+ |
SMG1 | up-regulates
phosphorylation
|
UPF1 |
0.971 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-200785 |
Ser1089 |
GLSQPELsQDSYLGD |
Homo sapiens |
|
pmid |
sentence |
23356578 |
Smg-1 directly phosphorylates upf1 helicase, another key component of nmd, upon recognition of ptc on postspliced mrna during the initial round of translation. Phosphorylated-upf1 recruits the smg-5/smg-7 complex to induce ribosome dissociation and decapping-mediated decay. T28 and s1096 are responsible for phospho-specific recruitment of smg-6 to the n-terminal conserved region, and the smg-5/smg-7 heterodimer complex to the c-terminal sq-rich region of upf1, respectively |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-200789 |
Ser1107 |
SQIDVALsQDSTYQG |
Homo sapiens |
|
pmid |
sentence |
23356578 |
Smg-1 directly phosphorylates upf1 helicase, another key component of nmd, upon recognition of ptc on postspliced mrna during the initial round of translation. Phosphorylated-upf1 recruits the smg-5/smg-7 complex to induce ribosome dissociation and decapping-mediated decay. T28 and s1096 are responsible for phospho-specific recruitment of smg-6 to the n-terminal conserved region, and the smg-5/smg-7 heterodimer complex to the c-terminal sq-rich region of upf1, respectively |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-200793 |
Thr28 |
AELLGADtQGSEFEF |
Homo sapiens |
|
pmid |
sentence |
23356578 |
Smg-1 directly phosphorylates upf1 helicase, another key component of nmd, upon recognition of ptc on postspliced mrna during the initial round of translation. Phosphorylated-upf1 recruits the smg-5/smg-7 complex to induce ribosome dissociation and decapping-mediated decay. T28 and s1096 are responsible for phospho-specific recruitment of smg-6 to the n-terminal conserved region, and the smg-5/smg-7 heterodimer complex to the c-terminal sq-rich region of upf1, respectively |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
AKT2 | up-regulates activity
phosphorylation
|
UPF1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277595 |
Thr151 |
FCNGRGNtSGSHIVN |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
35675814 |
AKT-Mediated UPF1 Phosphorylation at T151 Promotes UPF1 Helicase Activity |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AKT3 | up-regulates activity
phosphorylation
|
UPF1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277596 |
Thr151 |
FCNGRGNtSGSHIVN |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
35675814 |
AKT-Mediated UPF1 Phosphorylation at T151 Promotes UPF1 Helicase Activity |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AKT1 | up-regulates activity
phosphorylation
|
UPF1 |
0.26 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277597 |
Thr151 |
FCNGRGNtSGSHIVN |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
35675814 |
AKT-Mediated UPF1 Phosphorylation at T151 Promotes UPF1 Helicase Activity |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MOV10 | up-regulates activity
binding
|
UPF1 |
0.535 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261139 |
|
|
Homo sapiens |
|
pmid |
sentence |
27016603 |
MOV10 has been shown to promote mRNA degradation by associating with UPF1, this activity requires the helicase activity of MOV10. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
UPF2 | up-regulates activity
binding
|
UPF1 |
0.979 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265246 |
|
|
in vitro |
|
pmid |
sentence |
18066079 |
UPF2 and UPF3b increase UPF1 ATPase activity |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
UPF3B | up-regulates activity
binding
|
UPF1 |
0.957 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265247 |
|
|
in vitro |
|
pmid |
sentence |
18066079 |
UPF2 and UPF3b increase UPF1 ATPase activity |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
UPF1 | form complex
binding
|
Upf-EJC |
0.968 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265237 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
17803942 |
The three Up-frameshift (Upf) proteins, Upf1, Upf2, and Upf3 that together form the Upf complex, constitute the conserved core of NMD from yeast to humans. hUpf3b Forms Multiple Contacts with the EJC and Depends on hUpf2 for Complex Formation with hUpf1 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |