kinetochores by aurora b (in the nonphosphorylatable mutant) or constitutively inactivating this attachment (in the phosphomimetic mutant). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-165562 |
Ser5 |
sVSSGGAG |
Homo sapiens |
|
pmid |
sentence |
20471944 |
To determine whether the combinatorial regulation of the kmn network by aurora b observed in vitro is critical to controlling kinetochore-microtubule attachments in vivo, we next investigated the effect of the phosphomimetic (to aspartate) and nonphosphorylatable (to alanine) mutants of dsn1, knl1, and ndc80 in vertebrate cells. We predicted that both types of mutations in critical phosphorylation sites would affect chromosome segregation, since preventing the inactivation of inappropriately attached kinetochores by aurora b (in the nonphosphorylatable mutant) or constitutively inactivating this attachment (in the phosphomimetic mutant). |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
AURKB | up-regulates activity
phosphorylation
|
SKA3 |
0.466 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262661 |
Ser159 |
SPRSPQLsDFGLERY |
in vitro |
|
pmid |
sentence |
22371557 |
Aurora B directly phosphorylated Ska1 and Ska3 in vitro, and expression of phosphomimetic mutants of Ska1 and Ska3 impaired Ska KT recruitment and formation of stable KT-MT fibers (K-fibers), disrupting mitotic progression. We propose that Aurora B phosphorylation antagonizes the interaction between the Ska complex and the KMN network, thereby controlling Ska recruitment to KTs and stabilization of KT-MT attachments. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
AURKB | up-regulates
phosphorylation
|
MAPRE3 |
0.485 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-202130 |
Ser176 |
MQTSGRLsNVAPPCI |
Homo sapiens |
|
pmid |
sentence |
23712260 |
Phosphorylation of eb3 at s176 by aurora b ensures successful cytokinesis completion by promoting midbody mt stability and midbody stabilization. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AURKB | up-regulates
phosphorylation
|
YY1 |
0.377 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-200075 |
Ser180 |
KKGGGKKsGKKSYLS |
Homo sapiens |
|
pmid |
sentence |
23226345 |
Aurora b kinase phosphorylates yy1 on serine 184 and to a lesser extent serine 180 at the g2/m stage of the cell cycle (fig. 7). We show that yy1 is rapidly dephosphorylated as the cells exit mitosis, likely by pp1. Also, our data indicates that phosphorylation at serine 180 and serine 184 can affect the dna binding activity of yy1 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-200079 |
Ser184 |
GKKSGKKsYLSGGAG |
Homo sapiens |
|
pmid |
sentence |
23226345 |
Aurora b kinase phosphorylates yy1 on serine 184 and to a lesser extent serine 180 at the g2/m stage of the cell cycle (fig. 7). We show that yy1 is rapidly dephosphorylated as the cells exit mitosis, likely by pp1. Also, our data indicates that phosphorylation at serine 180 and serine 184 can affect the dna binding activity of yy1 |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
AURKB | down-regulates
phosphorylation
|
TP53 |
0.708 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-197598 |
Ser183 |
CPHHERCsDSDGLAP |
Homo sapiens |
|
pmid |
sentence |
22611192 |
We show that aurora b phosphorylates p53 at s183, t211, and s215 to accelerate the degradation of p53 through the polyubiquitination-proteasome pathway, thus functionally suppressing the expression of p53 target genes involved in cell cycle inhibition and apoptosis (e.g., p21 and puma). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-197602 |
Ser215 |
DRNTFRHsVVVPYEP |
Homo sapiens |
|
pmid |
sentence |
22611192 |
We show that aurora b phosphorylates p53 at s183, t211, and s215 to accelerate the degradation of p53 through the polyubiquitination-proteasome pathway, thus functionally suppressing the expression of p53 target genes involved in cell cycle inhibition and apoptosis (e.g., p21 and puma). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-168745 |
Ser269 |
GNLLGRNsFEVRVCA |
Homo sapiens |
|
pmid |
sentence |
20959462 |
Importantly, the aurora b-mediated phosphorylation on ser(269) or thr(284) significantly compromises p53 transcriptional activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-197606 |
Thr211 |
EYLDDRNtFRHSVVV |
Homo sapiens |
|
pmid |
sentence |
22611192 |
We show that aurora b phosphorylates p53 at s183, t211, and s215 to accelerate the degradation of p53 through the polyubiquitination-proteasome pathway, thus functionally suppressing the expression of p53 target genes involved in cell cycle inhibition and apoptosis (e.g., p21 and puma). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-168749 |
Thr284 |
CPGRDRRtEEENLRK |
Homo sapiens |
