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Entry version 209 (08 May 2019)
Sequence version 1 (01 Oct 1993)
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Protein

Transcription factor p65

Gene

Rela

Organism
Mus musculus (Mouse)
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 (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).By similarity3 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 processTranscription, Transcription regulation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-MMU-1169091 Activation of NF-kappaB in B cells
R-MMU-1810476 RIP-mediated NFkB activation via ZBP1
R-MMU-193692 Regulated proteolysis of p75NTR
R-MMU-202424 Downstream TCR signaling
R-MMU-209560 NF-kB is activated and signals survival
R-MMU-2871837 FCERI mediated NF-kB activation
R-MMU-3134963 DEx/H-box helicases activate type I IFN and inflammatory cytokines production
R-MMU-3214841 PKMTs methylate histone lysines
R-MMU-445989 TAK1 activates NFkB by phosphorylation and activation of IKKs complex
R-MMU-448706 Interleukin-1 processing
R-MMU-4755510 SUMOylation of immune response proteins
R-MMU-5607764 CLEC7A (Dectin-1) signaling
R-MMU-5621575 CD209 (DC-SIGN) signaling
R-MMU-9020702 Interleukin-1 signaling
R-MMU-933542 TRAF6 mediated NF-kB activation

<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 19

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

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MGIi
MGI:103290 Rela

<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

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>Mutagenesisi38C → S: Abolishes sulfhydration and impairs interaction with RPS3. 1 Publication1
Mutagenesisi281S → A or E: Abolishes DNA-binding and transcriptional activity. 1 Publication1
Mutagenesisi310K → R: Abolishes monomethylation by SETD6 and interaction with EHMT1. 1 Publication1
Mutagenesisi361 – 370DEFSPMLLPS → AAAAAAAAAA: Loss of interaction with ZBTB7A. 1 Publication10

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL5902

<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_00002051701 – 549Transcription factor p65Add BLAST549

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-acetylmethionineBy similarity1
<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)By similarity
Modified residuei38Cysteine persulfide; alternate1 Publication1
Modified residuei38S-nitrosocysteine; alternate1 Publication1
Modified residuei122N6-acetyllysine; by PCAF and EP300; alternateBy similarity1
Cross-linki122Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3); alternateBy similarity
Modified residuei123N6-acetyllysine; by PCAF and EP300; alternateBy similarity1
Cross-linki123Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3); alternateBy similarity
Modified residuei176PhosphothreonineCombined sources1
Modified residuei218N6-acetyllysineBy similarity1
Modified residuei221N6-acetyllysineBy similarity1
Modified residuei254PhosphothreonineBy similarity1
Modified residuei276Phosphoserine; by RPS6KA4 and RPS6KA5By similarity1
Modified residuei281PhosphoserineBy similarity1
Modified residuei310N6-acetyllysine; alternateCombined sources1
Modified residuei310N6-methyllysine; by SETD6; alternate1 Publication1
Modified residuei311Phosphoserine; by PKC/PRKCZ2 Publications1
Modified residuei433PhosphothreonineBy similarity1
Modified residuei467Phosphoserine; by IKKB and IKKEBy similarity1
Modified residuei504Phosphothreonine; by CHEK1By similarity1
Modified residuei527Phosphoserine; by CK2By similarity1
Modified residuei534Phosphoserine; by IKKBBy similarity1

<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, leading to its proteasomal degradation. Degradation is required for termination of NF-kappa-B response (By similarity).By similarity
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.2 Publications
Phosphorylation on Ser-534 stimulates acetylation on Lys-310 and interaction with CBP; the phosphorylated and acetylated forms show enhanced transcriptional activity (By similarity). Phosphorylation at Ser-311 disrupts the interaction with EHMT1 and promotes transcription factor activity. Phosphorylation at Ser-276 by RPS6KA4 and RPS6KA5 promotes its transactivation and transcriptional activities.By similarity2 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 (By similarity).By similarity
S-nitrosylation of Cys-38 inactivates the enzyme activity.1 Publication
Sulfhydration at Cys-38 mediates the anti-apoptotic activity by promoting the interaction with RPS3 and activating the transcription factor activity.
Sumoylation by PIAS3 negatively regulates DNA-bound activated NF-kappa-B.By similarity
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.By similarity

Keywords - PTMi

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

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q04207

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

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PaxDbi
Q04207

PeptideAtlas

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PeptideAtlasi
Q04207

PRoteomics IDEntifications database

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PRIDEi
Q04207

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q04207

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

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PhosphoSitePlusi
Q04207

<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
ENSMUSG00000024927 Expressed in 318 organ(s), highest expression level in right lung

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q04207 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q04207 MM

