+ |
POLA1 | form complex
binding
|
DNA polymerase alpha:primase complex |
0.979 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261343 |
|
|
in vitro |
|
pmid |
sentence |
24043831 |
At the replication fork, primase is present in a constitutive complex with DNA polymerase α (Pol α), which extends the RNA primer with deoxynucleotides and makes the resulting RNA–DNA primer available to the leading- and lagging-strand polymerases, Pols ε and δ, for processive elongation |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
POLA1 | up-regulates
|
DNA_replication |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261275 |
|
|
Homo sapiens |
|
pmid |
sentence |
19608746 |
Mcm10 is an essential eukaryotic protein required for the initiation and elongation phases of chromosomal replication. Specifically, Mcm10 is required for the association of several replication proteins, including DNA polymerase alpha (pol alpha), with chromatin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PARP1 | up-regulates activity
binding
|
POLA1 |
0.348 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261270 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
9518481 |
We provide evidence that in proliferating cells: (i) PARP is physically associated with the catalytic subunit of the DNA polymerase α–primase tetramer, an association confirmed by confocal microscopy, demonstrating that both enzymes are co-localized at the nuclear periphery of HeLa cells.|(iii) PARP-deficient cells derived from PARP knock-out mice exhibited reduced DNA polymerase activity, |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPA1 | up-regulates activity
binding
|
POLA1 |
0.673 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261272 |
|
|
in vitro |
|
pmid |
sentence |
9214288 |
In our studies, we have shown that T antigen, DNA polymerase R, and the activation domain of VP16 all interact with overlapping regions of the 70-kDa subunit of RPA.| In the latter, both the direct protein-protein interaction and ssDNA-binding activities of RPA were needed for RPA to modulate polymerase processivity. We also found that SV40 T antigen inhibited the ability of RPA to increase processivity of DNA polymerase alpha, suggesting that this activity of RPA may be important for elongation but not during the initiation of DNA replication. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
MCM10 | up-regulates quantity by stabilization
relocalization
|
POLA1 |
0.857 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261271 |
|
|
in vitro |
|
pmid |
sentence |
19608746 |
Mcm10 is an essential eukaryotic protein required for the initiation and elongation phases of chromosomal replication. Specifically, Mcm10 is required for the association of several replication proteins, including DNA polymerase alpha (pol alpha), with chromatin. |
|
Publications: |
1 |
Organism: |
In Vitro |