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Entry version 234 (16 Oct 2019)
Sequence version 2 (26 Apr 2005)
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Protein

Transcription factor p65

Gene

RELA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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. Beside its activity as a direct transcriptional activator, it is also able to modulate promoters accessibility to transcription factors and thereby indirectly regulate gene expression. Associates with chromatin at the NF-kappa-B promoter region via association with DDX1. Essential for cytokine gene expression in T-cells (PubMed:15790681). The NF-kappa-B homodimeric RELA-RELA complex appears to be involved in invasin-mediated activation of IL-8 expression.8 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, DNA-binding
Biological processHost-virus interaction, Transcription, Transcription regulation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-1169091 Activation of NF-kappaB in B cells
R-HSA-1810476 RIP-mediated NFkB activation via ZBP1
R-HSA-193692 Regulated proteolysis of p75NTR
R-HSA-202424 Downstream TCR signaling
R-HSA-209560 NF-kB is activated and signals survival
R-HSA-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-3134963 DEx/H-box helicases activate type I IFN and inflammatory cytokines production
R-HSA-3214841 PKMTs methylate histone lysines
R-HSA-381340 Transcriptional regulation of white adipocyte differentiation
R-HSA-445989 TAK1 activates NFkB by phosphorylation and activation of IKKs complex
R-HSA-448706 Interleukin-1 processing
R-HSA-4755510 SUMOylation of immune response proteins
R-HSA-5603029 IkBA variant leads to EDA-ID
R-HSA-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-HSA-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5621575 CD209 (DC-SIGN) signaling
R-HSA-5660668 CLEC7A/inflammasome pathway
R-HSA-844456 The NLRP3 inflammasome
R-HSA-9020702 Interleukin-1 signaling
R-HSA-933542 TRAF6 mediated NF-kB activation

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
Q04206

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
Q04206

SIGNOR Signaling Network Open Resource

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SIGNORi
Q04206

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Transcription factor p65
Alternative name(s):
Nuclear factor NF-kappa-B p65 subunit
Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:RELA
Synonyms:NFKB3
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:9955 RELA

Online Mendelian Inheritance in Man (OMIM)

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MIMi
164014 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q04206

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

A chromosomal aberration involving C11orf95 is found in more than two-thirds of supratentorial ependymomas. Translocation with C11orf95 produces a C11orf95-RELA fusion protein. C11orf95-RELA translocations are potent oncogenes that probably transform neural stem cells by driving an aberrant NF-kappa-B transcription program (PubMed:24553141).1 Publication
Mucocutaneous ulceration, chronic (CMCU)1 Publication
The disease may be caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant, mucocutaneous disease characterized by chronic mucosal lesions, in absence of recurrent infections.
Related information in OMIM

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi254T → A: Abolishes interaction with PIN1. 1 Publication1
Mutagenesisi276S → C: Loss of phosphorylation. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

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DisGeNETi
5970

MalaCards human disease database

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MalaCardsi
RELA
MIMi618287 phenotype

Open Targets

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OpenTargetsi
ENSG00000173039

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
251636 Ependymoma
530792 RELA fusion-positive ependymoma

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA296

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
Q04206

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL5533

Drug and drug target database

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DrugBanki
DB08908 Dimethyl fumarate
DB14059 SC-236

DrugCentral

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DrugCentrali
Q04206

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
RELA

Domain mapping of disease mutations (DMDM)

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DMDMi
62906901

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002051691 – 551Transcription factor p65Add BLAST551

