| + |
ATM | up-regulates 
phosphorylation
|
FANCD2 |
0.786 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-90109 |
Ser1401 |
LQGEEIKsQNSQEST |
Homo sapiens |
|
| pmid |
sentence |
| 12086603 |
These results suggest that s222 and either s1401, s1404, or s1408 are sites of atm-dependent phosphorylation in vitro.Phosphorylation Of fancd2 is required for activation of an s phase checkpoint |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-90113 |
Ser1404 |
EEIKSQNsQESTADE |
Homo sapiens |
|
| pmid |
sentence |
| 12086603 |
These results suggest that s222 and either s1401, s1404, or s1408 are sites of atm-dependent phosphorylation in vitro.Phosphorylation Of fancd2 is required for activation of an s phase checkpoint |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-90117 |
Ser1407 |
KSQNSQEsTADESED |
Homo sapiens |
|
| pmid |
sentence |
| 12086603 |
These results suggest that s222 and either s1401, s1404, or s1408 are sites of atm-dependent phosphorylation in vitro.Phosphorylation Of fancd2 is required for activation of an s phase checkpoint |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-90121 |
Ser222 |
LPEILGDsQHADVGK |
Homo sapiens |
|
| pmid |
sentence |
| 12086603 |
Atm phosphorylates fancd2 on serine 222 in vitro. This site is also phosphorylated in vivo in an atm-dependent manner following ir. Phosphorylation of fancd2 is required for activation of an s phase checkpoint. The atm-dependent phosphorylation of fancd2 on s222 and the fa pathway-dependent monoubiquitination of fancd2 on k561 are independent posttranslational modifications regulating discrete cellular signaling pathways. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
CHEK1 | up-regulates activity
phosphorylation
|
FANCD2 |
0.583 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263252 |
Ser331 |
KSKGRASsSGNQESS |
Homo sapiens |
Fanconi Anemia Disease Specific Cell Type |
| pmid |
sentence |
| 19861535 |
In this study, we report a novel phosphorylation site serine 331 (S331) of FANCD2, the pivotal downstream player of the Fanconi anemia pathway. Phosphorylation of S331 is important for its DNA damage-inducible monoubiquitylation, resistance to DNA cross-linkers, and in vivo interaction with FANCD1/BRCA2.|In vitro and in vivo experiments show that phosphorylation of S331 is mediated by CHK1, |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-107042 |
Ser331 |
KSKGRASsSGNQESS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 19861535 |
In vitro and in vivo experiments show that phosphorylation of s331 is mediated by chk1, the s-phase checkpoint kinase implicated in the fanconi anemia dna repair pathway. phosphorylation at this site is dependent on chk1, signifying the importance of the s-phase checkpoint in the activation of fanconi anemia pathway. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ATR | up-regulates
phosphorylation
|
FANCD2 |
0.671 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149305 |
Ser717 |
KDGGPVTsQESGQKL |
Homo sapiens |
|
| pmid |
sentence |
| 16943440 |
In the present study, we identify two novel dna damage-inducible phosphorylation sites on fancd2, threonine 691 and serine 717. Atr phosphorylates fancd2 on these two sites, thereby promoting fancd2 monoubiquitination and enhancing cellular resistance to dna cross-linking agents |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149309 |
Thr691 |
YGLEEYDtQDGIAIN |
Homo sapiens |
|
| pmid |
sentence |
| 16943440 |
In the present study, we identify two novel dna damage-inducible phosphorylation sites on fancd2, threonine 691 and serine 717. Atr phosphorylates fancd2 on these two sites, thereby promoting fancd2 monoubiquitination and enhancing cellular resistance to dna cross-linking agents |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CSNK2A1 | down-regulates activity 
phosphorylation
|
FANCD2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276730 |
Ser882 |
DGSKTSSsDTLSEEK |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 31167143 |
Here, we report a cluster of phosphosites on FANCD2 whose phosphorylation by CK2 inhibits both FANCD2 recruitment to ICLs and its monoubiquitination in vitro and in vivo. We have found that phosphorylated FANCD2 possesses reduced DNA binding activity, explaining the previous observations. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276731 |
Ser886 |
TSSSDTLsEEKNSEC |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 31167143 |
Here, we report a cluster of phosphosites on FANCD2 whose phosphorylation by CK2 inhibits both FANCD2 recruitment to ICLs and its monoubiquitination in vitro and in vivo. We have found that phosphorylated FANCD2 possesses reduced DNA binding activity, explaining the previous observations. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276728 |
Ser891 |
TLSEEKNsECDPTPS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 31167143 |
Here, we report a cluster of phosphosites on FANCD2 whose phosphorylation by CK2 inhibits both FANCD2 recruitment to ICLs and its monoubiquitination in vitro and in vivo. We have found that phosphorylated FANCD2 possesses reduced DNA binding activity, explaining the previous observations. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276729 |
Ser898 |
SECDPTPsHRGQLNK |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 31167143 |
Here, we report a cluster of phosphosites on FANCD2 whose phosphorylation by CK2 inhibits both FANCD2 recruitment to ICLs and its monoubiquitination in vitro and in vivo. We have found that phosphorylated FANCD2 possesses reduced DNA binding activity, explaining the previous observations. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276732 |
Thr884 |
SKTSSSDtLSEEKNS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 31167143 |
Here, we report a cluster of phosphosites on FANCD2 whose phosphorylation by CK2 inhibits both FANCD2 recruitment to ICLs and its monoubiquitination in vitro and in vivo. We have found that phosphorylated FANCD2 possesses reduced DNA binding activity, explaining the previous observations. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276733 |
Thr896 |
KNSECDPtPSHRGQL |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 31167143 |
Here, we report a cluster of phosphosites on FANCD2 whose phosphorylation by CK2 inhibits both FANCD2 recruitment to ICLs and its monoubiquitination in vitro and in vivo. We have found that phosphorylated FANCD2 possesses reduced DNA binding activity, explaining the previous observations. |