|
pmid |
sentence |
20959462 |
Importantly, the aurora b-mediated phosphorylation on ser(269) or thr(284) significantly compromises p53 transcriptional activity. |
|
Publications: |
5 |
Organism: |
Homo Sapiens |
+ |
AURKB | up-regulates
phosphorylation
|
NINL |
0.255 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-168045 |
Ser185 |
WDSEDFGsPQKSCSP |
Homo sapiens |
|
pmid |
sentence |
20864540 |
Importantly, nlp is characterized as a novel substrate of aurora b and can be phosphorylated by aurora b. The specific phosphorylation sites are mapped at ser-185, ser-448, and ser-585. The phosphorylation at ser-448 and ser-585 is likely required for nlp association with aurora b and localization at midbody. Meanwhile, the phosphorylation at ser-185 is vital to nlp protein stability. Disruptions of these phosphorylation sites abolish cytokinesis and lead to chromosomal instability. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-168049 |
Ser448 |
QGYRERLsLLRSEVE |
Homo sapiens |
|
pmid |
sentence |
20864540 |
Importantly, nlp is characterized as a novel substrate of aurora b and can be phosphorylated by aurora b. The specific phosphorylation sites are mapped at ser-185, ser-448, and ser-585. The phosphorylation at ser-448 and ser-585 is likely required for nlp association with aurora b and localization at midbody. Meanwhile, the phosphorylation at ser-185 is vital to nlp protein stability. Disruptions of these phosphorylation sites abolish cytokinesis and lead to chromosomal instability. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-168053 |
Ser585 |
RLPKNRHsPSWSPDG |
Homo sapiens |
|
pmid |
sentence |
20864540 |
Importantly, nlp is characterized as a novel substrate of aurora b and can be phosphorylated by aurora b. The specific phosphorylation sites are mapped at ser-185, ser-448, and ser-585. The phosphorylation at ser-448 and ser-585 is likely required for nlp association with aurora b and localization at midbody. Meanwhile, the phosphorylation at ser-185 is vital to nlp protein stability. Disruptions of these phosphorylation sites abolish cytokinesis and lead to chromosomal instability. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
AURKB | down-regulates quantity by destabilization
phosphorylation
|
SSU72 |
0.257 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275529 |
Ser19 |
CSSNQNRsMEAHNIL |
|
|
pmid |
sentence |
24149858 |
Here we report that Aurora B kinase directly interacts with and phosphorylates Ssu72, a new cohesin-binding phosphatase, at Ser 19 in vitro and in vivo. The Aurora B-mediated phosphorylation of Ssu72 causes the structural modification of Ssu72 protein, downregulates phosphatase activity and triggers the ubiquitin-dependent degradation of Ssu72. |
|
Publications: |
1 |
+ |
AURKB | down-regulates activity
phosphorylation
|
SSU72 |
0.257 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275530 |
Ser19 |
CSSNQNRsMEAHNIL |
|
|
pmid |
sentence |
24149858 |
Here we report that Aurora B kinase directly interacts with and phosphorylates Ssu72, a new cohesin-binding phosphatase, at Ser 19 in vitro and in vivo. The Aurora B-mediated phosphorylation of Ssu72 causes the structural modification of Ssu72 protein, downregulates phosphatase activity and triggers the ubiquitin-dependent degradation of Ssu72. |
|
Publications: |
1 |
+ |
AURKB | up-regulates
phosphorylation
|
DIAPH2 |
0.293 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-172803 |
Ser196 |
SLTSNPVsWVNNFGH |
Homo sapiens |
|
pmid |
sentence |
21397845 |
The microtubule binding fh2 domain of mdia3 is phosphorylated by aurora b kinase in vitro, and cells expressing the nonphosphorylatable mdia3 mutant cannot position chromosomes at the metaphase plate |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AURKB | down-regulates
phosphorylation
|
RASSF1 |
0.45 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-184561 |
Ser207 |
TSVRRRTsFYLPKDA |
Homo sapiens |
|
pmid |
sentence |
19276349 |
Here, we show that aurora a and b associate with and phosphorylate rassf1a on serine 203 aurora a regulates prometaphase progression by inhibiting the ability of rassf1a to suppress apc-cdc20 activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AURKB | up-regulates
phosphorylation
|
CHMP4C |
0.483 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-197967 |
Ser210 |
MSSTARRsRAASSQR |
Homo sapiens |
|
pmid |
sentence |
22724069 |
Moreover, we find that the cpc's catalytic subunit, aurora b kinase, phosphorylates one of the three human snf7 paralogues-chmp4c-in its c-terminal tail, a region known to regulate its ability to form polymers and associate with membranes. Phosphorylation at these sites appears essential for chmp4c function because their mutation leads to cytokinesis defects. The introduction of the s214a and s215a mutations together with s210a almost completely abolished aurora b phosphorylation |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-197971 |