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki37Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3)1 Publication
Modified residuei38Cysteine persulfide; alternateBy similarity1
Modified residuei38S-nitrosocysteine; alternateBy similarity1
Modified residuei122N6-acetyllysine; by PCAF and EP300; alternate1 Publication1
Cross-linki122Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3); alternate
Modified residuei123N6-acetyllysine; by PCAF and EP300; alternate1 Publication1
Cross-linki123Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3); alternate
Modified residuei218N6-acetyllysine1 Publication1
Modified residuei221N6-acetyllysine1 Publication1
Modified residuei254Phosphothreonine1 Publication1
Modified residuei276Phosphoserine; by RPS6KA4 and RPS6KA51 Publication1
Modified residuei281Phosphoserine1 Publication1
Modified residuei310N6-acetyllysine; alternateCombined sources4 Publications1
Modified residuei310N6-methyllysine; by SETD6; alternateBy similarity1
Modified residuei311Phosphoserine; by PKC/PRKCZBy similarity1
Modified residuei435Phosphothreonine1 Publication1
Modified residuei468Phosphoserine; by IKKB and IKKE2 Publications1
Modified residuei505Phosphothreonine; by CHEK11 Publication1
Modified residuei529Phosphoserine; by CK21 Publication1
Modified residuei536Phosphoserine; by IKKB2 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Ubiquitinated by RNF182, leading to its proteasomal degradation. Degradation is required for termination of NF-kappa-B response.2 Publications
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 (By similarity).By similarity
Phosphorylation at Ser-311 disrupts the interaction with EHMT1 and promotes transcription factor activity (By similarity). Phosphorylation on Ser-536 stimulates acetylation on Lys-310 and interaction with CBP; the phosphorylated and acetylated forms show enhanced transcriptional activity. Phosphorylation at Ser-276 by RPS6KA4 and RPS6KA5 promotes its transactivation and transcriptional activities.By similarity14 Publications
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 SIRT2.5 Publications
S-nitrosylation of Cys-38 inactivates the enzyme activity.By similarity
Sulfhydration at Cys-38 mediates the anti-apoptotic activity by promoting the interaction with RPS3 and activating the transcription factor activity.By similarity
Sumoylation by PIAS3 negatively regulates DNA-bound activated NF-kappa-B.1 Publication
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 (PubMed:18212740).1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q04206

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q04206

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q04206

MaxQB - The MaxQuant DataBase

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MaxQBi
Q04206

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q04206

PeptideAtlas

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PeptideAtlasi
Q04206

PRoteomics IDEntifications database

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PRIDEi
Q04206

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
58236 [Q04206-1]
58237 [Q04206-2]
58238 [Q04206-3]
58239 [Q04206-4]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q04206

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q04206

SwissPalm database of S-palmitoylation events

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SwissPalmi
Q04206

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000173039 Expressed in 227 organ(s), highest expression level in tibial artery

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q04206 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q04206 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB004264
CAB005030
HPA063461

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the NF-kappa-B p65-p50 complex.

Component of the NF-kappa-B p65-c-Rel complex. Homodimer; component of the NF-kappa-B p65-p65 complex.

Component of the NF-kappa-B p65-p52 complex. May interact with ETHE1. Binds TLE5 and TLE1.

Interacts with TP53BP2. Binds to and is phosphorylated by the activated form of either RPS6KA4 or RPS6KA5.

Interacts with ING4 and this interaction may be indirect.

Interacts with CARM1, USP48 and UNC5CL.

Interacts with IRAK1BP1 (By similarity).

Interacts with NFKBID (By similarity).

Interacts with NFKBIA (PubMed:1493333).

Interacts with GSK3B.

Interacts with NFKBIB (By similarity).

Interacts with NFKBIE.

Interacts with NFKBIZ.

Interacts with EHMT1 (via ANK repeats) (By similarity).

Part of a 70-90 kDa complex at least consisting of CHUK, IKBKB, NFKBIA, RELA, ELP1 and MAP3K14.

Interacts with HDAC3; HDAC3 mediates the deacetylation of RELA.

Interacts with HDAC1; the interaction requires non-phosphorylated RELA.

Interacts with CBP; the interaction requires phosphorylated RELA.

Interacts (phosphorylated at 'Thr-254') with PIN1; the interaction inhibits p65 binding to NFKBIA.

Interacts with SOCS1.

Interacts with UXT.

Interacts with MTDH and PHF11.

Interacts with ARRB2.

Interacts with NFKBIA (when phosphorylated), the interaction is direct; phosphorylated NFKBIA is part of a SCF(BTRC)-like complex lacking CUL1.

Interacts with RNF25.

