| + |
CSNK2A1 | down-regulates 
phosphorylation
|
SPTBN1 |
0.339 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-150467 |
Ser2110 |
PEPSTKVsEEAESQQ |
Homo sapiens |
|
| pmid |
sentence |
| 17088250 |
We show here that the short c-terminal splice variant of betaii-spectrin (betaiisigma2) is a substrate for phosphorylation. In vitro, protein kinase ck2 phosphorylates ser-2110 and thr-2159 / phosphorylation of ?II?2 C-terminal fragment inhibits its interaction with ?II N-terminal fragment. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-150471 |
Thr2159 |
NGATEQRtSSKESSP |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 17088250 |
We show here that the short c-terminal splice variant of betaii-spectrin (betaiisigma2) is a substrate for phosphorylation. In vitro, protein kinase ck2 phosphorylates ser-2110 and thr-2159 / phosphorylation of ?II?2 C-terminal fragment inhibits its interaction with ?II N-terminal fragment. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKACA | down-regulates activity
phosphorylation
|
SPTBN1 |
0.336 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250054 |
Thr2159 |
NGATEQRtSSKESSP |
in vitro |
|
| pmid |
sentence |
| 17088250 |
Short C-terminal splice variant of betaII-spectrin (betaIISigma2) is a substrate for phosphorylation. protein kinase A phosphorylates Thr-2159. Mammalian alphaII- and betaII-spectrin subunits form dimers that associate head to head with high affinity to form tetramers In vitro, protein kinase A phosphorylation of an active fragment of betaIISigma2 greatly reduced its interaction with alphaII-spectrin at the tetramerization site. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
TGFBR1 | up-regulates 
phosphorylation
|
SPTBN1 |
0.501 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-97626 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12543979 |
This suggests that, upon stimulation with tgf-beta1, phosphorylation of elf could induce a conformational change that reduces its affinity for ankyrin and tropomyosin and facilitates an association with smad3 and smad4 instead. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ANK3 | up-regulates activity
binding
|
SPTBN1 |
0.63 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266711 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 17620337 |
Ankyrin-G is a molecular partner of E-cadherin in epithelial cells and early embryos. Ankyrin-G also recruits beta-2-spectrin to E-cadherin-beta-catenin complexes, thus providing a direct connection between E-cadherin and the spectrin/actin skeleton. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PJA1 | down-regulates
ubiquitination
|
SPTBN1 |
0.413 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141216 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16247473 |
The present study indicates that praja, a ring finger e3 ubiquitin ligase, interacts with elf and ubiquitinates it. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
SPTBN1
- 
- 