Ser214 |
ARRSRAAsSQRAEEE |
Homo sapiens |
|
pmid |
sentence |
22724069 |
Moreover, we find that the cpc's catalytic subunit, aurora b kinase, phosphorylates one of the three human snf7 paralogues-chmp4c-in its c-terminal tail, a region known to regulate its ability to form polymers and associate with membranes. Phosphorylation at these sites appears essential for chmp4c function because their mutation leads to cytokinesis defects. The introduction of the s214a and s215a mutations together with s210a almost completely abolished aurora b phosphorylation |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-196728 |
Ser215 |
RRSRAASsQRAEEED |
Homo sapiens |
|
pmid |
sentence |
22422861 |
Chmp4c functioned in the aurora b-dependent abscission checkpoint to prevent both premature resolution of intercellular chromosome bridges and accumulation of dna damage. Chmp4c engaged the chromosomal passenger complex (cpc) via interaction with borealin, which suggested a model whereby chmp4c inhibits abscission upon phosphorylation by aurora b |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
AURKB | down-regulates
phosphorylation
|
HDAC9 |
0.266 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-198654 |
Ser239 |
QKVAERRsSPLLRRK |
Homo sapiens |
|
pmid |
sentence |
22865920 |
We define the precise site of aurb-mediated phosphorylation as a conserved serine within the nuclear localization signals of hdac4, hdac5, and hdac9 at ser265, ser278, and ser242, respectivelyduring mitosis, aurb-mediated phosphorylation may localize class iia hdacs to a phosphorylation gradient at the spindle midzone, permitting temporal and spatial regulatory mechanisms altering hdac protein interactions |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AURKB | down-regulates
phosphorylation
|
KNL1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-165502 |
Ser24 |
RPVRRRHsSILKPPR |
Homo sapiens |
|
pmid |
sentence |
20471944 |
To determine whether the combinatorial regulation of the kmn network by aurora b observed in vitro is critical to controlling kinetochore-microtubule attachments in vivo, we next investigated the effect of the phosphomimetic (to aspartate) and nonphosphorylatable (to alanine) mutants of dsn1, knl1, and ndc80 in vertebrate cells. We predicted that both types of mutations in critical phosphorylation sites would affect chromosome segregation, since preventing the inactivation of inappropriately attached kinetochores by aurora b (in the nonphosphorylatable mutant) or constitutively inactivating this attachment (in the phosphomimetic mutant). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-165506 |
Ser60 |
KKNSRRVsFADTIKV |
Homo sapiens |
|
pmid |
sentence |
20471944 |
To determine whether the combinatorial regulation of the kmn network by aurora b observed in vitro is critical to controlling kinetochore-microtubule attachments in vivo, we next investigated the effect of the phosphomimetic (to aspartate) and nonphosphorylatable (to alanine) mutants of dsn1, knl1, and ndc80 in vertebrate cells. We predicted that both types of mutations in critical phosphorylation sites would affect chromosome segregation, since preventing the inactivation of inappropriately attached kinetochores by aurora b (in the nonphosphorylatable mutant) or constitutively inactivating this attachment (in the phosphomimetic mutant). |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
AURKB | up-regulates activity
phosphorylation
|
ZWINT |
0.637 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265009 |
Ser250 |
PTRPQEQsTGDTMGR |
in vitro |
|
pmid |
sentence |
21775627 |
Zwint-1 is a novel Aurora B substrate required for the assembly of a dynein-binding platform on kinetochores|During prometaphase, AurB phosphorylation of zwint-1 is required for recruitment of ZW10-, pT89 dynein-, and RZZ-dependent proteins to kinetochores. This is defective after AurB inhibition or after expression of the triple-A zwint-1 mutant. Triple-E mutant zwint-1 mimics phospho–zwint-1 in RZZ recruitment, even after AurB inhibition |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265011 |
Ser262 |
MGRDPGVsFKAVGLQ |
in vitro |
|
pmid |
sentence |
21775627 |
Zwint-1 is a novel Aurora B substrate required for the assembly of a dynein-binding platform on kinetochores|During prometaphase, AurB phosphorylation of zwint-1 is required for recruitment of ZW10-, pT89 dynein-, and RZZ-dependent proteins to kinetochores. This is defective after AurB inhibition or after expression of the triple-A zwint-1 mutant. Triple-E mutant zwint-1 mimics phospho–zwint-1 in RZZ recruitment, even after AurB inhibition |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265010 |