Interacts (via C-terminus) with DDX1.

Interacts with UFL1 and COMMD1.

Interacts with BRMS1; this promotes deacetylation of 'Lys-310'.

Interacts with NOTCH2 (By similarity). Directly interacts with MEN1; this interaction represses NFKB-mediated transactivation.

Interacts with AKIP1, which promotes the phosphorylation and nuclear retention of RELA.

Interacts (via the RHD) with GFI1; the interaction, after bacterial lipopolysaccharide (LPS) stimulation, inhibits the transcriptional activity by interfering with the DNA-binding activity to target gene promoter DNA.

Interacts (when acetylated at Lys-310) with BRD4; leading to activation of the NF-kappa-B pathway.

Interacts with MEFV.

Interacts with CLOCK (By similarity).

Interacts (via N-terminus) with CPEN1; this interaction induces proteolytic cleavage of p65/RELA subunit and inhibition of NF-kappa-B transcriptional activity (PubMed:18212740).

Interacts with FOXP3.

Interacts with CDK5RAP3; stimulates the interaction of RELA with HDAC1, HDAC2 and HDAC3 thereby inhibiting NF-kappa-B transcriptional activity (PubMed:17785205).

Interacts with DHX9; this interaction is direct and activates NF-kappa-B-mediated transcription (PubMed:15355351).

Interacts with LRRC25 (PubMed:29044191).

Interacts with TBX21 (By similarity).

Interacts with KAT2A (By similarity).

Interacts with ZBTB7A; involved in the control by RELA of the accessibility of target gene promoters (PubMed:29813070).

By similarity7 Publications

(Microbial infection) Interacts with human respiratory syncytial virus (HRSV) protein M2-1.

1 Publication

(Microbial infection) Interacts with molluscum contagiosum virus MC132.

1 Publication

(Microbial infection) Interacts with herpes virus 8 virus protein LANA1.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-73886,EBI-73886
AATFQ9NY613EBI-73886,EBI-372428
ATF3P18847-35EBI-73886,EBI-9844134
BRD4O608858EBI-73886,EBI-723869
Brd4Q9ESU66EBI-73886,EBI-6260864From Mus musculus.
CDK5RAP3Q96JB54EBI-73886,EBI-718818
CHUKO151112EBI-73886,EBI-81249
COMMD1Q8N6687EBI-73886,EBI-1550112
CREBBPQ927936EBI-73886,EBI-81215
CRIP2P529432EBI-73886,EBI-947590
CTNNB1P352223EBI-73886,EBI-491549
DAXXQ9UER75EBI-73886,EBI-77321
DHX9Q082114EBI-73886,EBI-352022
EHMT1Q9H9B13EBI-73886,EBI-766087
ESR1P033729EBI-73886,EBI-78473
GAMMAHV.ORF73O419743EBI-73886,EBI-6933128From Murid herpesvirus 4.
GFI1Q996842EBI-73886,EBI-949368
HDAC1Q135476EBI-73886,EBI-301834
IER3P466956EBI-73886,EBI-1748945
IKBKBO149202EBI-73886,EBI-81266
IRF5Q135684EBI-73886,EBI-3931258
KDM2AQ9Y2K72EBI-73886,EBI-765758
KEAP1Q141454EBI-73886,EBI-751001
KLF6Q996126EBI-73886,EBI-714994
LMO2P257913EBI-73886,EBI-739696
MACROD1Q9BQ697EBI-73886,EBI-5324932
MAPK10P537792EBI-73886,EBI-713543
MEN1O00255-24EBI-73886,EBI-9869387
MyocdQ8VIM5-12EBI-73886,EBI-15626132From a different organism.
NFKB1P1983812EBI-73886,EBI-300010
NFKBIAP2596324EBI-73886,EBI-307386
NFKBIBQ156536EBI-73886,EBI-352889
NR4A1P22736-13EBI-73886,EBI-16085263
NSD1Q96L732EBI-73886,EBI-2862434
OGTO152942EBI-73886,EBI-539828
P/VP0C7743EBI-73886,EBI-3650423From Measles virus (strain Ichinose-B95a).
PDCD4Q53EL66EBI-73886,EBI-935824
PIAS4Q8N2W92EBI-73886,EBI-473160
PPP2CAP677756EBI-73886,EBI-712311
PPP2R1AP301532EBI-73886,EBI-302388
RELQ048643EBI-10223388,EBI-307352
RELBQ012012EBI-73886,EBI-357837
RPS3P233968EBI-73886,EBI-351193
RPS6KA5O755822EBI-73886,EBI-73869
SETD7Q8WTS612EBI-73886,EBI-1268586
SIRT1Q96EB65EBI-73886,EBI-1802965
SIRT2Q8IXJ62EBI-73886,EBI-477232
SIRT6Q8N6T74EBI-73886,EBI-712415
SNAI1O958635EBI-73886,EBI-1045459
SOCS1O155242EBI-73886,EBI-968198
STAT3P407634EBI-73886,EBI-518675
TCF4P158843EBI-10223388,EBI-533224
TGM2P219803EBI-73886,EBI-727668
TP53BP2Q136254EBI-73886,EBI-77642
TP53BP2Q13625-26EBI-73886,EBI-287091
UBCP0CG486EBI-73886,EBI-3390054
UL42P102266EBI-73886,EBI-1029310From Human herpesvirus 1 (strain 17).
UXTQ9UBK95EBI-73886,EBI-357355
yerAP314912EBI-73886,EBI-2840013From Yersinia pestis.
YPO2940A0A384KL232EBI-73886,EBI-20592225From Yersinia pestis.
YPO3877A0A384L2L72EBI-73886,EBI-20592206From Yersinia pestis.
yscLP699762EBI-73886,EBI-2846298From Yersinia pestis.

