| + |
AURKA | up-regulates activity 
phosphorylation
|
WDR62 |
0.362 |
| 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 |
| + |
MAPK8 | down-regulates quantity by destabilization 
phosphorylation
|
WDR62 |
0.577 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271710 |
Thr1053 |
PSSSLPQtPEQEKFL |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 30566428 |
WDR62 is also negatively regulated by T1053 phosphorylation, leading to the recruitment of F-box and WD repeat domain-containing protein 7 (FBW7) and proteasomal degradation. |JNK1 can induce the phosphorylation of WDR62 T1053 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBXO7 | down-regulates quantity by destabilization
ubiquitination
|
WDR62 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271711 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 30566428 |
WDR62 is also negatively regulated by T1053 phosphorylation, leading to the recruitment of F-box and WD repeat domain-containing protein 7 (FBW7) and proteasomal degradation. |JNK1 can induce the phosphorylation of WDR62 T1053 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
WDR62 | up-regulates activity
relocalization
|
MAPK8 |
0.577 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271718 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 30566428 |
In the WT brain, the WDR62 scaffold organizes a protein complex including MEKK3, MKK4/7, and JNK1 to control NPC development during corticogenesis |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
WDR62 | up-regulates activity
relocalization
|
MAP3K3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271717 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 30566428 |
In the WT brain, the WDR62 scaffold organizes a protein complex including MEKK3, MKK4/7, and JNK1 to control NPC development during corticogenesis |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
WDR62 | up-regulates activity
relocalization
|
CDK2 |
0.248 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271726 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 26297806 |
Primary microcephaly (MCPH) associated proteins CDK5RAP2, CEP152, WDR62 and CEP63 colocalize at the centrosome. We found that they interact to promote centriole duplication and form a hierarchy in which each is required to localize another to the centrosome, with CDK5RAP2 at the apex, and CEP152, WDR62 and CEP63 at sequentially lower positions. MCPH proteins interact with distinct centriolar satellite proteins; CDK5RAP2 interacts with SPAG5 and CEP72, CEP152 with CEP131, WDR62 with MOONRAKER, and CEP63 with CEP90 and CCDC14. These satellite proteins localize their cognate MCPH interactors to centrosomes and also promote centriole duplication. Consistent with a role for satellites in microcephaly, homozygous mutations in one satellite gene, CEP90, may cause MCPH. The satellite proteins, with the exception of CCDC14, and MCPH proteins promote centriole duplication by recruiting CDK2 to the centrosome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
WDR62 | up-regulates activity
relocalization
|
MAP2K4 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271715 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 30566428 |
In the WT brain, the WDR62 scaffold organizes a protein complex including MEKK3, MKK4/7, and JNK1 to control NPC development during corticogenesis |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
WDR62 | up-regulates activity
relocalization
|
MAP2K7 |
0.303 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271716 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 30566428 |
In the WT brain, the WDR62 scaffold organizes a protein complex including MEKK3, MKK4/7, and JNK1 to control NPC development during corticogenesis |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
MAP3K3 | up-regulates quantity by stabilization
binding
|
WDR62 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271714 |
|
|
|
|
| pmid |
sentence |
| 30566428 |
Specifically, we demonstrate that MEKK3 interacts with WDR62 to stabilize WDR62 and regulates JNK activity in a synergic way. On the other hand, JNK activity also regulates the phosphorylation of WDR62 at T1053 in a feedback loop which facilities the recruitment of FBW7 degradation of WDR62 |
|
| Publications: |
1 |
| + |
CDK5RAP2 | up-regulates activity
relocalization
|
WDR62 |
0.571 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271723 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 26297806 |
Primary microcephaly (MCPH) associated proteins CDK5RAP2, CEP152, WDR62 and CEP63 colocalize at the centrosome. We found that they interact to promote centriole duplication and form a hierarchy in which each is required to localize another to the centrosome, with CDK5RAP2 at the apex, and CEP152, WDR62 and CEP63 at sequentially lower positions. MCPH proteins interact with distinct centriolar satellite proteins; CDK5RAP2 interacts with SPAG5 and CEP72, CEP152 with CEP131, WDR62 with MOONRAKER, and CEP63 with CEP90 and CCDC14. These satellite proteins localize their cognate MCPH interactors to centrosomes and also promote centriole duplication. Consistent with a role for satellites in microcephaly, homozygous mutations in one satellite gene, CEP90, may cause MCPH. The satellite proteins, with the exception of CCDC14, and MCPH proteins promote centriole duplication by recruiting CDK2 to the centrosome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
WDR62
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