P53539 · FOSB_HUMAN

  • Protein
    Protein FosB
  • Gene
    FOSB
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

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:12618758, PubMed:28981703).
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 (By similarity).
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 (PubMed:12618758).
Exhibits transactivation activity in vitro (By similarity).
Involved in the display of nurturing behavior towards newborns (By similarity).
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 (By similarity).
Implicated in behavioral responses related to morphine reward and spatial memory (By similarity).

Isoform 11

Exhibits lower transactivation activity than isoform 1 in vitro (By similarity).
The heterodimer with JUN does not display any transcriptional activity, and may thereby act as an transcriptional inhibitor (By similarity).
May be involved in the regulation of neurogenesis in the hippocampus (By similarity).
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 (By similarity).
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 (By similarity).

GO annotations

AspectTerm
Cellular Componentchromatin
Cellular Componentcytosol
Cellular Componentintracellular membrane-bounded organelle
Cellular Componentnucleoplasm
Cellular Componentnucleus
Molecular FunctionDNA binding
Molecular FunctionDNA-binding transcription activator activity, RNA polymerase II-specific
Molecular FunctionDNA-binding transcription factor activity, RNA polymerase II-specific
Molecular FunctionRNA polymerase II cis-regulatory region sequence-specific DNA binding
Molecular Functionsequence-specific double-stranded DNA binding
Biological Processbehavioral response to cocaine
Biological Processcellular response to calcium ion
Biological Processcellular response to hormone stimulus
Biological Processfemale pregnancy
Biological Processnegative regulation of transcription by RNA polymerase II
Biological Processregulation of transcription by RNA polymerase II
Biological Processresponse to amphetamine
Biological Processresponse to cAMP
Biological Processresponse to corticosterone
Biological Processresponse to ethanol
Biological Processresponse to mechanical stimulus
Biological Processresponse to morphine
Biological Processresponse to progesterone
Biological Processresponse to xenobiotic stimulus
Biological Processtranscription by RNA polymerase II

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein FosB
  • Alternative names
    • FosB proto-oncogene, AP-1 transcription factor subunit
    • G0/G1 switch regulatory protein 3
    • Transcription factor AP-1 subunit FosB

Gene names

    • Name
      FOSB
    • Synonyms
      G0S3

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    P53539
  • Secondary accessions
    • A8K9K5
    • A8VJE1
    • A8VJE6
    • A8VJF0
    • A8VJF3

Proteomes

Organism-specific databases

Subcellular Location

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_02228633in dbSNP:rs28381241

Variants

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The viewer provides 355 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue, modified residue (large scale data), disulfide bond.

TypeIDPosition(s)SourceDescription
ChainPRO_00000764761-338UniProtProtein FosB
Modified residue27UniProtPhosphoserine
Modified residue (large scale data)151PRIDEPhosphothreonine
Disulfide bond172UniProtInterchain (with C-285 in JUND)

Post-translational modification

Phosphorylated.

Isoform 11

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

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Isoform 11

Expressed in the nucleus accumbens of the striatum (at protein level).

Gene expression databases

Organism-specific databases

Interaction

Subunit

Heterodimer; binds to DNA as heterodimer (PubMed:28981703).
Component of an AP-1 transcription factor complex; composed of FOS-JUN heterodimers (By similarity).
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:28981703).
Interacts with the BAF multiprotein chromatin-remodeling complex subunits SMARCB1 and SMARCD1 (By similarity).
Interacts with ARID1A and JUN (By similarity).

Isoform 11

Homodimer under oxidizing conditions and monomer under reducing conditions (in vitro) (PubMed:32542236).
Heterodimer; binds to DNA as heterodimer (By similarity).
Forms heterodimers with JUNB, JUN or JUND; thereby binding to the AP-1 consensus sequence but does not stimulate transcription (By similarity).
Forms heterodimers with JUND under oxidizing conditions (PubMed:32542236).

Binary interactions

Protein-protein interaction databases

Chemistry

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-54Disordered
Compositional bias10-38Polar residues
Region79-191Disordered
Compositional bias103-132Polar residues
Compositional bias140-163Basic and acidic residues
Domain155-218bZIP
Region157-182Basic motif
Compositional bias172-190Basic and acidic residues
Region183-211Leucine-zipper
Region222-276Disordered
Compositional bias253-269Pro residues
Region316-338Disordered

Domain

Binds DNA via bZIP domain; DNA-binding is under control of cellular redox homeostasis (in vitro) (PubMed:28981703).
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) (PubMed:28981703).
The bZIP domain is able to form homomeric oligomers via formation of interchain disulfide bonds under non-reducing conditions (in vitro) (PubMed:32542236).
Under reducing conditions, the disulfide-bonded homomeric species dissociates into monomers (in vitro) (PubMed:32542236).