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
111902, 332 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q04206

Database of interacting proteins

More...
DIPi
DIP-24238N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
Q04206

Protein interaction database and analysis system

More...
IntActi
Q04206, 159 interactors

Molecular INTeraction database

More...
MINTi
Q04206

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000384273

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q04206

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1551
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q04206

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q04206

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini19 – 306RHDPROSITE-ProRule annotationAdd BLAST288

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni342 – 389Transcriptional activation domain 3By similarityAdd BLAST48
Regioni415 – 476Transcriptional activation domain 11 PublicationAdd BLAST62
Regioni520 – 551Transcriptional activation domain 2By similarityAdd BLAST32

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi301 – 304Nuclear localization signalSequence analysis4
Motifi536 – 5449aaTADSequence analysis9

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The transcriptional activation domain 3/TA3 does not participate to the direct transcriptional activity of RELA but is involved in the control by RELA of the accessibility of target gene promoters. Mediates interaction with ZBTB7A.By similarity
The transcriptional activation domain 1/TA1 and the transcriptional activation domain 2/TA2 have direct transcriptional activation properties (By similarity). The 9aaTAD motif found within the transcriptional activation domain 2 is a conserved motif present in a large number of transcription factors that is required for their transcriptional transactivation activity (PubMed:17467953).By similarity1 Publication

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IG8F Eukaryota
ENOG410XT64 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000159867

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000230474

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q04206

KEGG Orthology (KO)

More...
KOi
K04735

Identification of Orthologs from Complete Genome Data

More...
OMAi
PTAEPML

Database of Orthologous Groups

More...
OrthoDBi
916931at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q04206

TreeFam database of animal gene trees

More...
TreeFami
TF325632

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01177 IPT_NFkappaB, 1 hit

Database of protein disorder

More...
DisProti
DP00085

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.10, 1 hit
2.60.40.340, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013783 Ig-like_fold
IPR014756 Ig_E-set
IPR002909 IPT_dom
IPR033926 IPT_NFkappaB
IPR000451 NFkB/Dor
IPR008967 p53-like_TF_DNA-bd
IPR030495 RelA
IPR030492 RHD_CS
IPR032397 RHD_dimer
IPR011539 RHD_DNA_bind_dom
IPR037059 RHD_DNA_bind_dom_sf