|
| Publications: |
6 |
Organism: |
Homo Sapiens |
| + |
Fanconi anemia core complex | up-regulates activity
ubiquitination
|
FANCD2 |
0.767 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263265 |
|
|
|
|
| pmid |
sentence |
| 18985065 |
Phosphorylation of FANCD2 and Fanconi anemia core components (broken pink circles) affects the efficiency of, but is not essential for, ID ubiquitination by the FA core complex, together with E1 and UBE2T. Analogously, ubiquitination of FANCD2 (solid orange ovals) is essential for DNA repair, activating the ID complex for chromatin binding |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263249 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17396147 |
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: |
2 |
Organism: |
, Homo Sapiens |
| + |
RAD18 | up-regulates activity
ubiquitination
|
FANCD2 |
0.52 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278712 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26871286 |
In summary, these findings suggest a model, where Rad18 promotes monoubiquitination of FANCD2, and associates with a functional complex involving Rad51, BRCA2, and FANCD2 in the repair of CPT induced stalled or collapsed forks.|In this study we focused on the role of Rad18 mediated activation of FANCD2 and its functional relationship with BRCA2 and Rad51 proteins in repair of CPT induced lesions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FANCD2 | form complex 
binding
|
Fanconi anemia ID complex |
0.956 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263268 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 17412408 |
Immunoprecipitation of HA-FLAG-tagged FANCI expressed in 293T cells with antibodies against either HA or FLAG, but not MYC, resulted in coimmunoprecipitation of endogenous FANCD2|The FANCI protein associates with FANCD2 and, together, as the FANCI-FANCD2 (ID) complex, localize to chromatin in response to DNA damage. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FANCL | up-regulates activity
ubiquitination
|
FANCD2 |
0.899 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263264 |
|
|
|
|
| pmid |
sentence |
| 18985065 |
Phosphorylation of FANCD2 and Fanconi anemia core components (broken pink circles) affects the efficiency of, but is not essential for, ID ubiquitination by the FA core complex, together with E1 and UBE2T. Analogously, ubiquitination of FANCD2 (solid orange ovals) is essential for DNA repair, activating the ID complex for chromatin binding |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263250 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 17396147 |
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: |
2 |
Organism: |
, Homo Sapiens |
| + |
FANCD2 | form complex
binding
|
D1-D2-G-X3 complex |
0.742 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263255 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 18212739 |
These results argue that FANCG has a role independent of the FA core complex, and we propose that phosphorylation of serine 7 is the signalling event required for forming a discrete complex comprising FANCD1/BRCA2-FANCD2-FANCG-XRCC3 (D1-D2-G-X3). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FANCD2 | up-regulates activity
binding, relocalization
|
BRCA2 |
0.809 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263238 |
|
|
Homo sapiens |
Fanconi Anemia Disease Specific Cell Type |
| pmid |
sentence |
| 19861535 |
Fanconi anemia complementation group FANCD2 protein serine 331 phosphorylation is important for fanconi anemia pathway function and BRCA2 interaction |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263253 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15199141 |
FANCD2-Ub then promotes BRCA2 loading into a chromatin complex. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
MEN1 | up-regulates
binding
|
FANCD2 |
0.442 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-103947 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12874027 |
Menin interacts with fancd2 / loss of menin expression in mouse embryonic fibroblasts leads to increased sensitivity to dna damage. Furthermore, menin is localized to chromatin and nuclear matrix, and the association with nuclear matrix is enhanced by gamma-irradiation. Together, these results suggest that menin plays a critical role in repair of dna damage in concert with fancd2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BRCA1-BARD1 complex | up-regulates activity
ubiquitination
|
FANCD2 |
0.708 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263237 |
|
|
Homo sapiens |
HCC-1937 Cell |
| pmid |
sentence |
| 12485996 |
The major genetic evidence supporting ubiquitin ligase function for BRCA1 in vivo comes from studies on the FANCD2 protein. Whereas in wild‐type cells the FANCD2 protein co‐localizes with BRCA1 in nuclear foci and becomes monoubiquitylated in response to DNA damage, HCC1937 cells, which encode a mutated form of BRCA1, are largely defective for both monoubiquitylation of FANCD2 and foci formation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BRCA1 | up-regulates activity
ubiquitination
|
FANCD2 |
0.844 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263236 |
|
|
Homo sapiens |
HCC-1937 Cell |
| pmid |
sentence |
| 12485996 |
The major genetic evidence supporting ubiquitin ligase function for BRCA1 in vivo comes from studies on the FANCD2 protein. Whereas in wild‐type cells the FANCD2 protein co‐localizes with BRCA1 in nuclear foci and becomes monoubiquitylated in response to DNA damage, HCC1937 cells, which encode a mutated form of BRCA1, are largely defective for both monoubiquitylation of FANCD2 and foci formation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
USP1 | down-regulates activity
deubiquitination
|
FANCD2 |
0.758 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263273 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 18082604 |
The deubiquitinating enzyme USP1 controls the cellular levels of the DNA damage response protein Ub-FANCD2|The level of monoubiquitinated FANCD2 protein increases in response to various types of DNA damage in mammalian cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
FANCD2
- 
- 