Thr251 |
TRPQEQStGDTMGRD |
in vitro |
|
pmid |
sentence |
21775627 |
Zwint-1 is a novel Aurora B substrate required for the assembly of a dynein-binding platform on kinetochores|During prometaphase, AurB phosphorylation of zwint-1 is required for recruitment of ZW10-, pT89 dynein-, and RZZ-dependent proteins to kinetochores. This is defective after AurB inhibition or after expression of the triple-A zwint-1 mutant. Triple-E mutant zwint-1 mimics phospho–zwint-1 in RZZ recruitment, even after AurB inhibition |
|
Publications: |
3 |
Organism: |
In Vitro |
+ |
AURKB | down-regulates
phosphorylation
|
HDAC4 |
0.268 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-198646 |
Ser265 |
QKVAERRsSPLLRRK |
Homo sapiens |
|
pmid |
sentence |
22865920 |
We define the precise site of aurb-mediated phosphorylation as a conserved serine within the nuclear localization signals of hdac4, hdac5, and hdac9 at ser265, ser278, and ser242, respectivelyduring mitosis, aurb-mediated phosphorylation may localize class iia hdacs to a phosphorylation gradient at the spindle midzone, permitting temporal and spatial regulatory mechanisms altering hdac protein interactions |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AURKB | up-regulates quantity by stabilization
phosphorylation
|
H1-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262658 |
Ser27 |
VKKKARKsAGAAKRK |
Homo sapiens |
MCF-7 Cell |
pmid |
sentence |
21511733 |
we showed previously that phosphorylation of S27 in human histone H1.4 (H1.4S27-P), prevents binding of heterochromatin protein 1 (HP1) family members (officially known as chromobox protein homologs) to the neighboring dimethylated K26. Here, we present the first functional characterization of H1.4S27-P in vivo and in vitro. We show that H1.4S27 phosphorylation is cell-cycle-regulated and its levels peak on metaphase chromosomes. We identify further Aurora B as the kinase phosphorylating H1.4S27. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AURKB | down-regulates
phosphorylation
|
HDAC5 |
0.261 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-198650 |
Ser278 |
QKVAERRsSPLLRRK |
Homo sapiens |
|
pmid |
sentence |
22865920 |
We define the precise site of aurb-mediated phosphorylation as a conserved serine within the nuclear localization signals of hdac4, hdac5, and hdac9 at ser265, ser278, and ser242, respectivelyduring mitosis, aurb-mediated phosphorylation may localize class iia hdacs to a phosphorylation gradient at the spindle midzone, permitting temporal and spatial regulatory mechanisms altering hdac protein interactions |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AURKB | down-regulates activity
phosphorylation
|
H3C1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-114852 |
Ser29 |
ATKAARKsAPATGGV |
Homo sapiens |
|
pmid |
sentence |
11856369 |
Histone code pathway involving h3 s28 phosphorylation and k27 acetylation activates transcription and antagonizes polycomb silencingaurora-b phosphorylates histone h3 at serine28 with regard to the mitotic chromosome condensation |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-171717 |
Ser29 |
ATKAARKsAPATGGV |
Homo sapiens |
|
pmid |
sentence |
21282660 |
Histone code pathway involving h3 s28 phosphorylation and k27 acetylation activates transcription and antagonizes polycomb silencingaurora-b phosphorylates histone h3 at serine28 with regard to the mitotic chromosome condensation |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CHEK1 | up-regulates
phosphorylation
|
AURKB |
0.367 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-152926 |
Ser331 |
HPWVRANsRRVLPPS |
Homo sapiens |
|
pmid |
sentence |
17276342 |
Chk1 phosphorylates aurora-b and enhances its catalytic activity in vitro. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AURKB |
phosphorylation
|
WWC1 |
0.253 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-176363 |
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 |
+ |
AURKB | down-regulates activity
phosphorylation
|
CDCA2 |
0.459 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274002 |
Ser542 |
KKINRRKsQETKCTK |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
32938714 |
This result demonstrates that the three sites of Repo-Man (Ser-543, Ser-977, and Ser-981) are phosphorylated by Aurora B in early mitosis. We uncover that PP1γ is recruited to mitotic chromosomes by its regulatory subunit Repo-Man in the absence of Aurora B activity and that Aurora B regulates dissociation of PP1γ by phosphorylating and disrupting PP1γ-Repo-Man interactions on chromatin. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274004 |
