+ |
AKT1 |
phosphorylation
|
FANCA |
0.471 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252567 |
Ser1149 |
CLRSRDPsLMVDFIL |
in vitro |
|
pmid |
sentence |
11855836 |
FANCA is phosphorylated at Ser1149 by Akt. The biological significance of FANCA phosphorylation and its regulation by Akt remains unclear at this time. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
AKT |
phosphorylation
|
FANCA |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251476 |
Ser1149 |
CLRSRDPsLMVDFIL |
in vitro |
|
pmid |
sentence |
11855836 |
FANCA is phosphorylated at Ser1149 by Akt. The biological significance of FANCA phosphorylation and its regulation by Akt remains unclear at this time. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
ATR | up-regulates
phosphorylation
|
FANCA |
0.58 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-182953 |
Ser1449 |
AAPDADLsQEPHLF |
Homo sapiens |
|
pmid |
sentence |
19109555 |
The s1449a mutant failed to completely correct a variety of fa-associated phenotypes. The dna damage response is coordinated by phosphorylation events initiated by apical kinases atm (ataxia telangectasia mutated) and atr (atm and rad3-related), and atr is essential for proper fa pathway function. Serine 1449 is in a consensus atm/atr site |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ATM | up-regulates
phosphorylation
|
FANCA |
0.418 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-182949 |
Ser1449 |
AAPDADLsQEPHLF |
Homo sapiens |
|
pmid |
sentence |
19109555 |
The s1449a mutant failed to completely correct a variety of fa-associated phenotypes. The dna damage response is coordinated by phosphorylation events initiated by apical kinases atm (ataxia telangectasia mutated) and atr (atm and rad3-related), and atr is essential for proper fa pathway function. Serine 1449 is in a consensus atm/atr site |
|
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 |
+ |
PRKAA1 | up-regulates activity
phosphorylation
|
FANCA |
0.338 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277264 |
Ser347 |
VQMQREWsFARTHPL |
Homo sapiens |
U2-OS Cell |
pmid |
sentence |
27449087 |
FANCA was phosphorylated by AMPK at S347 and phosphorylation increased with MMC treatment. MMC-induced FANCD2 monoubiquitination and nuclear foci formation were compromised in a U2OS cell line that stably overexpressed the S347A mutant form of FANCA compared to wild-type FANCA-overexpressing cells, indicating a requirement for FANCA phosphorylation at S347 for proper activation of the FA/BRCA pathway. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FANCA | form complex
binding
|
Fanconi anemia core complex |
0.95 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263240 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
17396147 |
This complex includes not only the five known FA proteins (FANC‐A, C, E, F, and G), but also four new polypeptides, which are named FAAPs for FANCA‐associated polypeptides. |Thus, eight of the nine components of the FA core complex are FA proteins (FANC‐A, B, C, E, F, G, L, and M). Furthermore, two of the newly discovered FA proteins have enzymatic activities: FANCL is a ubiquitin ligase essential for FANCD2 monoubiquitination in vivo |
|
Publications: |
1 |
Organism: |
Homo Sapiens |