| + |
MAPK7 | down-regulates activity 
phosphorylation
|
GJA1 |
0.527 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250115 |
Ser255 |
HATSGALsPAKDCGS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12637502 |
Activated BMK1 selectively phosphorylates Cx43 on Ser-255 in vitro and in vivo. These data demonstrate that BMK1 kinase activity alone is both a necessary and sufficient component in the mediation of EGF-induced Cx43 Ser-255 phosphorylation and subsequent inhibition of GJC. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK1 | down-regulates activity
phosphorylation
|
GJA1 |
0.598 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249401 |
Ser255 |
HATSGALsPAKDCGS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 9535909 |
These studies confirm that connexin-43 is a MAP kinase substrate in vivo and that phosphorylation on Ser255, Ser279, and/or Ser282 initiates the down-regulation of gap junctional communication. Studies with connexin-43 mutants suggest that MAP kinase phosphorylation at one or more of the tandem Ser279/Ser282 sites is sufficient to disrupt gap junctional intercellular communication. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249402 |
Ser279 |
SSPTAPLsPMSPPGY |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 9535909 |
These studies confirm that connexin-43 is a MAP kinase substrate in vivo and that phosphorylation on Ser255, Ser279, and/or Ser282 initiates the down-regulation of gap junctional communication. Studies with connexin-43 mutants suggest that MAP kinase phosphorylation at one or more of the tandem Ser279/Ser282 sites is sufficient to disrupt gap junctional intercellular communication. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249403 |
Ser282 |
TAPLSPMsPPGYKLV |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 9535909 |
These studies confirm that connexin-43 is a MAP kinase substrate in vivo and that phosphorylation on Ser255, Ser279, and/or Ser282 initiates the down-regulation of gap junctional communication. Studies with connexin-43 mutants suggest that MAP kinase phosphorylation at one or more of the tandem Ser279/Ser282 sites is sufficient to disrupt gap junctional intercellular communication. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
MAPK3 | down-regulates activity
phosphorylation
|
GJA1 |
0.629 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249465 |
Ser255 |
HATSGALsPAKDCGS |
Homo sapiens |
|
| pmid |
sentence |
| 9535909 |
These studies confirm that connexin-43 is a MAP kinase substrate in vivo and that phosphorylation on Ser255, Ser279, and/or Ser282 initiates the down-regulation of gap junctional communication. Studies with connexin-43 mutants suggest that MAP kinase phosphorylation at one or more of the tandem Ser279/Ser282 sites is sufficient to disrupt gap junctional intercellular communication. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249466 |
Ser279 |
SSPTAPLsPMSPPGY |
Homo sapiens |
|
| pmid |
sentence |
| 9535909 |
These studies confirm that connexin-43 is a MAP kinase substrate in vivo and that phosphorylation on Ser255, Ser279, and/or Ser282 initiates the down-regulation of gap junctional communication. Studies with connexin-43 mutants suggest that MAP kinase phosphorylation at one or more of the tandem Ser279/Ser282 sites is sufficient to disrupt gap junctional intercellular communication. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249467 |
Ser282 |
TAPLSPMsPPGYKLV |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 9535909 |
These studies confirm that connexin-43 is a MAP kinase substrate in vivo and that phosphorylation on Ser255, Ser279, and/or Ser282 initiates the down-regulation of gap junctional communication. Studies with connexin-43 mutants suggest that MAP kinase phosphorylation at one or more of the tandem Ser279/Ser282 sites is sufficient to disrupt gap junctional intercellular communication. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PRKCA | down-regulates
phosphorylation
|
GJA1 |
0.548 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120907 |
Ser262 |
SPAKDCGsQKYAYFN |
Homo sapiens |
|
| pmid |
sentence |
| 14702389 |
Using immunoblotting and phosphospecific antibodies we were able to show that serine-262 (s262) on cx43 becomes phosphorylated in response to growth factor or pkc stimulation of cardiomyocytes.In cell-cell contact forming cultures, the s262d mutation reversed while the s262a mutation increased the inhibitory effect of cx43.Phosphorylation at s262, a pkc site that becomes phosphorylated in the cell environment in response to growth factor stimulation, cancels cx43 inhibition only in contact-forming myocytes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK1D | up-regulates activity 
phosphorylation
|
GJA1 |
