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Protein

Nuclear factor NF-kappa-B p105 subunit

Gene

NFKB1

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 and the heterodimeric p65-p50 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. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappa-B p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3. NFKB1 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p105 and generation of p50 by a cotranslational processing. The proteasome-mediated process ensures the production of both p50 and p105 and preserves their independent function, although processing of NFKB1/p105 also appears to occur post-translationally. p50 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. In a complex with MAP3K8, NFKB1/p105 represses MAP3K8-induced MAPK signaling; active MAP3K8 is released by proteasome-dependent degradation of NFKB1/p105.1 Publication

<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 processApoptosis, 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-5603029 IkBA variant leads to EDA-ID
R-HSA-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5621575 CD209 (DC-SIGN) signaling
R-HSA-5660668 CLEC7A/inflammasome pathway
R-HSA-5684264 MAP3K8 (TPL2)-dependent MAPK1/3 activation
R-HSA-6798695 Neutrophil degranulation
R-HSA-844456 The NLRP3 inflammasome
R-HSA-9020702 Interleukin-1 signaling
R-HSA-933542 TRAF6 mediated NF-kB activation

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

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SignaLinki
P19838

SIGNOR Signaling Network Open Resource

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SIGNORi
P19838

<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:
Nuclear factor NF-kappa-B p105 subunit
Alternative name(s):
DNA-binding factor KBF1
EBP-1
Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1
Cleaved into the following chain:
<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:NFKB1
<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 4

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000109320.11

Human Gene Nomenclature Database

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HGNCi
HGNC:7794 NFKB1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
164011 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P19838

<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; 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

Immunodeficiency, common variable, 12 (CVID12)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen.
See also OMIM:616576

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>Mutagenesisi61C → S: Suppresses S-nitrosylation-induced inhibition of DNA-binding activity. Loss of S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine-induced inhibition of DNA-binding activity. 2 Publications1
Mutagenesisi678N → A: Fails to promote HIF1AN-dependent 2-oxoglutarate decarboxylation. 1 Publication1
Mutagenesisi903S → A: Prevents p105 proteolysis in response to TNF-alpha. 1 Publication1
Mutagenesisi907S → A: Prevents p105 proteolysis in response to TNF-alpha. 1 Publication1
Mutagenesisi921S → A: Decrease in stimuli-induced phosphorylation. Loss of phosphorylation; when associated with A-923 and A-932. 1 Publication1
Mutagenesisi923S → A: Decrease in stimuli-induced phosphorylation. Loss of phosphorylation; when associated with A-921 and A-932. 1 Publication1
Mutagenesisi932S → A: Decrease in stimuli-induced phosphorylation. Loss of phosphorylation; when associated with A-921 and A-923. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
4790

MalaCards human disease database

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MalaCardsi
NFKB1
MIMi616576 phenotype

Open Targets

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OpenTargetsi
ENSG00000109320

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

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Orphaneti
1572 Common variable immunodeficiency

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA248

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3251

Drug and drug target database

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DrugBanki
DB00945 Acetylsalicylic acid
DB05487 CC-8490
DB05212 HE3286
DB05767 HMPL-004
DB05464 NOX-700
DB05451 P54
DB01411 Pranlukast
DB05471 SGN-30
DB01041 Thalidomide
DB08814 Triflusal

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
NFKB1

Domain mapping of disease mutations (DMDM)

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DMDMi
21542418

<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_00000303101 – 968Nuclear factor NF-kappa-B p105 subunitAdd BLAST968
ChainiPRO_00000303111 – 433Nuclear factor NF-kappa-B p50 subunitAdd BLAST433

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 residuei61S-nitrosocysteine; alternate1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi61S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine; alternate1 Publication1
<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-linki325Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei337Phosphoserine; by PKASequence analysis1
Modified residuei431N6-acetyllysine; by EP3001 Publication1
Modified residuei440N6-acetyllysine; by EP3001 Publication1
Modified residuei441N6-acetyllysine; by EP3001 Publication1
Modified residuei449PhosphoserineBy similarity1
Modified residuei678(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication1
Modified residuei759PhosphoserineBy similarity1
Modified residuei892PhosphoserineCombined sources1
Modified residuei903Phosphoserine; by GSK3-beta; in vitroCombined sources1 Publication1
Modified residuei907Phosphoserine; by GSK3-beta; in vitroCombined sources1 Publication1
Modified residuei927Phosphoserine; by IKKB2 Publications1
Modified residuei932Phosphoserine; by IKKB1 Publication1
Modified residuei937PhosphoserineCombined sources1
Modified residuei943PhosphothreonineBy 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