<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. Interacts with NFKBIA. Interacts with GSK3B. Interacts with NFKBIB. Interacts with NFKBIE. Interacts with NFKBIZ. 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 MTDH and PHF11. Interacts with NFKBID. Interacts with ARRB2. Interacts with NFKBIA (when phosphorylated), the interaction is direct; phosphorylated NFKBIA is associated with a SCF(BTRC)-like complex lacking CUL1. Interacts with RNF25. Interacts (via C-terminus) with DDX1 (By similarity). Interacts with UFL1 and COMMD1 (By similarity). Interacts with BRMS1; this promotes deacetylation of 'Lys-310'. Interacts (when acetylated at Lys-310) with BRD4; leading to activation of the NF-kappa-B pathway (By similarity). Interacts with EHMT1 (via ANK repeats). Interacts with NOTCH2. Directly interacts with MEN1; this interaction represses NFKB-mediated transactivation (By similarity). Interacts with AKIP1, which promotes the phosphorylation and nuclear retention of RELA (By similarity). 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 with MEFV (By similarity). Interacts with CLOCK. Interacts with FOXP3 (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 (By similarity). Interacts with CDK5RAP3; stimulates the interaction of RELA with HDAC1, HDAC2 and HDAC3 thereby inhibiting NF-kappa-B transcriptional activity (By similarity). Interacts with DHX9; this interaction is direct and activates NF-kappa-B-mediated transcription (By similarity). Interacts with TBX21 (PubMed:23616576). Interacts with LRRC25 (By similarity). Interacts with KAT2A (PubMed:25024434). Interacts (via transcriptional activation domain 3) with ZBTB7A; involved in the control by RELA of the accessibility of target gene promoters (PubMed:29813070).By similarity12 Publications

<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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
202853, 31 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q04207

Database of interacting proteins

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DIPi
DIP-6219N

Protein interaction database and analysis system

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IntActi
Q04207, 28 interactors

Molecular INTeraction database

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MINTi
Q04207

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000025867

<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

1549
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Database of protein disorder

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DisProti
DP00129

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

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SMRi
Q04207

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q04207

<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 – 390Transcriptional activation domain 31 PublicationAdd BLAST49
Regioni413 – 475Transcriptional activation domain 11 PublicationAdd BLAST63
Regioni519 – 549Transcriptional activation domain 21 PublicationAdd BLAST31

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
Motifi534 – 5429aaTADSequence 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.1 Publication
The transcriptional activation domain 1/TA1 and the transcriptional activation domain 2/TA2 have direct transcriptional activation properties (PubMed:29813070). 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 (By similarity).By similarity1 Publication

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IG8F Eukaryota
ENOG410XT64 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000159867

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000230474

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q04207

KEGG Orthology (KO)

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KOi
K04735

Identification of Orthologs from Complete Genome Data

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OMAi
EFSPMVF

Database of Orthologous Groups

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OrthoDBi
916931at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q04207

TreeFam database of animal gene trees

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TreeFami
TF325632

Family and domain databases

Conserved Domains Database

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CDDi
cd01177 IPT_NFkappaB, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.40.10, 1 hit
2.60.40.340, 1 hit

Integrated resource of protein families, domains and functional sites

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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

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PANTHERi
PTHR24169 PTHR24169, 1 hit
PTHR24169:SF1 PTHR24169:SF1, 1 hit

Pfam protein domain database

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

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00057 NFKBTNSCPFCT

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00429 IPT, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF49417 SSF49417, 1 hit
SSF81296 SSF81296, 1 hit

PROSITE; a protein domain and family database

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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 (2+)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 2 <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 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform p65 (identifier: Q04207-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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MDDLFPLIFP SEPAQASGPY VEIIEQPKQR GMRFRYKCEG RSAGSIPGER
60 70 80 90 100
STDTTKTHPT IKINGYTGPG TVRISLVTKD PPHRPHPHEL VGKDCRDGYY
110 120 130 140 150
EADLCPDRSI HSFQNLGIQC VKKRDLEQAI SQRIQTNNNP FHVPIEEQRG
160 170 180 190 200
DYDLNAVRLC FQVTVRDPAG RPLLLTPVLS 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 SIMKKSPFNG PTEPRPPTRR IAVPTRNSTS VPKPAPQPYT
360 370 380 390 400
FPASLSTINF DEFSPMLLPS GQISNQALAL APSSAPVLAQ TMVPSSAMVP
410 420 430 440 450
LAQPPAPAPV LTPGPPQSLS APVPKSTQAG EGTLSEALLH LQFDADEDLG
460 470 480 490 500
ALLGNSTDPG VFTDLASVDN SEFQQLLNQG VSMSHSTAEP MLMEYPEAIT
510 520 530 540
RLVTGSQRPP DPAPTPLGTS GLPNGLSGDE DFSSIADMDF SALLSQISS
Length:549
Mass (Da):60,212
Last modified:October 1, 1993 - v1
<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:iBDF1673D2FE398B9
GO
Isoform p65 delta (identifier: Q04207-2) [UniParc]FASTAAdd to basket

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

Show »
Length:539
Mass (Da):59,061
Checksum:iF834FD0302D351BD
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 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q4U113Q4U113_MOUSE
NF-kB RelA splice variant 1
Rela
121Annotation 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>
A0A494BA44A0A494BA44_MOUSE
Transcription factor p65
Rela
348Annotation score:

