| + |
Erlin | down-regulates quantity by destabilization 
binding
|
ITPR1 |
0.512 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271915 |
|
|
Rattus fuscipes |
Rat-1 Cell |
| pmid |
sentence |
| 19240031 |
Here we report that the ER membrane protein SPFH1 and its homolog SPFH2 form a heteromeric approximately 2 MDa complex that binds to IP(3)R tetramers immediately after their activation and is required for their processing. The complex is ring-shaped (diameter approximately 250A(),) and RNA interference-mediated depletion of SPFH1 and SPFH2 blocks IP(3)R polyubiquitination and degradation. |
|
| Publications: |
1 |
Organism: |
Rattus Fuscipes |
| + |
Erlin | up-regulates activity 
binding
|
RNF170 |
0.512 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271918 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 21610068 |
In summary, here we present evidence that RNF170 is an E3 ligase that mediates IP3 receptor ubiquitination and processing by the UPP and that it is recruited to activated IP3 receptors by the erlin1/2 complex to which it is constitutively bound. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271917 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 21610068 |
In summary, here we present evidence that RNF170 is an E3 ligase that mediates IP3 receptor ubiquitination and processing by the UPP and that it is recruited to activated IP3 receptors by the erlin1/2 complex to which it is constitutively bound. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ERLIN2 | form complex 
binding
|
Erlin |
0.625 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275393 |
|
|
Rattus fuscipes |
Rat-1 Cell |
| pmid |
sentence |
| 19240031 |
Here we report that the ER membrane protein SPFH1 and its homolog SPFH2 form a heteromeric approximately 2 MDa complex that binds to IP(3)R tetramers immediately after their activation and is required for their processing. The complex is ring-shaped (diameter approximately 250A(),) and RNA interference-mediated depletion of SPFH1 and SPFH2 blocks IP(3)R polyubiquitination and degradation. |
|
| Publications: |
1 |
Organism: |
Rattus Fuscipes |
| + |
ERLIN1 | form complex
binding
|
Erlin |
0.625 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275392 |
|
|
Rattus fuscipes |
Rat-1 Cell |
| pmid |
sentence |
| 19240031 |
Here we report that the ER membrane protein SPFH1 and its homolog SPFH2 form a heteromeric approximately 2 MDa complex that binds to IP(3)R tetramers immediately after their activation and is required for their processing. The complex is ring-shaped (diameter approximately 250A(),) and RNA interference-mediated depletion of SPFH1 and SPFH2 blocks IP(3)R polyubiquitination and degradation. |
|
| Publications: |
1 |
Organism: |
Rattus Fuscipes |
| + |
Erlin | down-regulates quantity by destabilization
binding
|
ITPR2 |
0.359 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271916 |
|
|
Rattus fuscipes |
Rat-1 Cell |
| pmid |
sentence |
| 19240031 |
Here we report that the ER membrane protein SPFH1 and its homolog SPFH2 form a heteromeric approximately 2 MDa complex that binds to IP(3)R tetramers immediately after their activation and is required for their processing. The complex is ring-shaped (diameter approximately 250A(),) and RNA interference-mediated depletion of SPFH1 and SPFH2 blocks IP(3)R polyubiquitination and degradation. |
|
| Publications: |
1 |
Organism: |
Rattus Fuscipes |
3.0
Erlin