The PANTHER Classification System

More...
PANTHERi
PTHR24169 PTHR24169, 1 hit
PTHR24169:SF1 PTHR24169:SF1, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF16179 RHD_dimer, 1 hit
PF00554 RHD_DNA_bind, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00057 NFKBTNSCPFCT

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00429 IPT, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49417 SSF49417, 1 hit
SSF81296 SSF81296, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01204 REL_1, 1 hit
PS50254 REL_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 4 described isoforms and 17 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q04206-1) [UniParc]FASTAAdd to basket
Also known as: p65

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MDELFPLIFP AEPAQASGPY VEIIEQPKQR GMRFRYKCEG RSAGSIPGER
60 70 80 90 100
STDTTKTHPT IKINGYTGPG TVRISLVTKD PPHRPHPHEL VGKDCRDGFY
110 120 130 140 150
EAELCPDRCI HSFQNLGIQC VKKRDLEQAI SQRIQTNNNP FQVPIEEQRG
160 170 180 190 200
DYDLNAVRLC FQVTVRDPSG RPLRLPPVLS HPIFDNRAPN TAELKICRVN
210 220 230 240 250
RNSGSCLGGD EIFLLCDKVQ KEDIEVYFTG PGWEARGSFS QADVHRQVAI
260 270 280 290 300
VFRTPPYADP SLQAPVRVSM QLRRPSDREL SEPMEFQYLP DTDDRHRIEE
310 320 330 340 350
KRKRTYETFK SIMKKSPFSG PTDPRPPPRR IAVPSRSSAS VPKPAPQPYP
360 370 380 390 400
FTSSLSTINY DEFPTMVFPS GQISQASALA PAPPQVLPQA PAPAPAPAMV
410 420 430 440 450
SALAQAPAPV PVLAPGPPQA VAPPAPKPTQ AGEGTLSEAL LQLQFDDEDL
460 470 480 490 500
GALLGNSTDP AVFTDLASVD NSEFQQLLNQ GIPVAPHTTE PMLMEYPEAI
510 520 530 540 550
TRLVTGAQRP PDPAPAPLGA PGLPNGLLSG DEDFSSIADM DFSALLSQIS

S
Length:551
Mass (Da):60,219
Last modified:April 26, 2005 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8147A6AF9F2445C6
GO
Isoform 2 (identifier: Q04206-2) [UniParc]FASTAAdd to basket
Also known as: p65 delta 2

The sequence of this isoform differs from the canonical sequence as follows:
     13-25: Missing.
     506-506: Missing.

Show »
Length:537
Mass (Da):58,807
Checksum:iA1F26DF2F53E662E
GO
Isoform 3 (identifier: Q04206-3) [UniParc]FASTAAdd to basket
Also known as: p65 delta

The sequence of this isoform differs from the canonical sequence as follows:
     222-231: Missing.

Show »
Length:541
Mass (Da):59,068
Checksum:i49F0493E19798AD1
GO
Isoform 4 (identifier: Q04206-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     143-145: Missing.

Note: No experimental confirmation available.
Show »
Length:548
Mass (Da):59,910
Checksum:iED40EF8B91F0A19A
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 17 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087X0W8A0A087X0W8_HUMAN
Transcription factor p65
RELA
448Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q2TAM5Q2TAM5_HUMAN
RELA protein
RELA
377Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PKH5E9PKH5_HUMAN
Transcription factor p65
RELA
418Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PI38E9PI38_HUMAN
Transcription factor p65
RELA
185Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PM47E9PM47_HUMAN
Transcription factor p65
RELA
64Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PMD5E9PMD5_HUMAN
Transcription factor p65
RELA
161Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PN69E9PN69_HUMAN
Transcription factor p65
RELA
134Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PNK5E9PNK5_HUMAN
Transcription factor p65
RELA
85Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PNV4E9PNV4_HUMAN
Transcription factor p65
RELA
153Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PRX2E9PRX2_HUMAN
Transcription factor p65
RELA
95Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
There are more potential isoformsShow all

