| + |
CDC7 | up-regulates 
phosphorylation
|
MCM2 |
0.961 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187388 |
Ser108 |
DVEELTAsQREAAER |
Homo sapiens |
|
| pmid |
sentence |
| 19647517 |
Phosphorylation of mcm2 by cdc7 promotes pre-replication complex assembly during cell-cycle re-entry |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143984 |
Ser13 |
ESFTMASsPAQRRRG |
Homo sapiens |
|
| pmid |
sentence |
| 16446360 |
In this work, by in vitro kinase reactions and mass spectrometry analysis of the products, we have mapped phosphorylation sites in the n terminus of mcm2 by cdc7, cdk2, cdk1, and ck2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143988 |
Ser139 |
RRGLLYDsDEEDEER |
Homo sapiens |
|
| pmid |
sentence |
| 16446360 |
In the present study, we report the identification of cdc7/dbf4 phosphorylation sites on mcm2 and determine the functional role of cdc7/dbf4 phosphorylation of mcm2 in the initiation of dna replication in human cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-148709 |
Ser139 |
RRGLLYDsDEEDEER |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 16899510 |
In the present study, we report the identification of cdc7/dbf4 phosphorylation sites on mcm2 and determine the functional role of cdc7/dbf4 phosphorylation of mcm2 in the initiation of dna replication in human cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143992 |
Ser27 |
GNDPLTSsPGRSSRR |
Homo sapiens |
|
| pmid |
sentence |
| 16446360 |
In the present study, we report the identification of cdc7/dbf4 phosphorylation sites on mcm2 and determine the functional role of cdc7/dbf4 phosphorylation of mcm2 in the initiation of dna replication in human cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-148713 |
Ser27 |
GNDPLTSsPGRSSRR |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 16899510 |
In the present study, we report the identification of cdc7/dbf4 phosphorylation sites on mcm2 and determine the functional role of cdc7/dbf4 phosphorylation of mcm2 in the initiation of dna replication in human cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187392 |
Ser40 |
RRTDALTsSPGRDLP |
Homo sapiens |
|
| pmid |
sentence |
| 19647517 |
Phosphorylation of mcm2 by cdc7 promotes pre-replication complex assembly during cell-cycle re-entry |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-148717 |
Ser41 |
RTDALTSsPGRDLPP |
Homo sapiens |
|
| pmid |
sentence |
| 16899510 |
In the present study, we report the identification of cdc7/dbf4 phosphorylation sites on mcm2 and determine the functional role of cdc7/dbf4 phosphorylation of mcm2 in the initiation of dna replication in human cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143996 |
Ser41 |
RTDALTSsPGRDLPP |
Homo sapiens |
|
| pmid |
sentence |
| 16446360 |
In the present study, we report the identification of cdc7/dbf4 phosphorylation sites on mcm2 and determine the functional role of cdc7/dbf4 phosphorylation of mcm2 in the initiation of dna replication in human cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187396 |
Ser5 |
sESFTMAS |
Homo sapiens |
|
| pmid |
sentence |
| 19647517 |
Phosphorylation of mcm2 by cdc7 promotes pre-replication complex assembly during cell-cycle re-entry |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187400 |
Ser53 |
LPPFEDEsEGLLGTE |
Homo sapiens |
|
| pmid |
sentence |
| 19647517 |
Phosphorylation of mcm2 by cdc7 promotes pre-replication complex assembly during cell-cycle re-entry |
|
| Publications: |
11 |
Organism: |
Homo Sapiens |
| + |
CDC7 | up-regulates activity
phosphorylation
|
DTD1 |
0.328 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273968 |
Ser179 |
KTRAKGPsESSKERN |
in vitro |
|
| pmid |
sentence |
| 25258324 |
Here we show that DUE-B is de-phosphorylated in M phase and phosphorylated in G1/S phase. Phosphorylated DUE-B forms homodimers, whereas de-phosphorylated DUE-B interacts with the Mcm2–7 complex and aminoacyl-tRNA synthetases. We find that CKII can prime DUE-B for Cdc7 phosphorylation. Confirming the importance of DUE-B phosphorylation in replication initiation, a C-terminal Ser/Thr to Ala mutant blocks Cdc45 and RPA loading on sperm chromatin and inhibits DNA replication. DUE-B C-terminal phosphorylation sites (serine 179, 181, 182, 194, 196, 197, 204, 205, and threonine 187) were mutated to unphosphorylatable alanine (DUE-B(S/T)-A) or phosphomimic aspartic acid (DUE-B(S/T)-D). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273966 |
Ser181 |
RAKGPSEsSKERNTP |
in vitro |
|
| pmid |
sentence |
| 25258324 |
Here we show that DUE-B is de-phosphorylated in M phase and phosphorylated in G1/S phase. Phosphorylated DUE-B forms homodimers, whereas de-phosphorylated DUE-B interacts with the Mcm2–7 complex and aminoacyl-tRNA synthetases. We find that CKII can prime DUE-B for Cdc7 phosphorylation. Confirming the importance of DUE-B phosphorylation in replication initiation, a C-terminal Ser/Thr to Ala mutant blocks Cdc45 and RPA loading on sperm chromatin and inhibits DNA replication. DUE-B C-terminal phosphorylation sites (serine 179, 181, 182, 194, 196, 197, 204, 205, and threonine 187) were mutated to unphosphorylatable alanine (DUE-B(S/T)-A) or phosphomimic aspartic acid (DUE-B(S/T)-D). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273967 |
Ser182 |
AKGPSESsKERNTPR |
in vitro |
|
| pmid |
sentence |
| 25258324 |
Here we show that DUE-B is de-phosphorylated in M phase and phosphorylated in G1/S phase. Phosphorylated DUE-B forms homodimers, whereas de-phosphorylated DUE-B interacts with the Mcm2–7 complex and aminoacyl-tRNA synthetases. We find that CKII can prime DUE-B for Cdc7 phosphorylation. Confirming the importance of DUE-B phosphorylation in replication initiation, a C-terminal Ser/Thr to Ala mutant blocks Cdc45 and RPA loading on sperm chromatin and inhibits DNA replication. DUE-B C-terminal phosphorylation sites (serine 179, 181, 182, 194, 196, 197, 204, 205, and threonine 187) were mutated to unphosphorylatable alanine (DUE-B(S/T)-A) or phosphomimic aspartic acid (DUE-B(S/T)-D). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273961 |
Ser194 |
TPRKEDRsASSGAEG |
in vitro |
|
| pmid |
sentence |
| 25258324 |
Here we show that DUE-B is de-phosphorylated in M phase and phosphorylated in G1/S phase. Phosphorylated DUE-B forms homodimers, whereas de-phosphorylated DUE-B interacts with the Mcm2–7 complex and aminoacyl-tRNA synthetases. We find that CKII can prime DUE-B for Cdc7 phosphorylation. Confirming the importance of DUE-B phosphorylation in replication initiation, a C-terminal Ser/Thr to Ala mutant blocks Cdc45 and RPA loading on sperm chromatin and inhibits DNA replication. DUE-B C-terminal phosphorylation sites (serine 179, 181, 182, 194, 196, 197, 204, 205, and threonine 187) were mutated to unphosphorylatable alanine (DUE-B(S/T)-A) or phosphomimic aspartic acid (DUE-B(S/T)-D). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273962 |
Ser196 |
RKEDRSAsSGAEGDV |
in vitro |
|
| pmid |
sentence |
| 25258324 |
Here we show that DUE-B is de-phosphorylated in M phase and phosphorylated in G1/S phase. Phosphorylated DUE-B forms homodimers, whereas de-phosphorylated DUE-B interacts with the Mcm2–7 complex and aminoacyl-tRNA synthetases. We find that CKII can prime DUE-B for Cdc7 phosphorylation. Confirming the importance of DUE-B phosphorylation in replication initiation, a C-terminal Ser/Thr to Ala mutant blocks Cdc45 and RPA loading on sperm chromatin and inhibits DNA replication. DUE-B C-terminal phosphorylation sites (serine 179, 181, 182, 194, 196, 197, 204, 205, and threonine 187) were mutated to unphosphorylatable alanine (DUE-B(S/T)-A) or phosphomimic aspartic acid (DUE-B(S/T)-D). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273963 |
Ser197 |
KEDRSASsGAEGDVS |
in vitro |
|
| pmid |
sentence |
| 25258324 |
Here we show that DUE-B is de-phosphorylated in M phase and phosphorylated in G1/S phase. Phosphorylated DUE-B forms homodimers, whereas de-phosphorylated DUE-B interacts with the Mcm2–7 complex and aminoacyl-tRNA synthetases. We find that CKII can prime DUE-B for Cdc7 phosphorylation. Confirming the importance of DUE-B phosphorylation in replication initiation, a C-terminal Ser/Thr to Ala mutant blocks Cdc45 and RPA loading on sperm chromatin and inhibits DNA replication. DUE-B C-terminal phosphorylation sites (serine 179, 181, 182, 194, 196, 197, 204, 205, and threonine 187) were mutated to unphosphorylatable alanine (DUE-B(S/T)-A) or phosphomimic aspartic acid (DUE-B(S/T)-D). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273965 |
