Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P25799 (NFKB1_MOUSE)

Entry version 225 (07 Apr 2021)
Sequence version 2 (27 Jul 2011)
Previous versions | rss
Add a publicationFeedback
Protein

Nuclear factor NF-kappa-B p105 subunit

Gene

Nfkb1

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 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. Plays a role in the regulation of apoptosis. Isoform 5, isoform 6 and isoform 7 act as inhibitors of transactivation of p50 NF-kappa-B subunit, probably by sequestering it in the cytoplasm. Isoform 3 (p98) (but not p84 or p105) acts as a transactivator of NF-kappa-B-regulated gene expression. In a complex with MAP3K8, NFKB1/p105 represses MAP3K8-induced MAPK signaling; active MAP3K8 is released by proteasome-dependent degradation of NFKB1/p105.

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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

More...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-5607764, CLEC7A (Dectin-1) signaling
R-MMU-5621575, CD209 (DC-SIGN) signaling
R-MMU-5684264, MAP3K8 (TPL2)-dependent MAPK1/3 activation
R-MMU-6798695, Neutrophil degranulation
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%5Fand%5Ftaxonomy%5Fsection">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
NF-kappa-B1 p84/NF-kappa-B1 p98
Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1
Cleaved into the following chain:
Nuclear factor NF-kappa-B p50 subunit
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 3

Organism-specific databases

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

More...MGIi		MGI:97312, Nfkb1

<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

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		CHEMBL1949489

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000303121 – 971Nuclear factor NF-kappa-B p105 subunitAdd BLAST971
ChainiPRO_00000303131 – 431Nuclear factor NF-kappa-B p50 subunitBy similarityAdd BLAST431

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 residuei59S-nitrosocysteine; alternateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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>Lipidationi59S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine; alternateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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-linki323Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei335Phosphoserine; by PKASequence analysis1
Modified residuei438N6-acetyllysine; by EP300By similarity1
Modified residuei447PhosphoserineCombined sources1
Modified residuei674(3S)-3-hydroxyasparagine; by HIF1ANBy similarity1
Modified residuei755PhosphoserineBy similarity1
Modified residuei896PhosphoserineBy similarity1
Modified residuei910Phosphoserine; by GSK3-beta; in vitroBy similarity1
Modified residuei930Phosphoserine; by IKKBBy similarity1
Modified residuei935Phosphoserine; by IKKBBy similarity1
Modified residuei940PhosphoserineCombined sources1
Modified residuei946PhosphothreonineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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.
Phosphorylation at 'Ser-930' and 'Ser-935' are required for BTRC/BTRCP-mediated proteolysis.By similarity
Polyubiquitination seems to allow p105 processing.
S-nitrosylation of Cys-59 affects DNA binding.By similarity
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 (By similarity).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>Sitei431 – 432Cleavage (when cotranslationally processed)By similarity2

Keywords - PTMi

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

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P25799

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P25799

MaxQB - The MaxQuant DataBase

More...MaxQBi		P25799

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

More...PaxDbi		P25799

PeptideAtlas

More...PeptideAtlasi		P25799

PRoteomics IDEntifications database

More...PRIDEi		P25799

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		287411 [P25799-1]
287412 [P25799-2]
287413 [P25799-3]
287414 [P25799-4]
287415 [P25799-5]
287416 [P25799-6]
287417 [P25799-7]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P25799

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

More...PhosphoSitePlusi		P25799

<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-alpha.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000028163, Expressed in spleen and 305 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P25799, 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%5Fsection">'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%5Fsection">'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 (By similarity). NFKB1/p50 interacts with NFKBIZ. Nuclear factor NF-kappa-B p50 subunit interacts with NFKBID. Directly interacts with MEN1 (By similarity).

Interacts with HIF1AN (By similarity).

By similarity

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		201751, 15 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P25799

Database of interacting proteins

More...DIPi		DIP-85N

Protein interaction database and analysis system

More...IntActi		P25799, 20 interactors

Molecular INTeraction database

More...MINTi		P25799

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000029812

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P25799, protein

<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

1971
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P25799

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P25799

<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%5Fand%5Fdomains%5Fsection">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>Domaini40 – 365RHDPROSITE-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>Repeati538 – 567ANK 1Add BLAST30
Repeati577 – 606ANK 2Add BLAST30
Repeati610 – 639ANK 3Add BLAST30
Repeati646 – 675ANK 4Add BLAST30
Repeati680 – 710ANK 5Add BLAST31
Repeati714 – 743ANK 6Add BLAST30
Repeati767 – 797ANK 7Add BLAST31
Domaini801 – 888DeathAdd 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>Regioni370 – 392GRRAdd BLAST23
Regioni433 – 971Interaction with CFLARBy similarityAdd BLAST539
Regioni646 – 680Essential for interaction with HIF1ANBy similarityAdd 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>Motifi358 – 363Nuclear 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 biasi373 – 431Gly-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

More...eggNOGi		KOG0504, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000158625

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_004343_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P25799

Database of Orthologous Groups

More...OrthoDBi		916931at2759

TreeFam database of animal gene trees

More...TreeFami		TF325632

Family and domain databases

Conserved Domains Database

More...CDDi		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
PF00023, Ank, 1 hit
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		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%5Flength">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 (7+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 7 <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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 7 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P25799-1) [UniParc]FASTAAdd to basket
Also known as: p105

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

« Hide
        10         20         30         40         50
MADDDPYGTG QMFHLNTALT HSIFNAELYS PEIPLSTDGP YLQILEQPKQ 
        60         70         80         90        100
RGFRFRYVCE GPSHGGLPGA SSEKNKKSYP QVKICNYVGP AKVIVQLVTN 
       110        120        130        140        150
GKNIHLHAHS LVGKHCEDGV CTVTAGPKDM VVGFANLGIL HVTKKKVFET 
       160        170        180        190        200
LEARMTEACI RGYNPGLLVH SDLAYLQAEG GGDRQLTDRE KEIIRQAAVQ 
       210        220        230        240        250
QTKEMDLSVV RLMFTAFLPD STGSFTRRLE PVVSDAIYDS KAPNASNLKI 
       260        270        280        290        300
VRMDRTAGCV TGGEEIYLLC DKVQKDDIQI RFYEEEENGG VWEGFGDFSP 
       310        320        330        340        350
TDVHRQFAIV FKTPKYKDVN ITKPASVFVQ LRRKSDLETS EPKPFLYYPE 
       360        370        380        390        400
IKDKEEVQRK RQKLMPNFSD SFGGGSGAGA GGGGMFGSGG GGGSTGSPGP 
       410        420        430        440        450
GYGYSNYGFP PYGGITFHPG VTKSNAGVTH GTINTKFKNG PKDCAKSDDE 
       460        470        480        490        500
ESLTLPEKET EGEGPSLPMA CTKTEPIALA STMEDKEQDM GFQDNLFLEK 
       510        520        530        540        550
ALQLARRHAN ALFDYAVTGD VKMLLAVQRH LTAVQDENGD SVLHLAIIHL 
       560        570        580        590        600
HAQLVRDLLE VTSGLISDDI INMRNDLYQT PLHLAVITKQ EDVVEDLLRV 
       610        620        630        640        650
GADLSLLDRW GNSVLHLAAK EGHDRILSIL LKSRKAAPLI DHPNGEGLNA 
       660        670        680        690        700
IHIAVMSNSL PCLLLLVAAG AEVNAQEQKS GRTALHLAVE YDNISLAGCL 
       710        720        730        740        750
LLEGDAHVDS TTYDGTTPLH IAAGRGSTRL AALLKAAGAD PLVENFEPLY 
       760        770        780        790        800
DLDDSWEKAG EDEGVVPGTT PLDMAANWQV FDILNGKPYE PVFTSDDILP 
       810        820        830        840        850
QGDMKQLTED TRLQLCKLLE IPDPDKNWAT LAQKLGLGIL NNAFRLSPAP 
       860        870        880        890        900
SKTLMDNYEV SGGTIKELME ALQQMGYTEA IEVIQAAFRT PATTASSPVT 
       910        920        930        940        950
TAQVHCLPLS SSSTRQHIDE LRDSDSVCDS GVETSFRKLS FTESLTGDSP 
       960        970 
LLSLNKMPHG YGQEGPIEGK I
Length:971
Mass (Da):105,615
Last modified:July 27, 2011 - 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:i91EA9C595E375C30
GO
Isoform 2 (identifier: P25799-2) [UniParc]FASTAAdd to basket
Also known as: p84

The sequence of this isoform differs from the canonical sequence as follows:
     780-971: VFDILNGKPY...GQEGPIEGKI → GT

Show »
Length:781
Mass (Da):84,817
Checksum:i51B98D66F21BF5EC
GO
Isoform 3 (identifier: P25799-3) [UniParc]FASTAAdd to basket
Also known as: p98

The sequence of this isoform differs from the canonical sequence as follows:
     860-971: VSGGTIKELM...GQEGPIEGKI → MNSGIVTASVTVVWRHPSANSALQSLLLETAHCYL

Show »
Length:894
Mass (Da):97,413
Checksum:i8445F5C4CA02D7E4
GO
Isoform 4 (identifier: P25799-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     353-356: DKEE → GTWV
     357-971: Missing.

Show »
Length:356
Mass (Da):39,756
Checksum:i09E32E7A3B63F46A
GO
Isoform 5 (identifier: P25799-5) [UniParc]FASTAAdd to basket
Also known as: P70, I-kappa-B gamma

The sequence of this isoform differs from the canonical sequence as follows:
     1-364: Missing.

Show »
Length:607
Mass (Da):64,782
Checksum:i1B79975F022DF4E2
GO
Isoform 6 (identifier: P25799-6) [UniParc]FASTAAdd to basket
Also known as: p63, I-kappa-B gamma-1

The sequence of this isoform differs from the canonical sequence as follows:
     1-364: Missing.
     860-971: VSGGTIKELM...GQEGPIEGKI → MNSGIVTASVTVVWRHPSANSALQSLLLETAHCYL

Show »
Length:530
Mass (Da):56,580
Checksum:iC7384490B44048FC
GO
Isoform 7 (identifier: P25799-7) [UniParc]FASTAAdd to basket
Also known as: p55, I-kappa-B gamma-2

The sequence of this isoform differs from the canonical sequence as follows:
     1-364: Missing.
     780-971: VFDILNGKPY...GQEGPIEGKI → GT

Note: Inhibits the activity of the p50 NF-kappa-B subunit.Curated
Show »
Length:417
Mass (Da):43,983
Checksum:iDEA2D2B56CDDC6D3
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
F6Z9G5F6Z9G5_MOUSE
Nuclear factor NF-kappa-B p105 subu...
Nfkb1
534Annotation 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>
V9GX90V9GX90_MOUSE
Nuclear factor NF-kappa-B p105 subu...
Nfkb1
270Annotation 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>
A0A0G2JGK6A0A0G2JGK6_MOUSE
Nuclear factor NF-kappa-B p105 subu...
Nfkb1
128Annotation 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>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAC35117 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

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 conflicti111L → P in AAR00341 (Ref. 9) Curated1
Sequence conflicti265E → G in BAC35117 (PubMed:16141072).Curated1
Sequence conflicti530H → D in BAE34261 (PubMed:16141072).Curated1
Sequence conflicti546A → G in BAE34261 (PubMed:16141072).Curated1
Sequence conflicti684A → P in AAA40415 (PubMed:2203532).Curated1
Sequence conflicti684A → P in AAB21851 (PubMed:1339305).Curated1
Sequence conflicti684A → P in AAB28573 (PubMed:8398903).Curated1
Sequence conflicti732A → T in BAE34261 (PubMed:16141072).Curated1
Sequence conflicti950P → A in BAE43399 (PubMed:16141072).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_0172361 – 364Missing in isoform 5, isoform 6 and isoform 7. 2 PublicationsAdd BLAST364
Alternative sequenceiVSP_017237353 – 356DKEE → GTWV in isoform 4. 2 Publications4
Alternative sequenceiVSP_017238357 – 971Missing in isoform 4. 2 PublicationsAdd BLAST615
Alternative sequenceiVSP_005583780 – 971VFDIL…IEGKI → GT in isoform 2 and isoform 7. 1 PublicationAdd BLAST192
Alternative sequenceiVSP_005584860 – 971VSGGT…IEGKI → MNSGIVTASVTVVWRHPSAN SALQSLLLETAHCYL in isoform 3 and isoform 6. 1 PublicationAdd BLAST112

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
M57999 mRNA Translation: AAA40415.1
S89033 mRNA Translation: AAB21851.1
S66656 mRNA Translation: AAB28573.1
AB119195 mRNA Translation: BAC84979.1
AY521462 mRNA Translation: AAS00547.1
AY521463 mRNA Translation: AAS00548.1
CH466532 Genomic DNA Translation: EDL12143.1
BC050841 mRNA Translation: AAH50841.1
BC138535 mRNA Translation: AAI38536.1
BC138536 mRNA Translation: AAI38537.1
AY423849 mRNA Translation: AAR00341.1
AK052726 mRNA Translation: BAC35117.1 Different initiation.
AK089660 mRNA Translation: BAE43399.1
AK157915 mRNA Translation: BAE34261.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS17858.1 [P25799-1]

Protein sequence database of the Protein Information Resource

More...PIRi		A35697

NCBI Reference Sequences

More...RefSeqi		NP_032715.2, NM_008689.2 [P25799-1]
XP_006501169.1, XM_006501106.2 [P25799-3]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000029812; ENSMUSP00000029812; ENSMUSG00000028163 [P25799-1]
ENSMUST00000164430; ENSMUSP00000128345; ENSMUSG00000028163 [P25799-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		18033

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:18033

UCSC genome browser

More...UCSCi		uc008rlw.1, mouse [P25799-1]
uc008rly.1, mouse [P25799-4]
uc012cyf.1, mouse [P25799-6]

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
M57999 mRNA Translation: AAA40415.1
S89033 mRNA Translation: AAB21851.1
S66656 mRNA Translation: AAB28573.1
AB119195 mRNA Translation: BAC84979.1
AY521462 mRNA Translation: AAS00547.1
AY521463 mRNA Translation: AAS00548.1
CH466532 Genomic DNA Translation: EDL12143.1
BC050841 mRNA Translation: AAH50841.1
BC138535 mRNA Translation: AAI38536.1
BC138536 mRNA Translation: AAI38537.1
AY423849 mRNA Translation: AAR00341.1
AK052726 mRNA Translation: BAC35117.1 Different initiation.
AK089660 mRNA Translation: BAE43399.1
AK157915 mRNA Translation: BAE34261.1
CCDSiCCDS17858.1 [P25799-1]
PIRiA35697
RefSeqiNP_032715.2, NM_008689.2 [P25799-1]
XP_006501169.1, XM_006501106.2 [P25799-3]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BFSX-ray2.20A245-350[»]
1IKNX-ray2.30C245-363[»]
1LE5X-ray2.75B/F39-350[»]
1LE9X-ray3.00B/F39-350[»]
1LEIX-ray2.70B39-350[»]
1NFKX-ray2.30A/B39-363[»]
1OOAX-ray2.45A/B39-363[»]
1U36X-ray1.89A245-350[»]
1U3JX-ray1.90A245-350[»]
1U3YX-ray1.90A245-350[»]
1U3ZX-ray1.90A245-350[»]
1U41X-ray2.20A/B/C/D245-350[»]
1U42X-ray2.70A245-350[»]
1VKXX-ray2.90B39-350[»]
2I9TX-ray2.80B39-350[»]
2V2TX-ray3.05B38-363[»]
3JV4X-ray3.15B/D/F245-359[»]
SMRiP25799
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi201751, 15 interactors
CORUMiP25799
DIPiDIP-85N
IntActiP25799, 20 interactors
MINTiP25799
STRINGi10090.ENSMUSP00000029812

Chemistry databases

ChEMBLiCHEMBL1949489

PTM databases

iPTMnetiP25799
PhosphoSitePlusiP25799

Proteomic databases

EPDiP25799
jPOSTiP25799
MaxQBiP25799
PaxDbiP25799
PeptideAtlasiP25799
PRIDEiP25799
ProteomicsDBi287411 [P25799-1]
287412 [P25799-2]
287413 [P25799-3]
287414 [P25799-4]
287415 [P25799-5]
287416 [P25799-6]
287417 [P25799-7]

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		P25799, 1 sequenced antibody

Antibodypedia a portal for validated antibodies

More...Antibodypediai		3415, 2359 antibodies

Genome annotation databases

EnsembliENSMUST00000029812; ENSMUSP00000029812; ENSMUSG00000028163 [P25799-1]
ENSMUST00000164430; ENSMUSP00000128345; ENSMUSG00000028163 [P25799-1]
GeneIDi18033
KEGGimmu:18033
UCSCiuc008rlw.1, mouse [P25799-1]
uc008rly.1, mouse [P25799-4]
uc012cyf.1, mouse [P25799-6]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		4790
MGIiMGI:97312, Nfkb1

Phylogenomic databases

eggNOGiKOG0504, Eukaryota
GeneTreeiENSGT00940000158625
HOGENOMiCLU_004343_1_0_1
InParanoidiP25799
OrthoDBi916931at2759
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-5607764, CLEC7A (Dectin-1) signaling
R-MMU-5621575, CD209 (DC-SIGN) signaling
R-MMU-5684264, MAP3K8 (TPL2)-dependent MAPK1/3 activation
R-MMU-6798695, Neutrophil degranulation
R-MMU-9020702, Interleukin-1 signaling
R-MMU-933542, TRAF6 mediated NF-kB activation

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		18033, 2 hits in 56 CRISPR screens

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

More...ChiTaRSi		Nfkb1, mouse
EvolutionaryTraceiP25799

Protein Ontology

More...PROi		PR:P25799
RNActiP25799, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000028163, Expressed in spleen and 305 other tissues
GenevisibleiP25799, 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
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
PF00023, Ank, 1 hit
PF12796, Ank_2, 2 hits
PF00531, Death, 1 hit
PF16179, RHD_dimer, 1 hit
PF00554, RHD_DNA_bind, 1 hit
PRINTSiPR00057, 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...

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 nameiNFKB1_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: P25799
Secondary accession number(s): B2RRQ6
, Q3TZE8, Q3V2V6, Q6TDG8, Q75ZL1, Q80Y21, Q8C712
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: July 27, 2011
Last modified: April 7, 2021
This is version 225 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

<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, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again