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti49E → R in CAA80524 (PubMed:8281153).Curated1
Sequence conflicti180S → P in AAA36408 (PubMed:2006423).Curated1
Sequence conflicti372 – 380QISQASALA → RSARPRLG in CAA80524 (PubMed:8281153).Curated9

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_081858246 – 549Missing Found in a patient diagnosed with autoimmune lymphoproliferative syndrome; unknown pathological significance. 1 PublicationAdd BLAST304

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_00558713 – 25Missing in isoform 2. 1 PublicationAdd BLAST13
Alternative sequenceiVSP_031245143 – 145Missing in isoform 4. 1 Publication3
Alternative sequenceiVSP_012031222 – 231Missing in isoform 3. 1 Publication10
Alternative sequenceiVSP_005588506Missing in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M62399 mRNA Translation: AAA36408.1
Z22948
, Z22949, Z22953, Z22950, Z22951 Genomic DNA Translation: CAA80524.2
L19067 mRNA Translation: AAA20946.1
BC033522 mRNA Translation: AAH33522.1
AY455868 Genomic DNA Translation: AAR13863.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS31609.1 [Q04206-1]
CCDS44651.1 [Q04206-4]

Protein sequence database of the Protein Information Resource

More...
PIRi
A40851
I53719
S51782 A42017

NCBI Reference Sequences

More...
RefSeqi
NP_001138610.1, NM_001145138.1 [Q04206-4]
NP_001230913.1, NM_001243984.1
NP_068810.3, NM_021975.3 [Q04206-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000308639; ENSP00000311508; ENSG00000173039 [Q04206-4]
ENST00000406246; ENSP00000384273; ENSG00000173039 [Q04206-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5970

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5970

UCSC genome browser

More...
UCSCi
uc001ofg.4 human [Q04206-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62399 mRNA Translation: AAA36408.1
Z22948
, Z22949, Z22953, Z22950, Z22951 Genomic DNA Translation: CAA80524.2
L19067 mRNA Translation: AAA20946.1
BC033522 mRNA Translation: AAH33522.1
AY455868 Genomic DNA Translation: AAR13863.1
CCDSiCCDS31609.1 [Q04206-1]
CCDS44651.1 [Q04206-4]
PIRiA40851
I53719
S51782 A42017
RefSeqiNP_001138610.1, NM_001145138.1 [Q04206-4]
NP_001230913.1, NM_001243984.1
NP_068810.3, NM_021975.3 [Q04206-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NFIX-ray2.70A/C20-320[»]
2LSPNMR-A304-316[»]
2O61X-ray2.80A20-291[»]
3GUTX-ray3.59A/C/E/G20-291[»]
3QXYX-ray2.09P/Q302-316[»]
3RC0X-ray2.19P/Q302-316[»]
4KV1X-ray1.50C/D308-314[»]
4KV4X-ray2.00B308-314[»]
5U4KNMR-B521-551[»]
5URNNMR-B521-551[»]
SMRiQ04206
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi111902, 332 interactors
CORUMiQ04206
DIPiDIP-24238N
ELMiQ04206
IntActiQ04206, 159 interactors
MINTiQ04206
STRINGi9606.ENSP00000384273

Chemistry databases

BindingDBiQ04206
ChEMBLiCHEMBL5533
DrugBankiDB08908 Dimethyl fumarate
DB14059 SC-236
DrugCentraliQ04206

PTM databases

iPTMnetiQ04206
PhosphoSitePlusiQ04206
SwissPalmiQ04206

Polymorphism and mutation databases

BioMutaiRELA
DMDMi62906901

Proteomic databases

EPDiQ04206
jPOSTiQ04206
MassIVEiQ04206
MaxQBiQ04206
PaxDbiQ04206
PeptideAtlasiQ04206
PRIDEiQ04206
ProteomicsDBi58236 [Q04206-1]
58237 [Q04206-2]
58238 [Q04206-3]
58239 [Q04206-4]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
5970