Ser204 |
SGAEGDVsSEREP |
in vitro |
|
| pmid |
sentence |
| 25258324 |
Here we show that DUE-B is de-phosphorylated in M phase and phosphorylated in G1/S phase. Phosphorylated DUE-B forms homodimers, whereas de-phosphorylated DUE-B interacts with the Mcm2–7 complex and aminoacyl-tRNA synthetases. We find that CKII can prime DUE-B for Cdc7 phosphorylation. Confirming the importance of DUE-B phosphorylation in replication initiation, a C-terminal Ser/Thr to Ala mutant blocks Cdc45 and RPA loading on sperm chromatin and inhibits DNA replication. DUE-B C-terminal phosphorylation sites (serine 179, 181, 182, 194, 196, 197, 204, 205, and threonine 187) were mutated to unphosphorylatable alanine (DUE-B(S/T)-A) or phosphomimic aspartic acid (DUE-B(S/T)-D). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273969 |
Ser205 |
GAEGDVSsEREP |
in vitro |
|
| pmid |
sentence |
| 25258324 |
Here we show that DUE-B is de-phosphorylated in M phase and phosphorylated in G1/S phase. Phosphorylated DUE-B forms homodimers, whereas de-phosphorylated DUE-B interacts with the Mcm2–7 complex and aminoacyl-tRNA synthetases. We find that CKII can prime DUE-B for Cdc7 phosphorylation. Confirming the importance of DUE-B phosphorylation in replication initiation, a C-terminal Ser/Thr to Ala mutant blocks Cdc45 and RPA loading on sperm chromatin and inhibits DNA replication. DUE-B C-terminal phosphorylation sites (serine 179, 181, 182, 194, 196, 197, 204, 205, and threonine 187) were mutated to unphosphorylatable alanine (DUE-B(S/T)-A) or phosphomimic aspartic acid (DUE-B(S/T)-D). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273964 |
Thr187 |
ESSKERNtPRKEDRS |
in vitro |
|
| pmid |
sentence |
| 25258324 |
Here we show that DUE-B is de-phosphorylated in M phase and phosphorylated in G1/S phase. Phosphorylated DUE-B forms homodimers, whereas de-phosphorylated DUE-B interacts with the Mcm2–7 complex and aminoacyl-tRNA synthetases. We find that CKII can prime DUE-B for Cdc7 phosphorylation. Confirming the importance of DUE-B phosphorylation in replication initiation, a C-terminal Ser/Thr to Ala mutant blocks Cdc45 and RPA loading on sperm chromatin and inhibits DNA replication. DUE-B C-terminal phosphorylation sites (serine 179, 181, 182, 194, 196, 197, 204, 205, and threonine 187) were mutated to unphosphorylatable alanine (DUE-B(S/T)-A) or phosphomimic aspartic acid (DUE-B(S/T)-D). |
|
| Publications: |
9 |
Organism: |
In Vitro |
| + |
CDC7 | up-regulates
phosphorylation
|
PSIP1 |
0.341 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-25763 |
Ser206 |
MVKQPCPsESDIITE |
Homo sapiens |
Leukemia Cell, Lymphoma Cell |
| pmid |
sentence |
| 7231784 |
We now report identification of the cdc7-activator of s-phase kinase (ask) heterodimer as a novel interactor of ledgf. the kinase phosphorylated ledgf in vitro, with ser-206 being the major target, and ledgf phosphorylated at this residue could be detected during s phase of the cell cycle. Ledgf potently stimulated the enzymatic activity of cdc7-ask, increasing phosphorylation of mcm2 in vitro by more than 10-fold. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDC7 |
phosphorylation
|
RAD18 |
0.503 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-170049 |
Ser434 |
IQEVLSSsESDSCNS |
Homo sapiens |
|
| pmid |
sentence |
| 21098111 |
Although the cdc7/rad18 interaction and phosphorylation at s434 are induced by dna damage, s434 was also observed to be phosphorylated basally |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CyclinE/CDK2 | up-regulates activity
phosphorylation
|
CDC7 |
0.585 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250726 |
Thr376 |
QVAPRAGtPGFRAPE |
|
|
| pmid |
sentence |
| 10846177 |
Among four possible Cdk phosphorylation sites of huCdc7, replacement of Thr-376, corresponding to the activating threonine of Cdk, with alanine (T376A mutant) dramatically reduces kinase activity, indicative of kinase activation by phosphorylation of this residue. In vitro, Cdk2-Cyclin E, Cdk2-Cyclin A, and Cdc2-Cyclin B, but not Cdk4-Cyclin D1, phosphorylates the Thr-376 residue of huCdc7, suggesting possible regulation of huCdc7 by Cdks. |