Ser977 |
EPGKRRKsFCISTLA |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
32938714 |
This result demonstrates that the three sites of Repo-Man (Ser-543, Ser-977, and Ser-981) are phosphorylated by Aurora B in early mitosis. We uncover that PP1γ is recruited to mitotic chromosomes by its regulatory subunit Repo-Man in the absence of Aurora B activity and that Aurora B regulates dissociation of PP1γ by phosphorylating and disrupting PP1γ-Repo-Man interactions on chromatin. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274001 |
Ser981 |
RRKSFCIsTLANTKA |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
32938714 |
This result demonstrates that the three sites of Repo-Man (Ser-543, Ser-977, and Ser-981) are phosphorylated by Aurora B in early mitosis. We uncover that PP1γ is recruited to mitotic chromosomes by its regulatory subunit Repo-Man in the absence of Aurora B activity and that Aurora B regulates dissociation of PP1γ by phosphorylating and disrupting PP1γ-Repo-Man interactions on chromatin. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
AURKB | up-regulates
phosphorylation
|
CKAP2 |
0.3 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-165410 |
Ser628 |
FLTPVRRsRRLQEKT |
Homo sapiens |
|
pmid |
sentence |
20458174 |
Here, we report that tmap is a novel substrate of the aurora b kinase. Ser627 of tmap was specifically phosphorylated by aurora b both in vitro and in vivo. Nearly all mutations at the phosphorylation motif had dramatic effects on the subcellular localization of tmap. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AURKB | up-regulates activity
phosphorylation
|
SHCBP1 |
0.38 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273552 |
Ser634 |
QIKKKRLsELGITQA |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
23704356 |
AurB phosphorylates Ser634 of SHCBP1 during mitosis. We generated a phosphorylation site mutant, S634A-SHCBP1, which was prematurely recruited to the central spindle during anaphase and inhibited furrowing. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AURKB |
phosphorylation
|
CENPA |
0.815 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250585 |
Ser7 |
sRKPEAPR |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
11756469 |
CENP-A–GST constructs were prepared in which Ser7 was mutated to alanine or glutamic acid. Phosphorylation of these proteins by Aurora B was reduced by 50%, demonstrating that Ser7 is a kinase substrate | Therefore, under the short term induction conditions used in these experiments, we can conclude that CENP-A Ser7 mutations do not grossly interfere with kinetochore formation, spindle assembly, or cell cycle progression. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AURKB | down-regulates
phosphorylation
|
VIM |
0.397 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-96057 |
Ser73 |
SAVRLRSsVPGVRLL |
Homo sapiens |
|
pmid |
sentence |
12458200 |
By identifying eight aurora-b phosphorylation sites on vimentin in vitro, we have demonstrated that vimentin-ser-72 is an in vitrophosphorylation site of aurora-b. in vitro analyses revealed that aurora-b phosphorylates vimentin at approximately 2 mol phosphate/mol of substrate for 30 min and that this phosphorylation dramatically inhibits vimentin filament formation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AURKB | down-regulates activity
phosphorylation
|
KIF20A |
0.772 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262659 |
Ser878 |
RILRSRRsPLLKSGP |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
27939310 |
We identify MKlp2 as an essential protein for promoting abscission, which may regulate tethering and stabilizing of the PM to the microtubule cytoskeleton. Aurora B phosphorylation of MKlp2 S878 in the LAM is a key inhibitory signal for abscission. Conversely, B56-PP2A promotes abscission by opposing Aurora B phosphorylation of MKlp2 S878. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AURKB | up-regulates
phosphorylation
|
INCENP |
0.973 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-118011 |
Ser893 |
PRYHKRTsSAVWNSP |
Homo sapiens |
|
pmid |
sentence |
12925766 |
Human incenp was a substrate of aurora b and mass spectrometry identified three consecutive residues (threonine 893, serine 894, and serine 895) containing at least two phosphorylation sites. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-118015 |
Ser894 |
RYHKRTSsAVWNSPP |
Homo sapiens |
|
pmid |
sentence |
12925766 |
Human incenp was a substrate of aurora b and mass spectrometry identified three consecutive residues (threonine 893, serine 894, and serine 895) containing at least two phosphorylation sites. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-118019 |
Thr892 |
KPRYHKRtSSAVWNS |
Homo sapiens |
|
pmid |
sentence |
12925766 |
Human incenp was a substrate of aurora b and mass spectrometry identified three consecutive residues (threonine 893, serine 894, and serine 895) containing at least two phosphorylation sites. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
AURKB | up-regulates
phosphorylation
|
KIF2C |
0.72 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-155890 |
Ser95 |
IQKQKRRsVNSKIPA |
Homo sapiens |
|
pmid |
sentence |
17567953 |
Here, we show that the binding of mcak to chromosome arms is also regulated by aurora b and that aurora b-dependent chromosome arm and centromere localization is regulated by distinct two-site phosphoregulatory mechanisms. Mcak association with chromosome arms is promoted by phosphorylation of t95 on mcak, whereas phosphorylation of s196 on mcak promotes dissociation from the arms. Although targeting of mcak to centromeres requires phosphorylation of s110 on mcak, dephosphorylation of t95 on mcak increases the binding of mcak to centromeres. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AURKB | down-regulates activity
phosphorylation
|
ARHGEF2 |
0.253 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276062 |
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 |
+ |
AURKB | down-regulates
phosphorylation
|
BIRC5 |
0.786 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-154569 |
Thr117 |
KNKIAKEtNNKKKEF |
Homo sapiens |
|
pmid |
sentence |
17457057 |
Phosphorylation by aurora-b negatively regulates survivin function . hat survivin is phosphorylated at t117 during mitosis, and once phosphorylated, dephosphorylation is crucial for chromosome congression and progression into anaphaseduring mitosis |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AURKB | up-regulates
phosphorylation
|
AURKB |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-121340 |
Thr232 |
APSLRRKtMCGTLDY |
Homo sapiens |
|
pmid |
sentence |
14722118 |
We report here that human aurora-b is phosphorylated at thr-232 through interaction with the inner centromere protein (incenp) in vivo. The phosphorylation of thr-232 occurs by means of an autophosphorylation mechanism, which is indispensable for the aurora-b kinase activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AURKB | up-regulates
phosphorylation
|
PLEKHG6 |
0.257 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-204534 |
Thr544 |
SPSTRPStPSLEGSQ |
Homo sapiens |
|
pmid |
sentence |
24482237 |
In this study we report that aurora b-mediated phosphorylation of myogef at thr-544 creates a docking site for plk1, leading to the localization and activation of myogef at the central spindle. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AURKB | up-regulates activity
phosphorylation
|
KIF4A |
0.533 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265992 |
Thr799 |
PPKLRRRtFSLTEVR |
in vitro |
|
pmid |
sentence |
28992084 |
Using in vitro kinase assays, we found that active AMPK and Aurora B phosphorylated KIF4A at Ser801 and Thr799 respectively in a time-dependent manner (Figure 5D). KIF4A is phosphoregulated by AMPK and Aurora B. Although AMPK phosphorylation increased the ATPase activity of KIF4A, Aurora B phosphorylation resulted in a stronger increase (Figure 5I), which might be consistent with the more powerful kinase function of Aurora B during mitosis. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
KLHL13 | up-regulates activity
binding
|
AURKB |
0.733 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271657 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
17543862 |
Aurora B Interacts with the Cul3 Complex during Mitosis and Is Ubiquitylated in a Cul3-Dependent Manner In Vivo and In Vitro. our results suggest that Cul3/KLHL9/KLHL13 activity is required to remove the chromosomal passenger protein Aurora B from mitotic chromosomes, and that Aurora B is ubiquitylated in vivo and in vitro in a KLHL9/13-dependent manner. We conclude that the Cul3/KLHL9/KLHL13 E3 ligase is an important cell-cycle regulator which, in addition to the anaphase-promoting complex (APC), coordinates mitotic progression and completion of cytokinesis. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
2-[3-[[7-[3-[ethyl(2-hydroxyethyl)amino]propoxy]-4-quinazolinyl]amino]-1H-pyrazol-5-yl]-N-(3-fluorophenyl)acetamide | down-regulates
chemical inhibition
|
AURKB |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-190245 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
KLHL9 | up-regulates activity
binding
|
AURKB |
0.699 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271658 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
17543862 |
Aurora B Interacts with the Cul3 Complex during Mitosis and Is Ubiquitylated in a Cul3-Dependent Manner In Vivo and In Vitro. our results suggest that Cul3/KLHL9/KLHL13 activity is required to remove the chromosomal passenger protein Aurora B from mitotic chromosomes, and that Aurora B is ubiquitylated in vivo and in vitro in a KLHL9/13-dependent manner. We conclude that the Cul3/KLHL9/KLHL13 E3 ligase is an important cell-cycle regulator which, in addition to the anaphase-promoting complex (APC), coordinates mitotic progression and completion of cytokinesis. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AURKB | up-regulates activity
phosphorylation
|
SKA1 |
0.725 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262662 |
|
|
in vitro |
|
pmid |
sentence |
22371557 |
Aurora B directly phosphorylated Ska1 and Ska3 in vitro, and expression of phosphomimetic mutants of Ska1 and Ska3 impaired Ska KT recruitment and formation of stable KT-MT fibers (K-fibers), disrupting mitotic progression. We propose that Aurora B phosphorylation antagonizes the interaction between the Ska complex and the KMN network, thereby controlling Ska recruitment to KTs and stabilization of KT-MT attachments. |
|
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
chemical inhibition
|
AURKB |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-192811 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
2-[3-[[7-[3-[ethyl(2-hydroxyethyl)amino]propoxy]-4-quinazolinyl]amino]-1H-pyrazol-5-yl]-N-(3-fluorophenyl)acetamide | down-regulates activity
chemical inhibition
|
AURKB |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-258181 |
|
|
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 |
+ |
Cullin 3-RBX1-Skp1 | up-regulates activity
polyubiquitination
|
AURKB |
0.436 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271661 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
17543862 |
Aurora B Interacts with the Cul3 Complex during Mitosis and Is Ubiquitylated in a Cul3-Dependent Manner In Vivo and In Vitro. our results suggest that Cul3/KLHL9/KLHL13 activity is required to remove the chromosomal passenger protein Aurora B from mitotic chromosomes, and that Aurora B is ubiquitylated in vivo and in vitro in a KLHL9/13-dependent manner. We conclude that the Cul3/KLHL9/KLHL13 E3 ligase is an important cell-cycle regulator which, in addition to the anaphase-promoting complex (APC), coordinates mitotic progression and completion of cytokinesis. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271662 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
17543862 |
Aurora B Interacts with the Cul3 Complex during Mitosis and Is Ubiquitylated in a Cul3-Dependent Manner In Vivo and In Vitro. our results suggest that Cul3/KLHL9/KLHL13 activity is required to remove the chromosomal passenger protein Aurora B from mitotic chromosomes, and that Aurora B is ubiquitylated in vivo and in vitro in a KLHL9/13-dependent manner. We conclude that the Cul3/KLHL9/KLHL13 E3 ligase is an important cell-cycle regulator which, in addition to the anaphase-promoting complex (APC), coordinates mitotic progression and completion of cytokinesis. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CCT129202 | down-regulates
chemical inhibition
|
AURKB |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-190880 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SNS-314 Mesylate | down-regulates
chemical inhibition
|
AURKB |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-207102 |
|
|
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
|
AURKB |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-207669 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ENMD-2076 | down-regulates
chemical inhibition
|
AURKB |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-191469 |
|
|
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
|
AURKB |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-193534 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AT9283 | down-regulates
chemical inhibition
|
AURKB |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-190014 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FBXL2 | down-regulates quantity by destabilization
binding
|
AURKB |
0.497 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272097 |
|
|
Mus musculus |
MLE-12 Cell |
pmid |
sentence |
23370391 |
The SCF complex contains a catalytic core consisting of Skp1, Cullin1, and the E2 ubiquitin-conjugating (Ubc) enzyme and a F box component that acts as a receptor targeting numerous substrates via phosphodegron elicited interactions. our screening studies suggested that FBXL2 also targets Aurora B protein for ubiquitination and degradation. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
hesperadin | down-regulates
chemical inhibition
|
