RELB

RELB (RELB Proto-Oncogene, NF-KB Subunit) is a Protein Coding gene. Diseases associated with RELB include Immunodeficiency 53 and Reticuloendotheliosis. Among its related pathways are RANK Signaling in Osteoclasts and Bacterial infections in CF airways. Gene Ontology (GO) annotations related to this gene include DNA binding transcription factor activity and transcription corepressor activity. An important paralog of this gene is RELA.

RELB

NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric RelB-p50 and RelB-p52 complexes are transcriptional activators. RELB neither associates with DNA nor with RELA/p65 or REL. Stimulates promoter activity in the presence of NFKB2/p49. As a member of the NUPR1/RELB/IER3 survival pathway, may provide pancreatic ductal adenocarcinoma with remarkable resistance to cell stress, such as starvation or gemcitabine treatment. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer in a CRY1/CRY2 independent manner. Increased repression of the heterodimer is seen in the presence of NFKB2/p52. Is required for both T and B lymphocyte maturation and function (PubMed:26385063).

Antigen processing and presentationIEA:Ensembl
Cellular response to osmotic stressIEA:Ensembl
Circadian regulation of gene expressionISS:UniProtKB
I-kappaB kinase/NF-kappaB signalingManual Assertion Based On ExperimentIBA:GO_Central
Inflammatory responseManual Assertion Based On ExperimentIBA:GO_Central
Innate immune responseManual Assertion Based On ExperimentIBA:GO_Central
Lymphocyte differentiationManual Assertion Based On ExperimentIMP:UniProtKB
Myeloid dendritic cell differentiationIEA:Ensembl
Negative regulation of interferon-beta productionManual Assertion Based On ExperimentIMP:CACAO
Negative regulation of transcription, DNA-templatedIEA:Ensembl
NIK/NF-kappaB signalingManual Assertion Based On ExperimentIBA:GO_Central
Positive regulation of gene expressionIEA:Ensembl
Positive regulation of transcription by RNA polymerase II1 PublicationIC:ComplexPortal
Regulation of transcription by RNA polymerase IIManual Assertion Based On ExperimentIBA:GO_Central
Response to cytokineManual Assertion Based On ExperimentIBA:GO_Central
T-helper 1 cell differentiationIEA:Ensembl

Nucleus
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
Colocalizes with NEK6 in the centrosome.

Immunodeficiency 53 (IMD53):
An autosomal recessive primary immunodeficiency apparent from early infancy and resulting in recurrent infections, severe autoimmune skin disease rheumatoid arthritis, and failure to thrive. Immunologic workup shows increased CD4+/CD8+ ratio, impaired T-cell proliferative response to multiple antigen, T-cell developmental and functional defects, and impaired ability to produce specific immunoglobulins.

Phosphorylation at 'Thr-103' and 'Ser-573' is followed by proteasomal degradation.