| + |
SYK |
phosphorylation
|
SLC4A1 |
0.462 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251411 |
Tyr21 |
ENLEQEEyEDPDIPE |
in vitro |
|
| pmid |
sentence |
| 10942405 |
The primary phosphorylation of band 3 catalyzed by p72syk generates the SH2 binding motifs that are a prerequisite for the following recruitment of Lyn. p72syk as the most likely candidate to perform this task and indicates Y8 and Y21. Syk and Lyn phosphorylate band 3 at both cytosolic and membrane domains, Y-phosphorylation/dephosphorylation is likely involved in the regulation of several erythrocyte functions (ie, glycolysis, cell shape, cytoskeleton |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251413 |
Tyr8 |
MEELQDDyEDMMEEN |
in vitro |
|
| pmid |
sentence |
| 10942405 |
The primary phosphorylation of band 3 catalyzed by p72syk generates the SH2 binding motifs that are a prerequisite for the following recruitment of Lyn. p72syk as the most likely candidate to perform this task and indicates Y8 and Y21. Syk and Lyn phosphorylate band 3 at both cytosolic and membrane domains, Y-phosphorylation/dephosphorylation is likely involved in the regulation of several erythrocyte functions (ie, glycolysis, cell shape, cytoskeleton |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
SYK | up-regulates 
phosphorylation
|
SLC4A1 |
0.462 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-80788 |
Tyr21 |
ENLEQEEyEDPDIPE |
Homo sapiens |
|
| pmid |
sentence |
| 10942405 |
Our findings suggest that, upon phosphorylation by p72syk, y8 and y21 act as docking sites for the sh2 domain of lyn, which subsequently phosphorylates band 3 at additional secondary sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-80792 |
Tyr8 |
MEELQDDyEDMMEEN |
Homo sapiens |
|
| pmid |
sentence |
| 10942405 |
Our findings suggest that, upon phosphorylation by p72syk, y8 and y21 act as docking sites for the sh2 domain of lyn, which subsequently phosphorylates band 3 at additional secondary sites. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
LYN |
phosphorylation
|
SLC4A1 |
0.343 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251412 |
Tyr359 |
AKPDSSFyKGLDLNG |
in vitro |
|
| pmid |
sentence |
| 10942405 |
Lyn phosphorylates Y904 and Y359 of band 3. The primary phosphorylation of band 3 catalyzed by p72syk generates the SH2 binding motifs that are a prerequisite for the following recruitment of Lyn. p72syk as the most likely candidate to perform this task and indicates Y8 and Y21. Syk and Lyn phosphorylate band 3 at both cytosolic and membrane domains, Y-phosphorylation/dephosphorylation is likely involved in the regulation of several erythrocyte functions (ie, glycolysis, cell shape, cytoskeleton movements, and anion transport. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251414 |
Tyr904 |
EEEGRDEyDEVAMPV |
in vitro |
|
| pmid |
sentence |
| 10942405 |
Lyn phosphorylates Y904 and Y359 of band 3. The primary phosphorylation of band 3 catalyzed by p72syk generates the SH2 binding motifs that are a prerequisite for the following recruitment of Lyn. p72syk as the most likely candidate to perform this task and indicates Y8 and Y21. Syk and Lyn phosphorylate band 3 at both cytosolic and membrane domains, Y-phosphorylation/dephosphorylation is likely involved in the regulation of several erythrocyte functions (ie, glycolysis, cell shape, cytoskeleton movements, and anion transport. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
SLC4A1 | form complex 
binding
|
Ankyrin complex |
0.416 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266015 |
|
|
Homo sapiens |
Erythrocyte |
| pmid |
sentence |
| 22465511 |
The ankyrin associated complex brings together proteins of both the band 3 tetrameric complex (band 3, glycophorin A (GPA), protein 4.2, carbonic anhydrase II) and the Rh complex (RhAG, RhCE, RhD, CD47, ICAM-4, glycophorin B (GPB)) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SLC4A1 | form complex
binding
|
4.1 complex |
0.386 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266036 |
|
|
Homo sapiens |
Erythrocyte |
| pmid |
sentence |
| 33187473 |
The cytoskeleton plays a key role in maintaining the morphology and function of erythrocyte membranes. Many proteins, such as ankyrin, spectrin alpha- and beta-chains, proteins 4.1, or 4.1R and actin, cover the inner surface of the erythrocyte membrane to form two protein complexes, the ankyrin and protein 4.1 complex| the latter consists of Band 3 dimers binding Adducins alpha and beta, Glycophorin C, GLUT1 and Stomatin [15, 16] |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
SLC4A1
- 
- 