0.59 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249329 |
Ser325 |
NRMGQAGsTISNSHA |
Rattus norvegicus |
Kidney Cell Line |
| pmid |
sentence |
| 12270943 |
We have examined the role of casein kinase 1 (CK1) in connexin-43 (Cx43) gap junction assembly. Cellular co-immunoprecipitation experiments and in vitro CK1 phosphorylation reactions indicate that CK1 interacted with and phosphorylated Cx43, initially on serine(s) 325, 328, or 330.| To examine CK1 function, normal rat kidney cells were treated with CKI-7, and Cx43 content was analyzed by Triton X-100 extraction, cell-surface biotinylation, and immunofluorescence. Western blot analysis indicated a slight increase in total Cx43, whereas gap junctional (Triton-insoluble) Cx43 decreased, and non-junctional plasma membrane Cx43 increased (as detected by cell surface biotinylation). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249330 |
Ser328 |
GQAGSTIsNSHAQPF |
Rattus norvegicus |
Kidney Cell Line |
| pmid |
sentence |
| 12270943 |
We have examined the role of casein kinase 1 (CK1) in connexin-43 (Cx43) gap junction assembly. Cellular co-immunoprecipitation experiments and in vitro CK1 phosphorylation reactions indicate that CK1 interacted with and phosphorylated Cx43, initially on serine(s) 325, 328, or 330.| To examine CK1 function, normal rat kidney cells were treated with CKI-7, and Cx43 content was analyzed by Triton X-100 extraction, cell-surface biotinylation, and immunofluorescence. Western blot analysis indicated a slight increase in total Cx43, whereas gap junctional (Triton-insoluble) Cx43 decreased, and non-junctional plasma membrane Cx43 increased (as detected by cell surface biotinylation). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249331 |
Ser330 |
AGSTISNsHAQPFDF |
Rattus norvegicus |
Kidney Cell Line |
| pmid |
sentence |
| 12270943 |
We have examined the role of casein kinase 1 (CK1) in connexin-43 (Cx43) gap junction assembly. Cellular co-immunoprecipitation experiments and in vitro CK1 phosphorylation reactions indicate that CK1 interacted with and phosphorylated Cx43, initially on serine(s) 325, 328, or 330.| To examine CK1 function, normal rat kidney cells were treated with CKI-7, and Cx43 content was analyzed by Triton X-100 extraction, cell-surface biotinylation, and immunofluorescence. Western blot analysis indicated a slight increase in total Cx43, whereas gap junctional (Triton-insoluble) Cx43 decreased, and non-junctional plasma membrane Cx43 increased (as detected by cell surface biotinylation). |
|
| Publications: |
3 |
Organism: |
Rattus Norvegicus |
| + |
PRKCE | up-regulates
phosphorylation
|
GJA1 |
0.448 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-144461 |
Ser365 |
IVDQRPSsRASSRAS |
Homo sapiens |
|
| pmid |
sentence |
| 16474210 |
We previously showed that follicle-stimulating hormone (fsh) promoted phosphorylation of cx43 in rat primary granulosa cells. We further identified ser365, ser368, ser369, and ser373 in the carboxy-terminal tail as the major sites of phosphorylation by fsh, and found that the phosphorylation of these residues was essential for channel activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-144469 |
Ser369 |
RPSSRASsRASSRPR |
Homo sapiens |
|
| pmid |
sentence |
| 16474210 |
We previously showed that follicle-stimulating hormone (fsh) promoted phosphorylation of cx43 in rat primary granulosa cells. We further identified ser365, ser368, ser369, and ser373 in the carboxy-terminal tail as the major sites of phosphorylation by fsh, and found that the phosphorylation of these residues was essential for channel activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-144473 |
Ser373 |
RASSRASsRPRPDDL |
Homo sapiens |
|
| pmid |
sentence |
| 16474210 |
We previously showed that follicle-stimulating hormone (fsh) promoted phosphorylation of cx43 in rat primary granulosa cells. We further identified ser365, ser368, ser369, and ser373 in the carboxy-terminal tail as the major sites of phosphorylation by fsh, and found that the phosphorylation of these residues was essential for channel activity. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PRKCG | down-regulates activity
phosphorylation
|
GJA1 |
0.582 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249050 |
Ser368 |
QRPSSRAsSRASSRP |
Rattus norvegicus |
|
| pmid |
sentence |
| 10871288 |
Phosphorylation of connexin43 on serine368 by protein kinase C regulates gap junctional communication.|These data strongly suggest that PKC directly phosphorylates Cx43 on S368 in vivo, which results in a change in single channel behavior that contributes to a decrease in intercellular communication. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PRKCE | down-regulates activity
phosphorylation
|
GJA1 |