|
| Publications: |
1 |
| + |
CyclinB/CDK1 | up-regulates activity
phosphorylation
|
CDC7 |
0.481 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250643 |
Thr376 |
QVAPRAGtPGFRAPE |
in vitro |
|
| pmid |
sentence |
| 10846177 |
Among four possible Cdk phosphorylation sites of huCdc7, replacement of Thr-376, corresponding to the activating threonine of Cdk, with alanine (T376A mutant) dramatically reduces kinase activity, indicative of kinase activation by phosphorylation of this residue. In vitro, Cdk2-Cyclin E, Cdk2-Cyclin A, and Cdc2-Cyclin B, but not Cdk4-Cyclin D1, phosphorylates the Thr-376 residue of huCdc7, suggesting possible regulation of huCdc7 by Cdks. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CyclinA2/CDK2 | up-regulates activity
phosphorylation
|
CDC7 |
0.604 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250725 |
Thr376 |
QVAPRAGtPGFRAPE |
|
|
| pmid |
sentence |
| 10846177 |
Among four possible Cdk phosphorylation sites of huCdc7, replacement of Thr-376, corresponding to the activating threonine of Cdk, with alanine (T376A mutant) dramatically reduces kinase activity, indicative of kinase activation by phosphorylation of this residue. In vitro, Cdk2-Cyclin E, Cdk2-Cyclin A, and Cdc2-Cyclin B, but not Cdk4-Cyclin D1, phosphorylates the Thr-376 residue of huCdc7, suggesting possible regulation of huCdc7 by Cdks. |
|
| Publications: |
1 |
| + |
CDK1 | up-regulates
phosphorylation
|
CDC7 |
0.551 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-78311 |
Thr376 |
QVAPRAGtPGFRAPE |
Homo sapiens |
|
| pmid |
sentence |
| 10846177 |
Hucdc7 and ask proteins can also be phosphorylated by cdks in vitro. Among four possible cdk phosphorylation sites of hucdc7, replacement of thr-376, corresponding to the activating threonine of cdk, with alanine (t376a mutant) dramatically reduces kinase activity, indicative of kinase activation by phosphorylation of this residue. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Benzofuro(3,2-d)pyrimidin-4(3H)-one, 8-chloro-2-((2S)-2-pyrrolidinyl)- | down-regulates activity 
chemical inhibition
|
CDC7 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261105 |
|
|
Homo sapiens |
Colo-205 Cell |
| pmid |
sentence |
| 22560567 |
In this paper, we disclose the discovery of a potent and selective CDC7 inhibitor, XL413. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDC7 | down-regulates
phosphorylation
|
ESCO1 |
0.442 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-200397 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23314252 |
We show here that eco1 degradation requires the sequential actions of cdk1 and two additional kinases, cdc7-dbf4 and the gsk-3 homolog mck1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDC7 | up-regulates
phosphorylation
|
MCM4 |
0.957 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-169453 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21070963 |
Activation of the eukaryotic replicative dna helicase, the mcm2-7 complex, requires phosphorylation by cdc7/dbf4 (dbf4-dependent kinase or ddk), which, in turn, depends on prior phosphorylation of mcm2-7 by an unknown kinase (or kinases).we propose that the resulting mec1 modification of mcm4 and mcm6 further activates ddk phosphorylation of mcm2-7 ( fig. 7aii ). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDC7 | up-regulates
phosphorylation
|
MCM7 |
0.94 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-169506 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21070963 |
We propose that phosphorylation of mcm4/6 s/tp sites, which are already phosphorylated in g1, allows initial mcm2-7 phosphorylation by ddk and initiation from the first origins of replication ( fig. 7ai ). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CHEK1 | up-regulates
phosphorylation
|
CDC7 |
0.724 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163161 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20068082 |
Chk1 directly phosphorylates essential s-phase kinases cdc7. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CDC7
- 
- 