While translation occurs, the particular unfolded structure after the GRR repeat promotes the generation of p50 making it an acceptable substrate for the proteasome. This process is known as cotranslational processing. The processed form is active and the unprocessed form acts as an inhibitor (I kappa B-like), being able to form cytosolic complexes with NF-kappa B, trapping it in the cytoplasm. Complete folding of the region downstream of the GRR repeat precludes processing.1 Publication
Phosphorylation at 'Ser-903' and 'Ser-907' primes p105 for proteolytic processing in response to TNF-alpha stimulation. Phosphorylation at 'Ser-927' and 'Ser-932' are required for BTRC/BTRCP-mediated proteolysis.4 Publications
Polyubiquitination seems to allow p105 processing.2 Publications
S-nitrosylation of Cys-61 affects DNA binding.2 Publications
The covalent modification of cysteine by 15-deoxy-Delta12,14-prostaglandin-J2 is autocatalytic and reversible. It may occur as an alternative to other cysteine modifications, such as S-nitrosylation and S-palmitoylation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei433 – 434Cleavage (when cotranslationally processed)2

Keywords - PTMi

Acetylation, Hydroxylation, Isopeptide bond, Lipoprotein, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P19838

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P19838

MaxQB - The MaxQuant DataBase

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MaxQBi
P19838

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

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PaxDbi
P19838

PeptideAtlas

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PeptideAtlasi
P19838

PRoteomics IDEntifications database

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PRIDEi
P19838

ProteomicsDB human proteome resource

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ProteomicsDBi
53694
53695 [P19838-2]
53696 [P19838-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P19838

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

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PhosphoSitePlusi
P19838

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
P19838

<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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By phorbol ester and TNF.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000109320 Expressed in 198 organ(s), highest expression level in leukocyte

CleanEx database of gene expression profiles

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CleanExi
HS_NFKB1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P19838 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P19838 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB004031
HPA027305

<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-p50 complex. Homodimer; component of the NF-kappa-B p50-p50 complex. Component of the NF-kappa-B p105-p50 complex. Component of the NF-kappa-B p50-c-Rel complex. Component of a complex consisting of the NF-kappa-B p50-p50 homodimer and BCL3. Also interacts with MAP3K8. NF-kappa-B p50 subunit interacts with NCOA3 coactivator, which may coactivate NF-kappa-B dependent expression via its histone acetyltransferase activity. Interacts with DSIPI; this interaction prevents nuclear translocation and DNA-binding. Interacts with SPAG9 and UNC5CL. NFKB1/p105 interacts with CFLAR; the interaction inhibits p105 processing into p50. NFKB1/p105 forms a ternary complex with MAP3K8 and TNIP2. Interacts with GSK3B; the interaction prevents processing of p105 to p50. NFKB1/p50 interacts with NFKBIE. NFKB1/p50 interacts with NFKBIZ. Nuclear factor NF-kappa-B p50 subunit interacts with NFKBID (By similarity). Directly interacts with MEN1. Interacts with HIF1AN.By similarity17 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
110857, 162 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P19838

Database of interacting proteins

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DIPi
DIP-106N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P19838

Protein interaction database and analysis system

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IntActi
P19838, 476 interactors

Molecular INTeraction database

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MINTi
P19838

STRING: functional protein association networks

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STRINGi
9606.ENSP00000226574

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P19838

<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

1968
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MDINMR-B55-67[»]
1MDJNMR-B55-67[»]
1MDKNMR-B55-67[»]
1NFIX-ray2.70B/D248-354[»]
1SVCX-ray2.60P2-365[»]
2DBFNMR-A806-893[»]
2O61X-ray2.80B40-352[»]
3GUTX-ray3.59B/D/F/H41-352[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P19838

