| + |
PRKCA | up-regulates activity 
phosphorylation
|
OCLN |
0.364 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249105 |
Ser340 |
DKRFYPEsSYKSTPV |
Canis lupus familiaris |
|
| pmid |
sentence |
| 11502742 |
Protein kinase C regulates the phosphorylation and cellular localization of occludin. Ser(338) of occludin was identified as an in vitro protein kinase C phosphorylation site using peptide mass fingerprint analysis and electrospray ionization tandem mass spectroscopy. Both the phosphorylation of occludin and its incorporation into tight junctions induced by calcium switch were markedly inhibited by the PKC inhibitor GF-109203X. |
|
| Publications: |
1 |
Organism: |
Canis Lupus Familiaris |
| + |
PRKCB | up-regulates activity
phosphorylation
|
OCLN |
0.457 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249106 |
Ser340 |
DKRFYPEsSYKSTPV |
Canis lupus familiaris |
MDCK Cell |
| pmid |
sentence |
| 11502742 |
Protein kinase C regulates the phosphorylation and cellular localization of occludin. Ser(338) of occludin was identified as an in vitro protein kinase C phosphorylation site using peptide mass fingerprint analysis and electrospray ionization tandem mass spectroscopy. Both the phosphorylation of occludin and its incorporation into tight junctions induced by calcium switch were markedly inhibited by the PKC inhibitor GF-109203X. |
|
| Publications: |
1 |
Organism: |
Canis Lupus Familiaris |
| + |
PRKCG | up-regulates activity
phosphorylation
|
OCLN |
0.307 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249107 |
Ser340 |
DKRFYPEsSYKSTPV |
Canis lupus familiaris |
|
| pmid |
sentence |
| 11502742 |
Protein kinase C regulates the phosphorylation and cellular localization of occludin. Ser(338) of occludin was identified as an in vitro protein kinase C phosphorylation site using peptide mass fingerprint analysis and electrospray ionization tandem mass spectroscopy. Both the phosphorylation of occludin and its incorporation into tight junctions induced by calcium switch were markedly inhibited by the PKC inhibitor GF-109203X. |
|
| Publications: |
1 |
Organism: |
Canis Lupus Familiaris |
| + |
CSNK2B |
phosphorylation
|
OCLN |
0.418 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251079 |
Ser408 |
DYTTGGEsCDELEED |
Homo sapiens |
ECV-304 Cell |
| pmid |
sentence |
| 12804768 |
Mutagenesis of serine 407 to alanine resulted in reduced ability of the kinase to phosphorylate occludin. The threonine 403 to alanine mutant had a smaller effect but the double mutant (T403/S407A) was even less phosphorylated than either of the single mutants. These data are consistent with the claim that CK2 is the kinase in brain extracts responsible for phosphorylation of occludin. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251080 |
Thr404 |
HYETDYTtGGESCDE |
Homo sapiens |
|
| pmid |
sentence |
| 12804768 |
Mutagenesis of serine 407 to alanine resulted in reduced ability of the kinase to phosphorylate occludin. The threonine 403 to alanine mutant had a smaller effect but the double mutant (T403/S407A) was even less phosphorylated than either of the single mutants. These data are consistent with the claim that CK2 is the kinase in brain extracts responsible for phosphorylation of occludin. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCE | up-regulates
phosphorylation
|
OCLN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173635 |
Thr404 |
HYETDYTtGGESCDE |
Homo sapiens |
CACO-2 Cell |
| pmid |
sentence |
| 21545357 |
Thr403, thr404, thr424 and thr438 in the occludin c-terminal domain are the predominant sites of pkc_-dependent phosphorylation . The present study demonstrates that pkc_ phosphorylates occludin on specific threonine residues and promotes assembly of epithelial tight junctions. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173639 |
Thr424 |
IREYPPItSDQQRQL |
Homo sapiens |
|
| pmid |
sentence |
| 21545357 |
Thr403, thr404, thr424 and thr438 in the occludin c-terminal domain are the predominant sites of pkc_-dependent phosphorylation . The present study demonstrates that pkc_ phosphorylates occludin on specific threonine residues and promotes assembly of epithelial tight junctions. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173643 |
Thr438 |
LYKRNFDtGLQEYKS |
Homo sapiens |
|
| pmid |
sentence |
| 21545357 |
Thr403, thr404, thr424 and thr438 in the occludin c-terminal domain are the predominant sites of pkc_-dependent phosphorylation . The present study demonstrates that pkc_ phosphorylates occludin on specific threonine residues and promotes assembly of epithelial tight junctions. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney |
| + |
ITCH | down-regulates quantity by destabilization 
ubiquitination
|
OCLN |
0.349 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278756 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28542131 |
Two mechanisms regarding junction protein turnover were illustrated in this process, that is, the Itch-induced occludin ubiquitination and proteasome degradation, and the caveolae-dependent endocytosis of junction proteins (JAM-A, N-cadherin, and \u03b2 -catenin), both of which led to the instability of junction apparatus between adjacent SCs and a subsequent damaged BTB. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
OCLN
- 
- 