| + |
RAD18 | up-regulates activity 
ubiquitination
|
PCNA |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278612 |
Lys164 |
AVVISCAkDGVKFSA |
Homo sapiens |
|
| pmid |
sentence |
| 20937699 |
Second, these findings suggest the following model (XREF_FIG) : upon replication fork stalling at cisplatin induced DNA lesions, the RAD18 and RAD6 complex ubiquitylates PCNA on Lys164.|The DNA damage-activated E3 ubiquitin ligase RAD18 promotes repair of interstrand DNA cross-links by ubiquitylating PCNA and recruiting FANCL to chromatin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UBE2A | up-regulates
ubiquitination
|
PCNA |
0.487 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-92737 |
Lys164 |
AVVISCAkDGVKFSA |
Homo sapiens |
|
| pmid |
sentence |
| 12226657 |
Pcna is mono-ubiquitinated through rad6 and rad18, modified by lysine-63-linked multi-ubiquitination--which additionally requires mms2, ubc13 and rad5--and is conjugated to sumo by ubc9. The first of these is monoubiquitination of lysine 164 on one or more of the pcna subunits by the e2-e3 complex of rad6-rad18. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187761 |
Lys164 |
AVVISCAkDGVKFSA |
Homo sapiens |
|
| pmid |
sentence |
| 19706603 |
Pcna is mono-ubiquitinated through rad6 and rad18, modified by lysine-63-linked multi-ubiquitination--which additionally requires mms2, ubc13 and rad5--and is conjugated to sumo by ubc9. The first of these is monoubiquitination of lysine 164 on one or more of the pcna subunits by the e2-e3 complex of rad6-rad18. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
IGF1R | up-regulates activity
phosphorylation
|
PCNA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277254 |
Tyr133 |
LGIPEQEySCVVKMP |
in vitro |
|
| pmid |
sentence |
| 28924044 |
In vitro MS analysis of PCNA co-incubated with the IGF-1R kinase indicated tyrosine residues 60, 133, and 250 in PCNA as IGF-1R targets, and PCNA phosphorylation was followed by mono- and polyubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277252 |
Tyr250 |
DMGHLKYyLAPKIED |
in vitro |
|
| pmid |
sentence |
| 28924044 |
In vitro MS analysis of PCNA co-incubated with the IGF-1R kinase indicated tyrosine residues 60, 133, and 250 in PCNA as IGF-1R targets, and PCNA phosphorylation was followed by mono- and polyubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277253 |
Tyr60 |
RSEGFDTyRCDRNLA |
in vitro |
|
| pmid |
sentence |
| 28924044 |
In vitro MS analysis of PCNA co-incubated with the IGF-1R kinase indicated tyrosine residues 60, 133, and 250 in PCNA as IGF-1R targets, and PCNA phosphorylation was followed by mono- and polyubiquitination. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
EGFR | up-regulates
phosphorylation
|
PCNA |
0.345 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-150852 |
Tyr211 |
QLTFALRyLNFFTKA |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 17115032 |
Here, we show that the chromatin-bound pcna protein is phosphorylated on tyr 211, which is required for maintaining its function on chromatin and is dependent on the tyrosine kinase activity of egf receptor (egfr) in the nucleus. Phosphorylation on tyr 211 by egfr stabilizes chromatin-bound pcna protein and associated functions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HLTF | up-regulates activity
ubiquitination
|
PCNA |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278608 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21845734 |
HLTF promotes the Lys-63-linked polyubiquitination of proliferating cell nuclear antigen (PCNA) that is required for maintaining genomic stability. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SHPRH | up-regulates
ubiquitination
|
PCNA |
0.536 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187757 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19706603 |
We provide evidence that similar to rad5, shprh physically interacts with the human rad6rad18 and mms2ubc13 protein complexes, and importantly, we show that it exhibits an ubiquitin ligase activity and mediates mms2ubc13-dependent polyubiquitylation of pcna. Thus, shprh is a functional homolog of rad5. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PCNA | down-regulates activity 
binding
|
NCR2 |
0.31 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260043 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22021614 |
NK cells play an important role in the early immune response to cancer. The NKp44 activating receptor is the only natural cytotoxicity receptor that is expressed exclusively by primate NK cells, yet its cellular ligands remain largely unknown. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDKN1A | down-regulates
binding
|
PCNA |
0.755 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-191939 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22911014 |
P21 exerts its effect on the cell cycle not only by inhibiting cyclin/cdk complexes, but also by inhibiting proliferating cell nuclear antigen (pcna) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PCNA | up-regulates activity
binding
|
DNA polymerase delta |
0.765 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265511 |
|
|
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 12930972 |
Processive DNA synthesis by DNA polymerases delta and epsilon requires the cellular replication factor C (RF‐C) and proliferating cell nuclear antigen (PCNA). |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
PCNA | up-regulates activity
binding
|
DNA polymerase epsilon |
0.561 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265512 |
|
|
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 12930972 |
Processive DNA synthesis by DNA polymerases delta and epsilon requires the cellular replication factor C (RF‐C) and proliferating cell nuclear antigen (PCNA). |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
TFDP1 | up-regulates quantity by expression 
transcriptional regulation
|
PCNA |
0.466 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253858 |
|
|
Homo sapiens |
HEP-3B Cell |
| pmid |
sentence |
| 14618416 |
To assess transactivating activity of E2F1/DP-1, we also analyzed expression of ten putative transcriptional targets of this complex in HCCs. Expression levels of TFDP1 and E2F1 correlated with those of seven transcriptional targets ( TYMS, DHFR, PCNA, RRM1, CCNE1, CDC2, and MYBL2) that play important roles in the G1/S transition, and down-regulation of TFDP1 inhibited growth of Hep3B cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RF-C complex | up-regulates activity
binding
|
PCNA |
0.81 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265510 |
|
|
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 12930972 |
Replication factor C (RF-C) complex binds to DNA primers and loads PCNA onto DNA, thereby increasing the processivity of DNA polymerases. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
RAD18 | up-regulates
ubiquitination
|
PCNA |
0.841 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187705 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19706603 |
Rad5 interacts with the e3 ligase rad18, which is initially required to monoubiquitinate pcna |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
E2F1 | up-regulates quantity by expression
transcriptional regulation
|
PCNA |
0.478 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253856 |
|
|
Homo sapiens |
HEP-3B Cell |
| pmid |
sentence |
| 14618416 |
To assess transactivating activity of E2F1/DP-1, we also analyzed expression of ten putative transcriptional targets of this complex in HCCs. Expression levels of TFDP1 and E2F1 correlated with those of seven transcriptional targets ( TYMS, DHFR, PCNA, RRM1, CCNE1, CDC2, and MYBL2) that play important roles in the G1/S transition, and down-regulation of TFDP1 inhibited growth of Hep3B cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PCNA
- 
- 