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

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SMRi
P19838

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
P19838

<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>Domaini42 – 367RHDPROSITE-ProRule annotationAdd BLAST326
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati542 – 571ANK 1Add BLAST30
Repeati581 – 610ANK 2Add BLAST30
Repeati614 – 643ANK 3Add BLAST30
Repeati650 – 679ANK 4Add BLAST30
Repeati684 – 714ANK 5Add BLAST31
Repeati718 – 747ANK 6Add BLAST30
Repeati771 – 801ANK 7Add BLAST31
Domaini805 – 892DeathAdd BLAST88

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>Regioni372 – 394GRRAdd BLAST23
Regioni435 – 968Interaction with CFLAR1 PublicationAdd BLAST534
Regioni650 – 684Essential for interaction with HIF1AN1 PublicationAdd BLAST35

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>Motifi360 – 365Nuclear localization signalSequence analysis6

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi375 – 433Gly-richAdd BLAST59

<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 C-terminus of p105 might be involved in cytoplasmic retention, inhibition of DNA-binding, and transcription activation.
Glycine-rich region (GRR) appears to be a critical element in the generation of p50.

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0504 Eukaryota
COG0666 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000158625

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000004822

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG052613

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P19838

KEGG Orthology (KO)

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KOi
K02580

Identification of Orthologs from Complete Genome Data

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OMAi
MTWIPRK

Database of Orthologous Groups

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OrthoDBi
916931at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P19838

TreeFam database of animal gene trees

More...
TreeFami
TF325632

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00204 ANK, 1 hit
cd01177 IPT_NFkappaB, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.25.40.20, 1 hit
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
IPR002110 Ankyrin_rpt
IPR020683 Ankyrin_rpt-contain_dom
IPR036770 Ankyrin_rpt-contain_sf
IPR011029 DEATH-like_dom_sf
IPR000488 Death_domain
IPR013783 Ig-like_fold
IPR014756 Ig_E-set
IPR002909 IPT_dom
IPR033926 IPT_NFkappaB
IPR030503 NF-kB_p105
IPR000451 NFkB/Dor
IPR008967 p53-like_TF_DNA-bd
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:SF9 PTHR24169:SF9, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12796 Ank_2, 2 hits
PF00531 Death, 1 hit
PF16179 RHD_dimer, 1 hit
PF00554 RHD_DNA_bind, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01415 ANKYRIN
PR00057 NFKBTNSCPFCT

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00248 ANK, 6 hits
SM00005 DEATH, 1 hit
SM00429 IPT, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47986 SSF47986, 1 hit
SSF48403 SSF48403, 1 hit
SSF49417 SSF49417, 1 hit
SSF81296 SSF81296, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50297 ANK_REP_REGION, 1 hit
PS50088 ANK_REPEAT, 5 hits
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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 <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 3 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P19838-1) [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.

« Hide
        10         20         30         40         50
MAEDDPYLGR PEQMFHLDPS LTHTIFNPEV FQPQMALPTD GPYLQILEQP
60 70 80 90 100
KQRGFRFRYV CEGPSHGGLP GASSEKNKKS YPQVKICNYV GPAKVIVQLV
110 120 130 140 150
TNGKNIHLHA HSLVGKHCED GICTVTAGPK DMVVGFANLG ILHVTKKKVF
160 170 180 190 200
ETLEARMTEA CIRGYNPGLL VHPDLAYLQA EGGGDRQLGD REKELIRQAA
210 220 230 240 250
LQQTKEMDLS VVRLMFTAFL PDSTGSFTRR LEPVVSDAIY DSKAPNASNL
260 270 280 290 300
KIVRMDRTAG CVTGGEEIYL LCDKVQKDDI QIRFYEEEEN GGVWEGFGDF
310 320 330 340 350
SPTDVHRQFA IVFKTPKYKD INITKPASVF VQLRRKSDLE TSEPKPFLYY
360 370 380 390 400
PEIKDKEEVQ RKRQKLMPNF SDSFGGGSGA GAGGGGMFGS GGGGGGTGST
410 420 430 440 450
GPGYSFPHYG FPTYGGITFH PGTTKSNAGM KHGTMDTESK KDPEGCDKSD
460 470 480 490 500
DKNTVNLFGK VIETTEQDQE PSEATVGNGE VTLTYATGTK EESAGVQDNL
510 520 530 540 550
FLEKAMQLAK RHANALFDYA VTGDVKMLLA VQRHLTAVQD ENGDSVLHLA
560 570 580 590 600
IIHLHSQLVR DLLEVTSGLI SDDIINMRND LYQTPLHLAV ITKQEDVVED
610 620 630 640 650
LLRAGADLSL LDRLGNSVLH LAAKEGHDKV LSILLKHKKA ALLLDHPNGD
660 670 680 690 700
GLNAIHLAMM SNSLPCLLLL VAAGADVNAQ EQKSGRTALH LAVEHDNISL
710 720 730 740 750
AGCLLLEGDA HVDSTTYDGT TPLHIAAGRG STRLAALLKA AGADPLVENF
760 770 780 790 800
EPLYDLDDSW ENAGEDEGVV PGTTPLDMAT SWQVFDILNG KPYEPEFTSD
810 820 830 840 850
DLLAQGDMKQ LAEDVKLQLY KLLEIPDPDK NWATLAQKLG LGILNNAFRL
860 870 880 890 900
SPAPSKTLMD NYEVSGGTVR ELVEALRQMG YTEAIEVIQA ASSPVKTTSQ
910 920 930 940 950
AHSLPLSPAS TRQQIDELRD SDSVCDSGVE TSFRKLSFTE SLTSGASLLT
960
LNKMPHDYGQ EGPLEGKI
Length:968
Mass (Da):105,356
Last modified:June 20, 2002 - 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:i2A7C8FF86A10D1A8
GO
Isoform 2 (identifier: P19838-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     39-39: T → TA