Genome annotation databases

EnsembliENST00000308639; ENSP00000311508; ENSG00000173039 [Q04206-4]
ENST00000406246; ENSP00000384273; ENSG00000173039 [Q04206-1]
GeneIDi5970
KEGGihsa:5970
UCSCiuc001ofg.4 human [Q04206-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5970
DisGeNETi5970

GeneCards: human genes, protein and diseases

More...
GeneCardsi
RELA
HGNCiHGNC:9955 RELA
HPAiCAB004264
CAB005030
HPA063461
MalaCardsiRELA
MIMi164014 gene
618287 phenotype
neXtProtiNX_Q04206
OpenTargetsiENSG00000173039
Orphaneti251636 Ependymoma
530792 RELA fusion-positive ependymoma
PharmGKBiPA296

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IG8F Eukaryota
ENOG410XT64 LUCA
GeneTreeiENSGT00940000159867
HOGENOMiHOG000230474
InParanoidiQ04206
KOiK04735
OMAiPTAEPML
OrthoDBi916931at2759
PhylomeDBiQ04206
TreeFamiTF325632

Enzyme and pathway databases

ReactomeiR-HSA-1169091 Activation of NF-kappaB in B cells
R-HSA-1810476 RIP-mediated NFkB activation via ZBP1
R-HSA-193692 Regulated proteolysis of p75NTR
R-HSA-202424 Downstream TCR signaling
R-HSA-209560 NF-kB is activated and signals survival
R-HSA-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-3134963 DEx/H-box helicases activate type I IFN and inflammatory cytokines production
R-HSA-3214841 PKMTs methylate histone lysines
R-HSA-381340 Transcriptional regulation of white adipocyte differentiation
R-HSA-445989 TAK1 activates NFkB by phosphorylation and activation of IKKs complex
R-HSA-448706 Interleukin-1 processing
R-HSA-4755510 SUMOylation of immune response proteins
R-HSA-5603029 IkBA variant leads to EDA-ID
R-HSA-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-HSA-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5621575 CD209 (DC-SIGN) signaling
R-HSA-5660668 CLEC7A/inflammasome pathway
R-HSA-844456 The NLRP3 inflammasome
R-HSA-9020702 Interleukin-1 signaling
R-HSA-933542 TRAF6 mediated NF-kB activation
SABIO-RKiQ04206
SignaLinkiQ04206
SIGNORiQ04206

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
RELA human
EvolutionaryTraceiQ04206

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
RELA

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
5970
PharosiQ04206

Protein Ontology

More...
PROi
PR:Q04206

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
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Gene expression databases

BgeeiENSG00000173039 Expressed in 227 organ(s), highest expression level in tibial artery
ExpressionAtlasiQ04206 baseline and differential
GenevisibleiQ04206 HS

Family and domain databases

CDDicd01177 IPT_NFkappaB, 1 hit
DisProtiDP00085
Gene3Di2.60.40.10, 1 hit
2.60.40.340, 1 hit
InterProiView protein in InterPro
IPR013783 Ig-like_fold
IPR014756 Ig_E-set
IPR002909 IPT_dom
IPR033926 IPT_NFkappaB
IPR000451 NFkB/Dor
IPR008967 p53-like_TF_DNA-bd
IPR030495 RelA
IPR030492 RHD_CS
IPR032397 RHD_dimer
IPR011539 RHD_DNA_bind_dom
IPR037059 RHD_DNA_bind_dom_sf
PANTHERiPTHR24169 PTHR24169, 1 hit
PTHR24169:SF1 PTHR24169:SF1, 1 hit
PfamiView protein in Pfam
PF16179 RHD_dimer, 1 hit
PF00554 RHD_DNA_bind, 1 hit
PRINTSiPR00057 NFKBTNSCPFCT
SMARTiView protein in SMART
SM00429 IPT, 1 hit
SUPFAMiSSF49417 SSF49417, 1 hit
SSF81296 SSF81296, 1 hit
PROSITEiView protein in PROSITE
PS01204 REL_1, 1 hit
PS50254 REL_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTF65_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q04206
Secondary accession number(s): Q6GTV1, Q6SLK1
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: April 26, 2005
Last modified: October 16, 2019
This is version 234 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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