Annotation score:1 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>
A0A494B901A0A494B901_MOUSE
Transcription factor p65
Rela
67Annotation score:

Annotation score:1 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 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 conflicti28K → N in AAB00795 (PubMed:8918242).Curated1
Sequence conflicti61I → IQKD in AAB00795 (PubMed:8918242).Curated1

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_005589222 – 231Missing in isoform p65 delta. Curated10

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M61909 mRNA Translation: AAA39811.1
BC003818 mRNA Translation: AAH03818.1
L77155 Genomic DNA Translation: AAB00795.1
Z22952 Genomic DNA Translation: CAA80528.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS29473.1 [Q04207-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A37932
PC4233
S48113

NCBI Reference Sequences

More...
RefSeqi
NP_033071.1, NM_009045.4 [Q04207-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000025867; ENSMUSP00000025867; ENSMUSG00000024927 [Q04207-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
19697

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:19697

UCSC genome browser

More...
UCSCi
uc008gee.1 mouse [Q04207-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61909 mRNA Translation: AAA39811.1
BC003818 mRNA Translation: AAH03818.1
L77155 Genomic DNA Translation: AAB00795.1
Z22952 Genomic DNA Translation: CAA80528.1
CCDSiCCDS29473.1 [Q04207-1]
PIRiA37932
PC4233
S48113
RefSeqiNP_033071.1, NM_009045.4 [Q04207-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BFTX-ray2.00A/B191-291[»]
1IKNX-ray2.30A19-304[»]
1K3ZX-ray2.50A/B191-326[»]
1LE5X-ray2.75A/E20-291[»]
1LE9X-ray3.00A/E20-291[»]
1LEIX-ray2.70A20-291[»]
1MY5X-ray1.80A/B191-304[»]
1MY7X-ray1.49A/B191-304[»]
1OY3X-ray2.05B/C191-326[»]
1RAMX-ray2.70A/B19-291[»]
1VKXX-ray2.90A20-291[»]
2I9TX-ray2.80A19-291[»]
2LWWNMR-B425-490[»]
2RAMX-ray2.40A/B19-291[»]
5U01X-ray2.50A/B/C/D19-291[»]
6GGRX-ray2.10A20-188[»]
DisProtiDP00129
SMRiQ04207
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202853, 31 interactors
CORUMiQ04207
DIPiDIP-6219N
IntActiQ04207, 28 interactors
MINTiQ04207
STRINGi10090.ENSMUSP00000025867

Chemistry databases

ChEMBLiCHEMBL5902

PTM databases

iPTMnetiQ04207
PhosphoSitePlusiQ04207

Proteomic databases

EPDiQ04207
PaxDbiQ04207
PeptideAtlasiQ04207
PRIDEiQ04207

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025867; ENSMUSP00000025867; ENSMUSG00000024927 [Q04207-1]
GeneIDi19697
KEGGimmu:19697
UCSCiuc008gee.1 mouse [Q04207-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5970
MGIiMGI:103290 Rela

Phylogenomic databases

eggNOGiENOG410IG8F Eukaryota
ENOG410XT64 LUCA
GeneTreeiENSGT00940000159867
HOGENOMiHOG000230474
InParanoidiQ04207
KOiK04735
OMAiEFSPMVF
OrthoDBi916931at2759
PhylomeDBiQ04207
TreeFamiTF325632

Enzyme and pathway databases

ReactomeiR-MMU-1169091 Activation of NF-kappaB in B cells
R-MMU-1810476 RIP-mediated NFkB activation via ZBP1
R-MMU-193692 Regulated proteolysis of p75NTR
R-MMU-202424 Downstream TCR signaling
R-MMU-209560 NF-kB is activated and signals survival
R-MMU-2871837 FCERI mediated NF-kB activation
R-MMU-3134963 DEx/H-box helicases activate type I IFN and inflammatory cytokines production
R-MMU-3214841 PKMTs methylate histone lysines
R-MMU-445989 TAK1 activates NFkB by phosphorylation and activation of IKKs complex
R-MMU-448706 Interleukin-1 processing
R-MMU-4755510 SUMOylation of immune response proteins
R-MMU-5607764 CLEC7A (Dectin-1) signaling
R-MMU-5621575 CD209 (DC-SIGN) signaling
R-MMU-9020702 Interleukin-1 signaling
R-MMU-933542 TRAF6 mediated NF-kB activation

Miscellaneous databases

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

More...
ChiTaRSi
Rela mouse
EvolutionaryTraceiQ04207

Protein Ontology

More...
PROi
PR:Q04207

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000024927 Expressed in 318 organ(s), highest expression level in right lung
ExpressionAtlasiQ04207 baseline and differential
GenevisibleiQ04207 MM

Family and domain databases

CDDicd01177 IPT_NFkappaB, 1 hit
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

More...
ProtoNeti
Search...

<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_MOUSE
<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: Q04207
Secondary accession number(s): Q62025
<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: October 1, 1993
Last modified: May 8, 2019
This is version 209 of the entry and version 1 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

<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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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