Show »
Length:969
Mass (Da):105,427
Checksum:iB4D57AC8A410941D
GO
Isoform 3 (identifier: P19838-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-180: Missing.
     181-189: EGGGDRQLG → MNGLCCMAL

Note: No experimental confirmation available.
Show »
Length:788
Mass (Da):85,520
Checksum:i7B9913B97F25DD3F
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 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D6RF93D6RF93_HUMAN
Nuclear factor NF-kappa-B p105 subu...
NFKB1
196Annotation 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>
D6RC45D6RC45_HUMAN
Nuclear factor NF-kappa-B p105 subu...
NFKB1
144Annotation 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>
D6RH30D6RH30_HUMAN
Nuclear factor NF-kappa-B p105 subu...
NFKB1
198Annotation 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>
D6RDI9D6RDI9_HUMAN
Nuclear factor NF-kappa-B p105 subu...
NFKB1
74Annotation 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 conflicti243K → SE in CAB94757 (PubMed:8825636).Curated1
Sequence conflicti361R → G in CAH18336 (PubMed:17974005).Curated1
Sequence conflicti551 – 552II → SS in CAB94757 (PubMed:8825636).Curated2
Sequence conflicti573D → G in BAF84139 (PubMed:14702039).Curated1
Sequence conflicti726A → V in CAB94757 (PubMed:8825636).Curated1
Sequence conflicti825I → T in CAH18336 (PubMed:17974005).Curated1
Sequence conflicti869V → I in CAB94757 (PubMed:8825636).Curated1
Sequence conflicti927S → T in AAA36361 (PubMed:2203531).Curated1
Sequence conflicti927S → T in AAA36360 (PubMed:1992489).Curated1
Sequence conflicti927S → T in CAB94757 (PubMed:8825636).Curated1

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_016268489T → I1 PublicationCorresponds to variant dbSNP:rs4648065Ensembl.1
Natural variantiVAR_016269506M → V1 PublicationCorresponds to variant dbSNP:rs4648072Ensembl.1
Natural variantiVAR_016270566T → I1 PublicationCorresponds to variant dbSNP:rs4648085Ensembl.1
Natural variantiVAR_016271578R → K1 PublicationCorresponds to variant dbSNP:rs4648086Ensembl.1
Natural variantiVAR_016272711H → Q1 PublicationCorresponds to variant dbSNP:rs4648099Ensembl.1
Natural variantiVAR_016273901A → T1 PublicationCorresponds to variant dbSNP:rs4648118Ensembl.1

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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0428691 – 180Missing in isoform 3. 1 PublicationAdd BLAST180
Alternative sequenceiVSP_02102539T → TA in isoform 2. 3 Publications1
Alternative sequenceiVSP_042870181 – 189EGGGDRQLG → MNGLCCMAL in isoform 3. 1 Publication9

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
M55643 mRNA Translation: AAA36361.1
M58603 mRNA Translation: AAA36360.1
Z47748
, Z47749, Z47750, Z47751, Z47752, Z47753, Z47754, Z47755, Z47734, Z47735, Z47736, Z47737, Z47738, Z47739, Z47740, Z47741, Z47742, Z47743, Z47744 Genomic DNA Translation: CAB94757.1
AF213884 Genomic DNA Translation: AAF35232.1
AK122850 mRNA Translation: BAG53760.1
AK291450 mRNA Translation: BAF84139.1
CR749522 mRNA Translation: CAH18336.1
AY223820 Genomic DNA Translation: AAO30127.1
BC033210 mRNA Translation: AAH33210.1
BC051765 mRNA Translation: AAH51765.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS3657.1 [P19838-2]
CCDS54783.1 [P19838-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A37867

NCBI Reference Sequences

More...
RefSeqi
NP_001158884.1, NM_001165412.1 [P19838-1]
NP_001306155.1, NM_001319226.1 [P19838-1]
NP_003989.2, NM_003998.3 [P19838-2]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.618430

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000226574; ENSP00000226574; ENSG00000109320 [P19838-2]
ENST00000394820; ENSP00000378297; ENSG00000109320 [P19838-1]
ENST00000505458; ENSP00000424790; ENSG00000109320 [P19838-1]
ENST00000600343; ENSP00000469340; ENSG00000109320 [P19838-3]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
4790

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:4790

UCSC genome browser

More...
UCSCi
uc011cep.2 human [P19838-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55643 mRNA Translation: AAA36361.1
M58603 mRNA Translation: AAA36360.1
Z47748
, Z47749, Z47750, Z47751, Z47752, Z47753, Z47754, Z47755, Z47734, Z47735, Z47736, Z47737, Z47738, Z47739, Z47740, Z47741, Z47742, Z47743, Z47744 Genomic DNA Translation: CAB94757.1
AF213884 Genomic DNA Translation: AAF35232.1
AK122850 mRNA Translation: BAG53760.1
AK291450 mRNA Translation: BAF84139.1
CR749522 mRNA Translation: CAH18336.1
AY223820 Genomic DNA Translation: AAO30127.1
BC033210 mRNA Translation: AAH33210.1
BC051765 mRNA Translation: AAH51765.1
CCDSiCCDS3657.1 [P19838-2]
CCDS54783.1 [P19838-1]
PIRiA37867
RefSeqiNP_001158884.1, NM_001165412.1 [P19838-1]
NP_001306155.1, NM_001319226.1 [P19838-1]
NP_003989.2, NM_003998.3 [P19838-2]
UniGeneiHs.618430

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MDINMR-B55-67[»]
1MDJNMR-B55-67[»]
1MDKNMR-B55-67[»]
1NFIX-ray2.70B/D248-354[»]
1SVCX-ray2.60P2-365[»]
2DBFNMR-A806-893[»]
2O61X-ray2.80B40-352[»]
3GUTX-ray3.59B/D/F/H41-352[»]
ProteinModelPortaliP19838
SMRiP19838
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110857, 162 interactors
CORUMiP19838
DIPiDIP-106N
ELMiP19838
IntActiP19838, 476 interactors
MINTiP19838
STRINGi9606.ENSP00000226574

Chemistry databases

BindingDBiP19838
ChEMBLiCHEMBL3251
DrugBankiDB00945 Acetylsalicylic acid
DB05487 CC-8490
DB05212 HE3286
DB05767 HMPL-004
DB05464 NOX-700
DB05451 P54
DB01411 Pranlukast
DB05471 SGN-30
DB01041 Thalidomide
DB08814 Triflusal

PTM databases

iPTMnetiP19838
PhosphoSitePlusiP19838

Polymorphism and mutation databases

BioMutaiNFKB1
DMDMi21542418

Proteomic databases

EPDiP19838
jPOSTiP19838
MaxQBiP19838
PaxDbiP19838
PeptideAtlasiP19838
PRIDEiP19838
ProteomicsDBi53694
53695 [P19838-2]
53696 [P19838-3]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
4790
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000226574; ENSP00000226574; ENSG00000109320 [P19838-2]
ENST00000394820; ENSP00000378297; ENSG00000109320 [P19838-1]
ENST00000505458; ENSP00000424790; ENSG00000109320 [P19838-1]
ENST00000600343; ENSP00000469340; ENSG00000109320 [P19838-3]
GeneIDi4790
KEGGihsa:4790
UCSCiuc011cep.2 human [P19838-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4790
DisGeNETi4790
EuPathDBiHostDB:ENSG00000109320.11

GeneCards: human genes, protein and diseases

More...
GeneCardsi
NFKB1
HGNCiHGNC:7794 NFKB1
HPAiCAB004031
HPA027305
MalaCardsiNFKB1
MIMi164011 gene
616576 phenotype
neXtProtiNX_P19838
OpenTargetsiENSG00000109320
Orphaneti1572 Common variable immunodeficiency
PharmGKBiPA248

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0504 Eukaryota
COG0666 LUCA
GeneTreeiENSGT00940000158625
HOGENOMiHOG000004822
HOVERGENiHBG052613
InParanoidiP19838
KOiK02580
OMAiMTWIPRK
OrthoDBi916931at2759
PhylomeDBiP19838
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-5603029 IkBA variant leads to EDA-ID
R-HSA-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5621575 CD209 (DC-SIGN) signaling
R-HSA-5660668 CLEC7A/inflammasome pathway
R-HSA-5684264 MAP3K8 (TPL2)-dependent MAPK1/3 activation
R-HSA-6798695 Neutrophil degranulation
R-HSA-844456 The NLRP3 inflammasome
R-HSA-9020702 Interleukin-1 signaling
R-HSA-933542 TRAF6 mediated NF-kB activation
SignaLinkiP19838
SIGNORiP19838

Miscellaneous databases

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

More...
ChiTaRSi
NFKB1 human
EvolutionaryTraceiP19838

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
NFKB1

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

More...
GenomeRNAii
4790
PMAP-CutDBiP19838

Protein Ontology

More...
PROi
PR:P19838

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000109320 Expressed in 198 organ(s), highest expression level in leukocyte
CleanExiHS_NFKB1
ExpressionAtlasiP19838 baseline and differential
GenevisibleiP19838 HS

Family and domain databases

CDDicd00204 ANK, 1 hit
cd01177 IPT_NFkappaB, 1 hit
Gene3Di1.25.40.20, 1 hit
2.60.40.10, 1 hit
2.60.40.340, 1 hit
InterProiView protein in InterPro
IPR002110 Ankyrin_rpt
IPR020683 Ankyrin_rpt-contain_dom
IPR036770 Ankyrin_rpt-contain_sf
IPR011029 DEATH-like_dom_sf
IPR000488 Death_domain
IPR013783 Ig-like_fold
IPR014756 Ig_E-set
IPR002909 IPT_dom
IPR033926 IPT_NFkappaB
IPR030503 NF-kB_p105
IPR000451 NFkB/Dor
IPR008967 p53-like_TF_DNA-bd
IPR030492 RHD_CS
IPR032397 RHD_dimer
IPR011539 RHD_DNA_bind_dom
IPR037059 RHD_DNA_bind_dom_sf
PANTHERiPTHR24169 PTHR24169, 1 hit
PTHR24169:SF9 PTHR24169:SF9, 1 hit
PfamiView protein in Pfam
PF12796 Ank_2, 2 hits
PF00531 Death, 1 hit
PF16179 RHD_dimer, 1 hit
PF00554 RHD_DNA_bind, 1 hit
PRINTSiPR01415 ANKYRIN
PR00057 NFKBTNSCPFCT
SMARTiView protein in SMART
SM00248 ANK, 6 hits
SM00005 DEATH, 1 hit
SM00429 IPT, 1 hit
SUPFAMiSSF47986 SSF47986, 1 hit
SSF48403 SSF48403, 1 hit
SSF49417 SSF49417, 1 hit
SSF81296 SSF81296, 1 hit
PROSITEiView protein in PROSITE
PS50297 ANK_REP_REGION, 1 hit
PS50088 ANK_REPEAT, 5 hits
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 nameiNFKB1_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: P19838
Secondary accession number(s): A8K5Y5
, B3KVE8, Q68D84, Q86V43, Q8N4X7, Q9NZC0
<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: February 1, 1991
Last sequence update: June 20, 2002
Last modified: January 16, 2019
This is version 239 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, Direct protein sequencing, Reference proteome

Documents

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