Rela
entrez
19697
canonical
uniprot
Q04207
canonical
ensembl
ENSMUSG00000024927
resolver
ensp
ENSMUSP00000025867
resolver
genesymbol
Rela
resolver
genesymbol_syn
Nfkb3
resolver
uniprot
Q548Y4
resolver
uniprot
Q62025
resolver
uniprot_entry
Q548Y4_MOUSE
resolver
uniprot_entry
TF65_MOUSE
resolver
uniprot_sec
Q62025
resolver
amino_acid_sequence
MDDLFPLIFPSEPAQASGPYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINGYTGPGTVRISLVTKDPPHRPHPHELVGKDCRDGYYEADLCPDRSIHSFQNLGIQCVKKRDLEQAISQRIQTNNNPFHVPIEEQRGDYDLNAVRLCFQVTVRDPAGRPLLLTPVLSHPIFDNRAPNTAELKICRVNRNSGSCLGGDEIFLLCDKVQKEDIEVYFTGPGWEARGSFSQADVHRQVAIVFRTPPYADPSLQAPVRVSMQLRRPSDRELSEPMEFQYLPDTDDRHRIEEKRKRTYETFKSIMKKSPFNGPTEPRPPTRRIAVPTRNSTSVPKPAPQPYTFPASLSTINFDEFSPMLLPSGQISNQALALAPSSAPVLAQTMVPSSAMVPLAQPPAPAPVLTPGPPQSLSAPVPKSTQAGEGTLSEALLHLQFDADEDLGALLGNSTDPGVFTDLASVDNSEFQQLLNQGVSMSHSTAEPMLMEYPEAITRLVTGSQRPPDPAPTPLGTSGLPNGLSGDEDFSSIADMDFSALLSQISS
uniprot
proteins
function
FUNCTION: NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes 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 heterodimeric RELA-NFKB1 complex appears to be most abundant one. 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. The NF-kappa-B heterodimeric RELA-NFKB1 and RELA-REL complexes, for instance, function as transcriptional activators. 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. The inhibitory effect of I-kappa-B on NF-kappa-B through retention in the cytoplasm is exerted primarily through the interaction with RELA. RELA shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappa-B complex. Besides its activity as a direct transcriptional activator, it is also able to modulate promoters accessibility to transcription factors and thereby indirectly regulate gene expression (PubMed:29813070). Associates with chromatin at the NF-kappa-B promoter region via association with DDX1. Essential for cytokine gene expression in T-cells (By similarity). The NF-kappa-B homodimeric RELA-RELA complex appears to be involved in invasin-mediated activation of IL-8 expression (By similarity). {ECO:0000250|UniProtKB:Q04206, ECO:0000269|PubMed:21131967, ECO:0000269|PubMed:22244329, ECO:0000269|PubMed:29813070}.
uniprot
proteins
mass_dalton
60212
uniprot
proteins
mutagenesis
MUTAGEN 38; /note="C->S: Abolishes sulfhydration and impairs interaction with RPS3."; /evidence="ECO:0000269|PubMed:22244329"; MUTAGEN 281; /note="S->A,E: Abolishes DNA-binding and transcriptional activity."; /evidence="ECO:0000269|PubMed:12874295"; MUTAGEN 310; /note="K->R: Abolishes monomethylation by SETD6 and interaction with EHMT1."; /evidence="ECO:0000269|PubMed:21131967"; MUTAGEN 361..370; /note="DEFSPMLLPS->AAAAAAAAAA: Loss of interaction with ZBTB7A."; /evidence="ECO:0000269|PubMed:29813070
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by MKRN2, leading to its proteasomal degradation (PubMed:28378844). Degradation is required for termination of NF-kappa-B response (By similarity). Polyubiquitinated via 'Lys-29'-linked ubiquitin; leading to lysosomal degradation (By similarity). {ECO:0000250|UniProtKB:Q04206, ECO:0000269|PubMed:28378844}.; PTM: Monomethylated at Lys-310 by SETD6. Monomethylation at Lys-310 is recognized by the ANK repeats of EHMT1 and promotes the formation of repressed chromatin at target genes, leading to down-regulation of NF-kappa-B transcription factor activity. Phosphorylation at Ser-311 disrupts the interaction with EHMT1 without preventing monomethylation at Lys-310 