Sequence similarities

Belongs to the bZIP family. Fos subfamily.

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

  • Sequence status
    Complete

This entry describes 11 isoforms produced by Alternative splicing.

P53539-1

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

  • Name
    1
  • Synonyms
    FosB-L
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    338
  • Mass (Da)
    35,928
  • Last updated
    1996-10-01 v1
  • Checksum
    DDFF827C5047850F
MFQAFPGDYDSGSRCSSSPSAESQYLSSVDSFGSPPTAAASQECAGLGEMPGSFVPTVTAITTSQDLQWLVQPTLISSMAQSQGQPLASQPPVVDPYDMPGTSYSTPGMSGYSSGGASGSGGPSTSGTTSGPGPARPARARPRRPREETLTPEEEEKRRVRRERNKLAAAKCRNRRRELTDRLQAETDQLEEEKAELESEIAELQKEKERLEFVLVAHKPGCKIPYEEGPGPGPLAEVRDLPGSAPAKEDGFSWLLPPPPPPPLPFQTSQDAPPNLTASLFTHSEVQVLGDPFPVVNPSYTSSFVLTCPEVSAFAGAQRTSGSDQPSDPLNSPSLLAL

P53539-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P53539-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P53539-4

  • Name
    4
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P53539-5

  • Name
    5
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P53539-6

P53539-7

  • Name
    7
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P53539-8

  • Name
    8
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P53539-9

P53539-10

  • Name
    10
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P53539-11

  • Name
    11
  • Synonyms
    deltaFosB
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
K7EJ89K7EJ89_HUMANFOSB177
K7EKA0K7EKA0_HUMANFOSB137
K7ERZ8K7ERZ8_HUMANFOSB188

Features

Showing features for alternative sequence, compositional bias, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_0555621-49in isoform 10
Compositional bias10-38Polar residues
Alternative sequenceVSP_05556342-80in isoform 3, isoform 5 and isoform 7
Alternative sequenceVSP_05556443-185in isoform 8 and isoform 9
Compositional bias103-132Polar residues
Compositional bias140-163Basic and acidic residues
Alternative sequenceVSP_046167150-185in isoform 2, isoform 5 and isoform 6
Compositional bias172-190Basic and acidic residues
Alternative sequenceVSP_055565238-284in isoform 4, isoform 6, isoform 7 and isoform 9
Alternative sequenceVSP_061374238-338in isoform 11
Compositional bias253-269Pro residues
Sequence conflict338in Ref. 2; AAB53946 and 3; ABW34730/ABW34731/ABW34732/ABW34733/ABW34734/ABW34735/ABW34736/ABW34737

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L49169
EMBL· GenBank· DDBJ
AAB53946.1
EMBL· GenBank· DDBJ
mRNA
EU178109
EMBL· GenBank· DDBJ
ABW34730.1
EMBL· GenBank· DDBJ
mRNA
EU178110
EMBL· GenBank· DDBJ
ABW34731.1
EMBL· GenBank· DDBJ
mRNA
EU178111
EMBL· GenBank· DDBJ
ABW34732.1
EMBL· GenBank· DDBJ
mRNA
EU178112
EMBL· GenBank· DDBJ
ABW34733.1
EMBL· GenBank· DDBJ
mRNA
EU178113
EMBL· GenBank· DDBJ
ABW34734.1
EMBL· GenBank· DDBJ
mRNA
EU178114
EMBL· GenBank· DDBJ
ABW34735.1
EMBL· GenBank· DDBJ
mRNA
EU178115
EMBL· GenBank· DDBJ
ABW34736.1
EMBL· GenBank· DDBJ
mRNA
EU178116
EMBL· GenBank· DDBJ
ABW34737.1
EMBL· GenBank· DDBJ
mRNA
AY898963
EMBL· GenBank· DDBJ
AAW65374.1
EMBL· GenBank· DDBJ
Genomic DNA
AK292720
EMBL· GenBank· DDBJ
BAF85409.1
EMBL· GenBank· DDBJ
mRNA
AC138128
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471126
EMBL· GenBank· DDBJ
EAW57351.1
EMBL· GenBank· DDBJ
Genomic DNA
BC036724
EMBL· GenBank· DDBJ
AAH36724.1
EMBL· GenBank· DDBJ
mRNA
BC040197
EMBL· GenBank· DDBJ
AAH40197.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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