| + |
PRKACA |
phosphorylation
|
SCRIB |
0.252 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263066 |
Ser1445 |
PSPTSRQsPASPPPL |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 20622900 |
HScrib is a substrate of ERK and PKA. Under normal growth conditions, hScrib is phosphorylated at S853, most likely by ERK, and at S1445 by PKA. Interestingly, stimulation of MAPK by osmotic stress results in a marked loss of phosphorylation at the PKA site S1445, but a concomitant increase in phosphorylation at S1448, presumably also by ERK. At present, we have no information as to what are the functional consequences of ERK or PKA phosphorylation of hScrib. However, we can speculate that this will most likely affect the ability of hScrib to interact with some of its cellular partners, and studies are currently in progress to investigate these aspects further. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERK1/2 |
phosphorylation
|
SCRIB |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263064 |
Ser1448 |
TSRQSPAsPPPLGGG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 20622900 |
HScrib is a substrate of ERK and PKA. Under normal growth conditions, hScrib is phosphorylated at S853, most likely by ERK, and at S1445 by PKA. Interestingly, stimulation of MAPK by osmotic stress results in a marked loss of phosphorylation at the PKA site S1445, but a concomitant increase in phosphorylation at S1448, presumably also by ERK. At present, we have no information as to what are the functional consequences of ERK or PKA phosphorylation of hScrib. However, we can speculate that this will most likely affect the ability of hScrib to interact with some of its cellular partners, and studies are currently in progress to investigate these aspects further. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263065 |
Ser853 |
LPLLPPEsPGPLRQR |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 20622900 |
HScrib is a substrate of ERK and PKA. Under normal growth conditions, hScrib is phosphorylated at S853, most likely by ERK, and at S1445 by PKA. Interestingly, stimulation of MAPK by osmotic stress results in a marked loss of phosphorylation at the PKA site S1445, but a concomitant increase in phosphorylation at S1448, presumably also by ERK. At present, we have no information as to what are the functional consequences of ERK or PKA phosphorylation of hScrib. However, we can speculate that this will most likely affect the ability of hScrib to interact with some of its cellular partners, and studies are currently in progress to investigate these aspects further. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
SCRIB | form complex 
binding
|
Scribble_complex_DLG5-LLGL1_variant |
0.445 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270900 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23397623 |
The Scribble polarity complex or module is one of the three polarity modules that regulate cell polarity in multiple epithelia including blood-tissue barriers. This protein complex is composed of Scribble, Lethal giant larvae (Lgl) and Discs large (Dlg), which are well conserved across species from fruitflies and worms to mammals. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCRIB | form complex
binding
|
Scribble_complex_DLG2-LLGL1_variant |
0.532 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270908 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23397623 |
The Scribble polarity complex or module is one of the three polarity modules that regulate cell polarity in multiple epithelia including blood-tissue barriers. This protein complex is composed of Scribble, Lethal giant larvae (Lgl) and Discs large (Dlg), which are well conserved across species from fruitflies and worms to mammals. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCRIB | down-regulates activity 
binding
|
ERK1/2 |
0.373 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263067 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 20622900 |
These two KIM sites are found at N- and C-terminal locations on hScrib, and both are essential for directing the interaction between ERK and hScrib, but with the C-terminal site having the strongest affinity for ERK. One of the most likely consequences of this interaction is to inhibit ERK translocation to the nucleus. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UBE3A | down-regulates quantity by destabilization
polyubiquitination
|
SCRIB |
0.536 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272573 |
|
|
in vitro |
|
| pmid |
sentence |
| 11027293 |
Human scribble (Vartul) is targeted for ubiquitin-mediated degradation by the high-risk papillomavirus E6 proteins and the E6AP ubiquitin-protein ligase |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CTNNB1 | up-regulates activity 
binding
|
SCRIB |
0.431 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265826 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 21255999 |
Cadherins mediate the localization of vesicles to presynaptic compartments through multiple mechanisms. Cadherin-bound β-catenin then recruits scribble (Scrib) which acts as a scaffold for the further recruitment of proteins that mediate the localization of SVs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Neurotransmitters release |
| + |
SCRIB | form complex
binding
|
Scribble_complex_DLG5-LLGL2_variant |
0.45 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270892 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23397623 |
The Scribble polarity complex or module is one of the three polarity modules that regulate cell polarity in multiple epithelia including blood-tissue barriers. This protein complex is composed of Scribble, Lethal giant larvae (Lgl) and Discs large (Dlg), which are well conserved across species from fruitflies and worms to mammals. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCRIB | form complex
binding
|
Scribble_complex_DLG2-LLGL2_variant |
0.538 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270880 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23397623 |
The Scribble polarity complex or module is one of the three polarity modules that regulate cell polarity in multiple epithelia including blood-tissue barriers. This protein complex is composed of Scribble, Lethal giant larvae (Lgl) and Discs large (Dlg), which are well conserved across species from fruitflies and worms to mammals. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCRIB | up-regulates 
|
Synaptic_vesicle_exocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265827 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 19458197 |
Our data supports a model by which scribble functions downstream of beta-catenin to cluster synaptic vesicles at developing synapses. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Neurotransmitters release |
| + |
SCRIB | form complex
binding
|
Scribble_complex_DLG1-LLGL1_variant |
0.541 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270912 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23397623 |
The Scribble polarity complex or module is one of the three polarity modules that regulate cell polarity in multiple epithelia including blood-tissue barriers. This protein complex is composed of Scribble, Lethal giant larvae (Lgl) and Discs large (Dlg), which are well conserved across species from fruitflies and worms to mammals. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCRIB | form complex
binding
|
Scribble_complex_DLG3-LLGL1_variant |
0.531 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270896 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23397623 |
The Scribble polarity complex or module is one of the three polarity modules that regulate cell polarity in multiple epithelia including blood-tissue barriers. This protein complex is composed of Scribble, Lethal giant larvae (Lgl) and Discs large (Dlg), which are well conserved across species from fruitflies and worms to mammals. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCRIB | form complex
binding
|
Scribble_complex_DLG4-LLGL2_variant |
0.529 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270888 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23397623 |
The Scribble polarity complex or module is one of the three polarity modules that regulate cell polarity in multiple epithelia including blood-tissue barriers. This protein complex is composed of Scribble, Lethal giant larvae (Lgl) and Discs large (Dlg), which are well conserved across species from fruitflies and worms to mammals. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCRIB | form complex
binding
|
Scribble_complex_DLG4-LLGL1_variant |
0.523 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270904 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23397623 |
The Scribble polarity complex or module is one of the three polarity modules that regulate cell polarity in multiple epithelia including blood-tissue barriers. This protein complex is composed of Scribble, Lethal giant larvae (Lgl) and Discs large (Dlg), which are well conserved across species from fruitflies and worms to mammals. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCRIB | form complex
binding
|
Scribble_complex_DLG3-LLGL2_variant |
0.536 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270884 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23397623 |
The Scribble polarity complex or module is one of the three polarity modules that regulate cell polarity in multiple epithelia including blood-tissue barriers. This protein complex is composed of Scribble, Lethal giant larvae (Lgl) and Discs large (Dlg), which are well conserved across species from fruitflies and worms to mammals. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
SCRIB
- 
- 