| Interaction ID | Mol A | Type | Species | Verb | Nature | Mol B | Type | Species |   |
|---|
|
| 53249 | NFKB1 | Protein | Homo sapiens-e | Bind | direct | RELB | Protein | Homo sapiens | |
| We demonstrate that human RelB (I-Rel) forms
with p50 and p52 (p50B) kappa B-binding heterodimeric
complexes which potently transactivate kappa B-dependent
constructs in transfection studies. | |
| |
Interaction id | 53249 | |
MOLECULE A | |
Id | 4790 |
Type | Protein |
Species | Homo sapiens-e | |
Attribute |
--
|
Structure Details | -- |
Disease Details | -- | |
MOLECULE B | |
Id | 5971 |
Type | Protein |
Species | Homo sapiens | |
Attribute | -- |
Structure Details | -- |
Disease Details | -- | | Kinetics | - | |
|
General Information |
Interaction term | Bind (
direct ) | |
Pathway | Protein Kinase Cascade:I-Kappab Kinase/Nf-Kappab Cascade | |
References | |
PubMed Id | 8183565 | |
Author | Bours V, Azarenko V, Dejardin E, Siebenlist U | |
Title | Human RelB (I-Rel) functions as a kappa B site-dependent
transactivating member of the family of Rel-related proteins. |
|
|
|
|
|
| 130208 | RELB | Protein | Homo sapiens | Bind | direct | NFKB2 | Protein | Homo sapiens-e | |
| We demonstrate that human RelB (I-Rel) forms
with p50 and p52 (p50B) kappa B-binding heterodimeric
complexes which potently transactivate kappa B-dependent
constructs in transfection studies. | |
| |
Interaction id | 130208 | |
MOLECULE A | |
Id | 5971 |
Type | Protein |
Species | Homo sapiens | |
Attribute |
--
|
Structure Details | -- |
Disease Details | -- | |
MOLECULE B | |
Id | 4791 |
Type | Protein |
Species | Homo sapiens-e | |
Attribute | -- |
Structure Details | -- |
Disease Details | -- | | Kinetics | - | |
|
General Information |
Interaction term | Bind (
direct ) | |
Pathway | Protein Kinase Cascade:I-Kappab Kinase/Nf-Kappab Cascade | |
References | |
PubMed Id | 8183565 | |
Author | Bours V, Azarenko V, Dejardin E, Siebenlist U | |
Title | Human RelB (I-Rel) functions as a kappa B site-dependent
transactivating member of the family of Rel-related proteins. |
|
|
|
|
|
| 232122 | RELB | Protein | Homo sapiens-e | Increases stability | direct | Nfkb2 | Protein | Mus musculus | |
| As a model system we used the murine S107
plasmacytoma cell line, which lacks endogenous RelB
expression. Analysis of S107 cells expressing wild type RelB
and serine 368 mutants reveals that serine 368 is not
required for nuclear import but that it is critical for RelB
dimerization with other members of the NFkappaB family. /
We further demonstrate that expression of functional RelB,
but not of serine 368 mutants, severely reduces p52
generation and strongly increases expression of the p52
precursor, p100. Wild type RelB, but not mutant RelB,
prolonged p100 half-life. | |
| |
Interaction id | 232122 | |
MOLECULE A | |
Id | 5971 |
Type | Protein |
Species | Homo sapiens-e | |
Attribute |
--
|
Structure Details | -- |
Disease Details | -- | |
MOLECULE B | |
Id | 18034 |
Type | Protein |
Species | Mus musculus | |
Attribute | -- |
Structure Details | -- |
Disease Details | -- | | Kinetics | - | |
|
General Information |
Interaction term | Increases stability (
direct ) | |
Experimental location and method | - Experimental method::Mutation analysis
- species::Mouse
- cell::S107 cells
| |
Comments | |
Property | | Mutated molecule:RELB(Se368) |
Domain_motif_site_residue | | [RES:Ser368](5971) |
| |
References | |
PubMed Id | 12874295 | |
Author | Maier HJ, Marienfeld R, Wirth T, Baumann B | |
Title | Critical role of RelB serine 368 for dimerization and p100 stabilization. |
|
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Structure