and relieves the repression of target genes. {ECO:0000269|PubMed:12881425, ECO:0000269|PubMed:21131967}.; PTM: Phosphorylation at Ser-467 and Ser-534 by IKKB/IKBKB and IKKE/IKBKE promotes NF-kappa-B activity (By similarity). Phosphorylation on Ser-534 by IKKB/IKBKB and IKKE/IKBKE stimulates acetylation on Lys-311 and interaction with CBP; the phosphorylated and acetylated forms show enhanced transcriptional activity (By similarity). Phosphorylation at Ser-276 by RPS6KA4 and RPS6KA5 promotes its transactivation and transcriptional activities (By similarity). Phosphorylation at Ser-311 disrupts the interaction with EHMT1 and promotes transcription factor activity (PubMed:12881425, PubMed:21131967). {ECO:0000250|UniProtKB:Q04206, ECO:0000269|PubMed:12881425, ECO:0000269|PubMed:21131967}.; PTM: Reversibly acetylated; the acetylation seems to be mediated by CBP, the deacetylation by HDAC3 and SIRT2. Acetylation at Lys-122 enhances DNA binding and impairs association with NFKBIA. Acetylation at Lys-310 is required for full transcriptional activity in the absence of effects on DNA binding and NFKBIA association. Acetylation at Lys-310 promotes interaction with BRD4. Acetylation can also lower DNA-binding and results in nuclear export. Interaction with BRMS1 promotes deacetylation of Lys-310. Lys-310 is deacetylated by SIRT2 (By similarity). {ECO:0000250}.; PTM: S-nitrosylation of Cys-38 inactivates the enzyme activity. {ECO:0000269|PubMed:22244329}.; PTM: Sulfhydration at Cys-38 mediates the anti-apoptotic activity by promoting the interaction with RPS3 and activating the transcription factor activity.; PTM: Sumoylation by PIAS3 negatively regulates DNA-bound activated NF-kappa-B. {ECO:0000250}.; PTM: Proteolytically cleaved within a conserved N-terminus region required for base-specific contact with DNA in a CPEN1-mediated manner, and hence inhibits NF-kappa-B transcriptional activity. {ECO:0000250|UniProtKB:Q04206}.; PTM: Ubiquitinated by the SCF-FBXO16 E3 ubiquitin ligase, leading to proteasomal degradation. {ECO:0000250|UniProtKB:Q04206}.
uniprot
proteins
pubmed
11931770
uniprot
proteins
pubmed
12874295
uniprot
proteins
pubmed
12881425
uniprot
proteins
pubmed
15051764
uniprot
proteins
pubmed
15485901
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15616592
uniprot
proteins
pubmed
18710934
uniprot
proteins
pubmed
2001591
uniprot
proteins
pubmed
21131967
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22244329
uniprot
proteins
pubmed
22895791
uniprot
proteins
pubmed
22921934
uniprot
proteins
pubmed
23616576
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
25024434
uniprot
proteins
pubmed
28378844
uniprot
proteins
pubmed
28600438
uniprot
proteins
pubmed
29813070
uniprot
proteins
pubmed
33939070
uniprot
proteins
pubmed
8281153
uniprot
proteins
pubmed
8816457
uniprot
proteins
pubmed
8918242
uniprot
proteins
pubmed
9437432
uniprot
proteins
pubmed
9450761
uniprot
proteins
pubmed
9865694
uniprot
proteins
pubmed
9990853
uniprot
proteins
sequence_length
549
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21131967, ECO:0000269|PubMed:28378844}. Cytoplasm {ECO:0000269|PubMed:21131967}. Note=Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B) (PubMed:21131967). Colocalized with DDX1 in the nucleus upon TNF induction (By similarity). Colocalizes with GFI1 in the nucleus after lipopolysaccharide (LPS) stimulation. {ECO:0000250|UniProtKB:Q04206, ECO:0000269|PubMed:21131967}.
uniprot
proteins