0.448 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-144465 |
Ser368 |
QRPSSRAsSRASSRP |
Rattus norvegicus |
|
| pmid |
sentence |
| 10871288 |
Phosphorylation of connexin43 on serine368 by protein kinase C regulates gap junctional communication.|These data strongly suggest that PKC directly phosphorylates Cx43 on S368 in vivo, which results in a change in single channel behavior that contributes to a decrease in intercellular communication. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PRKCB | down-regulates activity
phosphorylation
|
GJA1 |
0.393 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249049 |
Ser368 |
QRPSSRAsSRASSRP |
Rattus norvegicus |
|
| pmid |
sentence |
| 10871288 |
Phosphorylation of connexin43 on serine368 by protein kinase C regulates gap junctional communication.|These data strongly suggest that PKC directly phosphorylates Cx43 on S368 in vivo, which results in a change in single channel behavior that contributes to a decrease in intercellular communication. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PRKCA | down-regulates activity
phosphorylation
|
GJA1 |
0.548 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249048 |
Ser368 |
QRPSSRAsSRASSRP |
Rattus norvegicus |
|
| pmid |
sentence |
| 10871288 |
Phosphorylation of connexin43 on serine368 by protein kinase C regulates gap junctional communication.|These data strongly suggest that PKC directly phosphorylates Cx43 on S368 in vivo, which results in a change in single channel behavior that contributes to a decrease in intercellular communication. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PTPN2 | up-regulates
dephosphorylation
|
GJA1 |
0.33 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-205097 |
Tyr247 |
VKGKSDPyHATSGAL |
Homo sapiens |
|
| pmid |
sentence |
| 24849651 |
Tc-ptp dephosphorylates cx43 residues y247 and y265, dephosphorylation maintained cx43 gap junctions at the plaque and partially reversed the channel closure caused by v-src-mediated phosphorylation of cx43. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-205101 |
Tyr265 |
KDCGSQKyAYFNGCS |
Homo sapiens |
|
| pmid |
sentence |
| 24849651 |
Tc-ptp dephosphorylates cx43 residues y247 and y265, dephosphorylation maintained cx43 gap junctions at the plaque and partially reversed the channel closure caused by v-src-mediated phosphorylation of cx43. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney |
| + |
SRC | down-regulates
phosphorylation
|
GJA1 |
0.605 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-148913 |
Tyr247 |
VKGKSDPyHATSGAL |
Homo sapiens |
|
| pmid |
sentence |
| 16916748 |
The oncogenic tyrosine kinase, v-src, phosphorylates connexin43 (cx43) on y247 and y265 and inhibits cx43 gap junctional communication (gjc), the process of intercellular exchange of ions and metabolites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-148917 |
Tyr265 |
KDCGSQKyAYFNGCS |
Homo sapiens |
|
| pmid |
sentence |
| 16916748 |
The oncogenic tyrosine kinase, v-src, phosphorylates connexin43 (cx43) on y247 and y265 and inhibits cx43 gap junctional communication (gjc), the process of intercellular exchange of ions and metabolites. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
Gbeta | down-regulates activity
phosphorylation
|
GJA1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270025 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 9535909 |
These studies confirm that connexin-43 is a MAP kinase substrate in vivo and that phosphorylation on Ser255, Ser279, and/or Ser282 initiates the down-regulation of gap junctional communication. Studies with connexin-43 mutants suggest that MAP kinase phosphorylation at one or more of the tandem Ser279/Ser282 sites is sufficient to disrupt gap junctional intercellular communication. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERK1/2 | down-regulates activity
phosphorylation
|
GJA1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270148 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 9535909 |
These studies confirm that connexin-43 is a MAP kinase substrate in vivo and that phosphorylation on Ser255, Ser279, and/or Ser282 initiates the down-regulation of gap junctional communication. Studies with connexin-43 mutants suggest that MAP kinase phosphorylation at one or more of the tandem Ser279/Ser282 sites is sufficient to disrupt gap junctional intercellular communication. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IRX3 | down-regulates quantity by repression
transcriptional regulation
|
GJA1 |
0.282 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266044 |
|
|
Mus musculus |
Cardiomyocyte Cell Line |
| pmid |
sentence |
| 21825130 |
Irx3 directly represses Cx43 transcription |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
3.0
GJA1
- 
- 