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Entry version 167 (16 Oct 2019)
Sequence version 1 (01 Nov 1999)
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Protein

Nuclear factor NF-kappa-B p100 subunit

Gene

Nfkb2

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 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. In a non-canonical activation pathway, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes. The NF-kappa-B heterodimeric RelB-p52 complex is a transcriptional activator. The NF-kappa-B p52-p52 homodimer is a transcriptional repressor. NFKB2 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p100 and generation of p52 by a cotranslational processing. The proteasome-mediated process ensures the production of both p52 and p100 and preserves their independent function. p52 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. p52 and p100 are respectively the minor and major form; the processing of p100 being relatively poor. Isoform p49 is a subunit of the NF-kappa-B protein complex, which stimulates the HIV enhancer in synergy with p65 (By similarity). In concert with RELB, regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer.By similarity1 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, Repressor
Biological processBiological rhythms, Transcription, Transcription regulation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-1810476 RIP-mediated NFkB activation via ZBP1
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-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-MMU-5676590 NIK-->noncanonical NF-kB 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:
Nuclear factor NF-kappa-B p100 subunit
Alternative name(s):
DNA-binding factor KBF2
Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2
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:Nfkb2
<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:1099800 Nfkb2

<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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3879845

<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_00000303231 – 899Nuclear factor NF-kappa-B p100 subunitAdd BLAST899
ChainiPRO_00000303241 – 454Nuclear factor NF-kappa-B p52 subunitAdd BLAST454

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 residuei23PhosphoserineBy similarity1
Modified residuei161PhosphoserineBy similarity1
Modified residuei425PhosphothreonineCombined sources1
Modified residuei713PhosphoserineBy similarity1
Modified residuei715PhosphoserineBy similarity1
Modified residuei717PhosphoserineBy similarity1
Modified residuei812PhosphoserineBy 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-linki855Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei865Phosphoserine; by MAP3K14By similarity1
Modified residuei869Phosphoserine; by MAP3K14By 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 p52 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 (By similarity).By similarity
Subsequent to MAP3K14-dependent serine phosphorylation, p100 polyubiquitination occurs then triggering its proteasome-dependent processing.By similarity
Constitutive processing is tightly suppressed by its C-terminal processing inhibitory domain, named PID, which contains the death domain.By similarity

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>Sitei454 – 455Cleavage (when cotranslationally processed)2

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q9WTK5

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q9WTK5

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q9WTK5

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

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PaxDbi
Q9WTK5

PRoteomics IDEntifications database

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PRIDEi
Q9WTK5

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9WTK5

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

More...
PhosphoSitePlusi
Q9WTK5

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q9WTK5

<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 provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Highly expressed in lymph nodes and thymus.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000025225 Expressed in 259 organ(s), highest expression level in spleen

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9WTK5 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9WTK5 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 RelB-p52 complex. Homodimer; component of the NF-kappa-B p52-p52 complex.

Component of the NF-kappa-B p65-p52 complex.

Component of the NF-kappa-B p52-c-Rel complex. NFKB2/p52 interacts with NFKBIE.

Component of a complex consisting of the NF-kappa-B p50-p50 homodimer and BCL3 (By similarity). Directly interacts with MEN1 (By similarity).

By similarity

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

WithEntry#Exp.IntActNotes
RelbQ048632EBI-1209166,EBI-1209145

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
201752, 7 interactors

Protein interaction database and analysis system

More...
IntActi
Q9WTK5, 3 interactors

Molecular INTeraction database

More...
MINTi
Q9WTK5

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000107512

<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

1899
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
Q9WTK5

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<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>Domaini35 – 224RHDPROSITE-ProRule annotationAdd BLAST190
<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>Repeati487 – 516ANK 1Add BLAST30
Repeati526 – 555ANK 2Add BLAST30
Repeati559 – 590ANK 3Add BLAST32
Repeati599 – 628ANK 4Add BLAST30
Repeati633 – 663ANK 5Add BLAST31
Repeati667 – 696ANK 6Add BLAST30
Repeati729 – 755ANK 7Add BLAST27
Domaini764 – 851DeathAdd 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>Regioni346 – 377GRRAdd BLAST32

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi337 – 341Nuclear localization signalSequence analysis5

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 biasi351 – 404Gly-richAdd BLAST54

<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 p100 might be involved in cytoplasmic retention, inhibition of DNA-binding by p52 homodimers, and/or transcription activation.By similarity
The glycine-rich region (GRR) appears to be a critical element in the generation of p52.

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
ENSGT00940000160968

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9WTK5

KEGG Orthology (KO)

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KOi
K04469

Identification of Orthologs from Complete Genome Data

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OMAi
VIYHAPH

Database of Orthologous Groups

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OrthoDBi
916931at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9WTK5

TreeFam database of animal gene trees

More...
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
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

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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
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

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PANTHERi
PTHR24169 PTHR24169, 1 hit

Pfam protein domain database

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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

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PRINTSi
PR01415 ANKYRIN
PR00057 NFKBTNSCPFCT

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00248 ANK, 7 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>. 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>Sequence (1+)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 has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

Q9WTK5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDNCYDPGLD GIPEYDDFEF SPSIVEPKDP APETADGPYL VIVEQPKQRG
60 70 80 90 100
FRFRYGCEGP SHGGLPGASS EKGRKTYPTV KICNYEGPAK IEVDLVTHSD
110 120 130 140 150
PPRAHAHSLV GKQCSELGVC AVSVGPKDMT AQFNNLGVLH VTKKNMMEIM
160 170 180 190 200
IQKLQRQRLR SKPQGLTEAE RRELEQEAKE LKKVMDLSIV RLRFSAFLRA
210 220 230 240 250
SDGSFSLPLK PVISQPIHDS KSPGASNLKI SRMDKTAGSV RGGDEVYLLC
260 270 280 290 300
DKVQKDDIEV RFYEDDENGW QAFGDFSPTD VHKQYAIVFR TPPYHKMKIE
310 320 330 340 350
RPVTVFLQLK RKRGGDVSDS KQFTYYPLVE DKEEVQRKRR KALPTFSQPF
360 370 380 390 400
GGGSHMGGGS GGSAGGYGGA GGGGSLGFFS SSLAYNPYQS GAAPMGCYPG
410 420 430 440 450
GGGGAQMAGS RRDTDAGEGA EEPRTPPEAP QGEPQALDTL QRAREYNARL
460 470 480 490 500
FGLAQRSARA LLDYGVTADA RALLAGQRHL LMAQDENGDT PLHLAIIHGQ
510 520 530 540 550
TGVIEQIAHV IYHAQYLGVI NLTNHLHQTP LHLAVITGQT RVVSFLLQVG
560 570 580 590 600
ADPTLLDRHG DSALHLALRA GAAAPELLQA LLRSGAHAVP QILHMPDFEG
610 620 630 640 650
LYPVHLAVHA RSPECLDLLV DCGAEVEAPE RQGGRTALHL ATEMEELGLV
660 670 680 690 700
THLVTKLHAN VNARTFAGNT PLHLAAGLGS PTLTRLLLKA GADIHAENEE
710 720 730 740 750
PLCPLPSPST SGSDSDSEGP ERDTQRNFRG HTPLDLTCST KVKTLLLNAA
760 770 780 790 800
QNTTEPPLAP PSPAGPGLSL GDAALQNLEQ LLDGPEAQGS WAELAERLGL
810 820 830 840 850
RSLVDTYRKT PSPSGSLLRS YKLAGGDLVG LLEALSDMGL HEGVRLLKGP
860 870 880 890
ETRDKLPSTE VKEDSAYGSQ SVEQEAEKLC PPPEPPGGLC HGHPQPQVH
Length:899
Mass (Da):96,832
Last modified:November 1, 1999 - 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:i3E98619F7D1C8AC7
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A494B9Y5A0A494B9Y5_MOUSE
Nuclear factor NF-kappa-B p100 subu...
Nfkb2
878Annotation 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>
A0A494BAQ2A0A494BAQ2_MOUSE
Nuclear factor NF-kappa-B p100 subu...
Nfkb2
776Annotation 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>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AF155373 mRNA Translation: AAD39547.1
AF135125 Genomic DNA Translation: AAD39462.1
AF155372 mRNA Translation: AAD39546.1
BC027423 mRNA Translation: AAH27423.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS29874.1

NCBI Reference Sequences

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RefSeqi
NP_001170840.1, NM_001177369.1
NP_062281.1, NM_019408.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000073116; ENSMUSP00000072859; ENSMUSG00000025225
ENSMUST00000111881; ENSMUSP00000107512; ENSMUSG00000025225
ENSMUST00000236591; ENSMUSP00000157542; ENSMUSG00000025225

Database of genes from NCBI RefSeq genomes

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GeneIDi
18034

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:18034

UCSC genome browser

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UCSCi
uc008hst.2 mouse

<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
AF155373 mRNA Translation: AAD39547.1
AF135125 Genomic DNA Translation: AAD39462.1
AF155372 mRNA Translation: AAD39546.1
BC027423 mRNA Translation: AAH27423.1
CCDSiCCDS29874.1
RefSeqiNP_001170840.1, NM_001177369.1
NP_062281.1, NM_019408.3

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
3JV5X-ray2.65A/B/C/D225-328[»]
3JV6X-ray2.78B/D/F225-331[»]
SMRiQ9WTK5
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi201752, 7 interactors
IntActiQ9WTK5, 3 interactors
MINTiQ9WTK5
STRINGi10090.ENSMUSP00000107512

Chemistry databases

ChEMBLiCHEMBL3879845

PTM databases

iPTMnetiQ9WTK5
PhosphoSitePlusiQ9WTK5
SwissPalmiQ9WTK5

Proteomic databases

EPDiQ9WTK5
jPOSTiQ9WTK5
MaxQBiQ9WTK5
PaxDbiQ9WTK5
PRIDEiQ9WTK5

Genome annotation databases

EnsembliENSMUST00000073116; ENSMUSP00000072859; ENSMUSG00000025225
ENSMUST00000111881; ENSMUSP00000107512; ENSMUSG00000025225
ENSMUST00000236591; ENSMUSP00000157542; ENSMUSG00000025225
GeneIDi18034
KEGGimmu:18034
UCSCiuc008hst.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4791
MGIiMGI:1099800 Nfkb2

Phylogenomic databases

eggNOGiKOG0504 Eukaryota
COG0666 LUCA
GeneTreeiENSGT00940000160968
InParanoidiQ9WTK5
KOiK04469
OMAiVIYHAPH
OrthoDBi916931at2759
PhylomeDBiQ9WTK5
TreeFamiTF325632

Enzyme and pathway databases

ReactomeiR-MMU-1810476 RIP-mediated NFkB activation via ZBP1
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-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-MMU-5676590 NIK-->noncanonical NF-kB 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
Nfkb2 mouse

Protein Ontology

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PROi
PR:Q9WTK5

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000025225 Expressed in 259 organ(s), highest expression level in spleen
ExpressionAtlasiQ9WTK5 baseline and differential
GenevisibleiQ9WTK5 MM

Family and domain databases

CDDicd01177 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
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
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, 7 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

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiNFKB2_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: Q9WTK5
<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: May 10, 2004
Last sequence update: November 1, 1999
Last modified: October 16, 2019
This is version 167 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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