AURKB |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-193128 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ZM447439 | down-regulates
chemical inhibition
|
AURKB |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-207923 |
|
|
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 activity
chemical inhibition
|
AURKB |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-258304 |
|
|
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
|
AURKB |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-205953 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AURKB | up-regulates
phosphorylation
|
Histone H3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265321 |
|
|
Homo sapiens |
|
pmid |
sentence |
10464286 |
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 |
+ |
ATM | down-regulates
|
AURKB |
0.444 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-160644 |
|
|
Homo sapiens |
|
pmid |
sentence |
18250156 |
Furthermore, atm-mediated i-2 phosphorylation results in the inhibition of the aurora-b kinase, the down-regulation of histone h3 serine 10 phosphorylation, and the activation of the g2/m checkpoint. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CCT137690 | down-regulates
chemical inhibition
|
AURKB |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-190895 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AURKB | form complex
binding
|
CPC |
0.857 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275426 |
|
|
Homo sapiens |
|
pmid |
sentence |
23175282 |
It is now known that the chromosomal passenger complex (CPC) is composed of four subunits: the enzymatic component Aurora B and the three regulatory and targeting components INCENP, Survivin and Borealin (also known as Dasra)5–7 (Figure 1A). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CYC-116 | down-regulates
chemical inhibition
|
AURKB |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-191224 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Cullin 1-RBX1-Skp1 | down-regulates quantity by destabilization
polyubiquitination
|
AURKB |
0.295 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272098 |
|
|
Mus musculus |
MLE-12 Cell |
pmid |
sentence |
23370391 |
The SCF complex contains a catalytic core consisting of Skp1, Cullin1, and the E2 ubiquitin-conjugating (Ubc) enzyme and a F box component that acts as a receptor targeting numerous substrates via phosphodegron elicited interactions. our screening studies suggested that FBXL2 also targets Aurora B protein for ubiquitination and degradation. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
TAK-901 | down-regulates
chemical inhibition
|
AURKB |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-207191 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
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
|
AURKB |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-191277 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PHA-680632 | down-regulates
chemical inhibition
|
AURKB |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-206100 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
POGZ | up-regulates activity
binding
|
AURKB |
0.329 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264497 |
|
|
Homo sapiens |
Neuroblastoma Cell Line |
pmid |
sentence |
20562864 |
POGZ is required for the correct activation and dissociation of Aurora B kinase from chromosome arms during M phase. These results reveal POGZ as an essential protein that links HP1alpha dissociation with Aurora B kinase activation during mitosis. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
KLHL21 | up-regulates activity
binding
|
AURKB |
0.522 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271848 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
19995937 |
KLHL21 directly binds to Aurora B and mediates ubiquitination of Aurora B in vitro. In contrast to KLHL9 and KLHL13, KLHL21 localizes to midzone microtubules in anaphase and recruits Aurora B and Cul3 to this region. Together, our results suggest that different Cul3 adaptors nonredundantly regulate Aurora B during mitosis, possibly by ubiquitinating different pools of Aurora B at distinct subcellular localizations. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AMG 900 | down-regulates
chemical inhibition
|
AURKB |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-189495 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
INCENP | up-regulates
binding
|
AURKB |
0.973 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-86218 |
|
|
Homo sapiens |
|
pmid |
sentence |
12925766 |
Using recombinant proteins, we found that aurora b kinase activity was stimulated by incenp and that the c-terminal region of incenp was sufficient for activation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |