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Entry version 163 (23 Feb 2022)
Sequence version 1 (01 Jan 1990)
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Protein

Protein FosB

Gene

Fosb

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

Heterodimerizes with proteins of the JUN family to form an AP-1 transcription factor complex, thereby enhancing their DNA binding activity to gene promoters containing an AP-1 consensus sequence 5'-TGA[GC]TCA-3' and enhancing their transcriptional activity (PubMed:2498083, PubMed:1900040).

As part of the AP-1 complex, facilitates enhancer selection together with cell-type-specific transcription factors by collaboratively binding to nucleosomal enhancers and recruiting the SWI/SNF (BAF) chromatin remodeling complex to establish accessible chromatin (PubMed:29272704).

Together with JUN, plays a role in activation-induced cell death of T cells by binding to the AP-1 promoter site of FASLG/CD95L, and inducing its transcription in response to activation of the TCR/CD3 signaling pathway (By similarity).

Exhibits transactivation activity in vitro (PubMed:17241283).

Involved in the display of nurturing behavior towards newborns (PubMed:8706134).

May play a role in neurogenesis in the hippocampus and in learning and memory-related tasks by regulating the expression of various genes involved in neurogenesis, depression and epilepsy (PubMed:23303048, PubMed:30902680).

Implicated in behavioral responses related to morphine reward and spatial memory (PubMed:9294222, PubMed:18407360).

By similarity9 Publications

Exhibits lower transactivation activity than isoform 1 in vitro (PubMed:17241283).

The heterodimer with JUN does not display any transcriptional activity, and may thereby act as an transcriptional inhibitor (PubMed:1900040).

May be involved in the regulation of neurogenesis in the hippocampus (PubMed:23303048).

May play a role in synaptic modifications in nucleus accumbens medium spiny neurons and thereby play a role in adaptive and pathological reward-dependent learning, including maladaptive responses involved in drug addiction (PubMed:23319622).

Seems to be more stably expressed with a half-life of ~9.5 hours in cell culture as compared to 1.5 hours half-life of isoform 1 (PubMed:18407360).

5 Publications

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

GO - Biological processi

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

Molecular functionDNA-binding

<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:
Protein FosBCurated
Alternative name(s):
FBJ osteosarcoma oncogene BImported
Transcription factor AP-1 subunit FosBCurated
<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:FosbImported
<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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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 7

Organism-specific databases

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

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MGIi
MGI:95575, Fosb

Eukaryotic Pathogen, Vector and Host Database Resources

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VEuPathDBi
HostDB:ENSMUSG00000003545

<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

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 describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Deficiency in the ability to nurture young animals and the majority of pups die within 1-2 days of birth (PubMed:8706134). Impaired nurturing behavior towards newborns is observed in postpartum mothers as well as in young females and males (PubMed:8706134). Failure in AP-1 binding activity after repeated cocaine administration (PubMed:9294222). Exaggerated locomotor activation in response to initial cocaine exposures as well as robust conditioned place preference to a lower dose of cocaine, but lack of increment in cocaine-induced hyperactivity over 6 days (i.e. sensitization) (PubMed:9294222). Decreased sensitivity to rewarding properties of morphine and spatial memory impairment (PubMed:18407360). Decreased proliferation and increased ectopic migration of neural progenitor cells in the hippocampus (PubMed:23303048). Exhibit impaired adult hippocampal neurogenesis and spontaneous epilepsy with depressive behavior (PubMed:23303048). Altered gene expression in the hippocampus, including genes implicated in neurogenesis, depression, or epilepsy (PubMed:23303048). Knockout in hippocampal neurons, including neurons of the subgranular zone of the dentate gyrus, leads to a reduction of antidepressant-induced neurogenesis and impedes hippocampus-dependent learning in the novel object recognition task (PubMed:30902680).5 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi27S → A: Increased degradation by the proteasome and a decrease in isoform 2/deltaFosB transactivation activity. 1 Publication1
Mutagenesisi27S → D: Increased protein stability. 1 Publication1

<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_00000764771 – 338Protein FosBAdd BLAST338

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 residuei27Phosphoserine1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi172Interchain (with C-279 in JUND)By similarity

<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

Phosphorylated.1 Publication
Phosphorylated at Ser-27 by CSNK2A1; phosphorylation increases protein stability and transactivation potential.2 Publications

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

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MaxQBi
P13346

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

More...
PaxDbi
P13346

PRoteomics IDEntifications database

More...
PRIDEi
P13346

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
271710

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P13346

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

More...
PhosphoSitePlusi
P13346

<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

Expressed in brain, including the preoptic area of the hypothalamus, the main and accessory olfactory bulbs, the pyriform cortex and the hippocampus (at protein level) (PubMed:8706134, PubMed:23303048). Expressed in the neurons of the subgranular zone of the dentate gyrus in the hippocampus (at protein level) (PubMed:23303048, PubMed:30902680). Expressed in pyramidal cells in CA1 and CA3, in the dentate gyrus and the nucleus accumbens of the striatum (at protein level) (PubMed:9294222, PubMed:26446228).5 Publications
Expressed in the core and shell of the nucleus accumbens of the striatum (at protein level) (PubMed:20473292). Expressed in the neurons of the subgranular zone of the dentate gyrus in the hippocampus (at protein level) (PubMed:23303048).2 Publications

<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

Induced by growth factors (PubMed:2498083). Up-regulated in the preoptic area of the hypothalamus after 6 hours of exposure to pups (PubMed:8706134). Induced by cocaine in the striatum (PubMed:9294222). Induced by kainic acid (PubMed:23303048). Induced in the hippocampus by novelty exposure and spatial learning (PubMed:26446228).5 Publications
Induced by cocaine in the striatum.1 Publication
Induced by cocaine in the striatum (PubMed:9294222). Induced by chronic social defeat stress, with resilient mice showing the greatest induction in both core and shell nucleus accumbens subregions (PubMed:20473292).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000003545, Expressed in islet of Langerhans and 126 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P13346, 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

Heterodimer; binds to DNA as heterodimer (PubMed:2498083, PubMed:1900040).

Component of an AP-1 transcription factor complex; composed of FOS-JUN heterodimers (PubMed:2498083, PubMed:1900040). As part of the AP-1 transcription factor complex, forms heterodimers with JUN, JUNB or JUND, thereby binding to the AP-1 consensus sequence and stimulating transcription (PubMed:2498083, PubMed:1900040).

Interacts with the BAF multiprotein chromatin-remodeling complex subunits SMARCB1 and SMARCD1 (PubMed:29272704).

Interacts with ARID1A and JUN (PubMed:29272704).

3 Publications

Homodimer under oxidizing conditions and monomer under reducing conditions (in vitro) (By similarity). Heterodimer; binds to DNA as heterodimer (PubMed:1900040). Forms heterodimers with JUNB, JUN or JUND; thereby binding to the AP-1 consensus sequence but does not stimulate transcription (PubMed:1900040). Forms heterodimers with JUND under oxidizing conditions (By similarity).

By similarity1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
199727, 2 interactors

Database of interacting proteins

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DIPi
DIP-1067N

Protein interaction database and analysis system

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IntActi
P13346, 1 interactor

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000003640

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
P13346, 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

3D structure databases

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

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SMRi
P13346

Database of comparative protein structure models

More...
ModBasei
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%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>Domaini155 – 218bZIPPROSITE-ProRule annotationAdd BLAST64

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>Regioni1 – 54DisorderedSequence analysisAdd BLAST54
Regioni80 – 179DisorderedSequence analysisAdd BLAST100
Regioni157 – 182Basic motifPROSITE-ProRule annotationAdd BLAST26
Regioni183 – 211Leucine-zipperPROSITE-ProRule annotationAdd BLAST29
Regioni222 – 276DisorderedSequence analysisAdd BLAST55
Regioni316 – 338DisorderedSequence analysisAdd BLAST23

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 type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi10 – 38Polar residuesSequence analysisAdd BLAST29
Compositional biasi103 – 134Polar residuesSequence analysisAdd BLAST32
Compositional biasi140 – 163Basic and acidic residuesSequence analysisAdd BLAST24
Compositional biasi254 – 269Pro residuesSequence analysisAdd BLAST16

<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

Binds DNA via bZIP domain; DNA-binding is under control of cellular redox homeostasis (in vitro) (By similarity). To enable DNA binding, the bZIP domain must undergo a conformational rearrangement which requires the reduction of the interchain disulfide bond between FosB and JunD (in vitro) (By similarity). The bZIP domain is able to form homomeric oligomers via formation of interchain disulfide bonds under non-reducing conditions (in vitro) (By similarity). Under reducing conditions, the disulfide-bonded homomeric species dissociates into monomers (in vitro) (By similarity).By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the bZIP family. Fos subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1414, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000160358

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_049742_0_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P13346

Identification of Orthologs from Complete Genome Data

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OMAi
QGMMQEV

Database of Orthologous Groups

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OrthoDBi
1221590at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P13346

TreeFam database of animal gene trees

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TreeFami
TF326301

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR000837, AP-1
IPR004827, bZIP
IPR029813, FosB

The PANTHER Classification System

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PANTHERi
PTHR23351, PTHR23351, 1 hit
PTHR23351:SF3, PTHR23351:SF3, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00170, bZIP_1, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00042, LEUZIPPRFOS

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00338, BRLZ, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50217, BZIP, 1 hit
PS00036, BZIP_BASIC, 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 (2+)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.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P13346-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><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
MFQAFPGDYD SGSRCSSSPS AESQYLSSVD SFGSPPTAAA SQECAGLGEM
60 70 80 90 100
PGSFVPTVTA ITTSQDLQWL VQPTLISSMA QSQGQPLASQ PPAVDPYDMP
110 120 130 140 150
GTSYSTPGLS AYSTGGASGS GGPSTSTTTS GPVSARPARA RPRRPREETL
160 170 180 190 200
TPEEEEKRRV RRERNKLAAA KCRNRRRELT DRLQAETDQL EEEKAELESE
210 220 230 240 250
IAELQKEKER LEFVLVAHKP GCKIPYEEGP GPGPLAEVRD LPGSTSAKED
260 270 280 290 300
GFGWLLPPPP PPPLPFQSSR DAPPNLTASL FTHSEVQVLG DPFPVVSPSY
310 320 330
TSSFVLTCPE VSAFAGAQRT SGSEQPSDPL NSPSLLAL
Length:338
Mass (Da):35,977
Last modified:January 1, 1990 - 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:iE9D031A4BEAE48EC
GO
Isoform 2 (identifier: P13346-2) [UniParc]FASTAAdd to basket
Also known as: deltaFosB1 Publication, FosB21 Publication, FosB[short form]1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     238-338: Missing.

Show »
Length:237
Mass (Da):25,435
Checksum:i5A169B83CD088E9F
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
A0A140LHW0A0A140LHW0_MOUSE
Protein fosB
Fosb
299Annotation 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>
A0A140LHS3A0A140LHS3_MOUSE
Protein fosB
Fosb
201Annotation 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>
A0A140LJH0A0A140LJH0_MOUSE
Protein fosB
Fosb
302Annotation 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>
A0A140LIT4A0A140LIT4_MOUSE
Protein fosB
Fosb
263Annotation 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>

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_061375238 – 338Missing in isoform 2. Add BLAST101

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
X14897 mRNA Translation: CAA33026.1
AF093624 Genomic DNA Translation: AAD13196.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS20897.1

Protein sequence database of the Protein Information Resource

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PIRi
S35477, TVMSFB

NCBI Reference Sequences

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RefSeqi
NP_032062.1, NM_008036.2
XP_006539606.1, XM_006539543.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000003640; ENSMUSP00000003640; ENSMUSG00000003545

Database of genes from NCBI RefSeq genomes

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GeneIDi
14282

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:14282

UCSC genome browser

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UCSCi
uc009flk.1, mouse

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
X14897 mRNA Translation: CAA33026.1
AF093624 Genomic DNA Translation: AAD13196.1
CCDSiCCDS20897.1
PIRiS35477, TVMSFB
RefSeqiNP_032062.1, NM_008036.2
XP_006539606.1, XM_006539543.2

3D structure databases

SMRiP13346
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi199727, 2 interactors
DIPiDIP-1067N
IntActiP13346, 1 interactor
STRINGi10090.ENSMUSP00000003640

PTM databases

iPTMnetiP13346
PhosphoSitePlusiP13346

Proteomic databases

MaxQBiP13346
PaxDbiP13346
PRIDEiP13346
ProteomicsDBi271710

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
4139, 542 antibodies from 39 providers

The DNASU plasmid repository

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DNASUi
14282

Genome annotation databases

EnsembliENSMUST00000003640; ENSMUSP00000003640; ENSMUSG00000003545
GeneIDi14282
KEGGimmu:14282
UCSCiuc009flk.1, mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
2354
MGIiMGI:95575, Fosb
VEuPathDBiHostDB:ENSMUSG00000003545

Phylogenomic databases

eggNOGiKOG1414, Eukaryota
GeneTreeiENSGT00940000160358
HOGENOMiCLU_049742_0_0_1
InParanoidiP13346
OMAiQGMMQEV
OrthoDBi1221590at2759
PhylomeDBiP13346
TreeFamiTF326301

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
14282, 0 hits in 64 CRISPR screens

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

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ChiTaRSi
Fosb, mouse

Protein Ontology

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PROi
PR:P13346
RNActiP13346, protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000003545, Expressed in islet of Langerhans and 126 other tissues
GenevisibleiP13346, MM

Family and domain databases

InterProiView protein in InterPro
IPR000837, AP-1
IPR004827, bZIP
IPR029813, FosB
PANTHERiPTHR23351, PTHR23351, 1 hit
PTHR23351:SF3, PTHR23351:SF3, 1 hit
PfamiView protein in Pfam
PF00170, bZIP_1, 1 hit
PRINTSiPR00042, LEUZIPPRFOS
SMARTiView protein in SMART
SM00338, BRLZ, 1 hit
PROSITEiView protein in PROSITE
PS50217, BZIP, 1 hit
PS00036, BZIP_BASIC, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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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 nameiFOSB_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: P13346
Secondary accession number(s): A0A140LIE4
<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: January 1, 1990
Last sequence update: January 1, 1990
Last modified: February 23, 2022
This is version 163 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

Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families
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