P53539 · FOSB_HUMAN
- ProteinProtein FosB
- GeneFOSB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids338 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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).
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
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein FosB
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP53539
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_022286 | 33 | in dbSNP:rs28381241 | |||
Sequence: G → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 355 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data), disulfide bond.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000076476 | 1-338 | UniProt | Protein FosB | |||
Sequence: MFQAFPGDYDSGSRCSSSPSAESQYLSSVDSFGSPPTAAASQECAGLGEMPGSFVPTVTAITTSQDLQWLVQPTLISSMAQSQGQPLASQPPVVDPYDMPGTSYSTPGMSGYSSGGASGSGGPSTSGTTSGPGPARPARARPRRPREETLTPEEEEKRRVRRERNKLAAAKCRNRRRELTDRLQAETDQLEEEKAELESEIAELQKEKERLEFVLVAHKPGCKIPYEEGPGPGPLAEVRDLPGSAPAKEDGFSWLLPPPPPPPLPFQTSQDAPPNLTASLFTHSEVQVLGDPFPVVNPSYTSSFVLTCPEVSAFAGAQRTSGSDQPSDPLNSPSLLAL | |||||||
Modified residue | 27 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 151 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Disulfide bond | 172 | UniProt | Interchain (with C-285 in JUND) | ||||
Sequence: C |
Post-translational modification
Phosphorylated.
Isoform 11
Phosphorylated at Ser-27 by CSNK2A1; phosphorylation increases protein stability and transactivation potential.
Keywords
- PTM
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).
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).
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
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-54 | Disordered | ||||
Sequence: MFQAFPGDYDSGSRCSSSPSAESQYLSSVDSFGSPPTAAASQECAGLGEMPGSF | ||||||
Compositional bias | 10-38 | Polar residues | ||||
Sequence: DSGSRCSSSPSAESQYLSSVDSFGSPPTA | ||||||
Region | 79-191 | Disordered | ||||
Sequence: MAQSQGQPLASQPPVVDPYDMPGTSYSTPGMSGYSSGGASGSGGPSTSGTTSGPGPARPARARPRRPREETLTPEEEEKRRVRRERNKLAAAKCRNRRRELTDRLQAETDQLE | ||||||
Compositional bias | 103-132 | Polar residues | ||||
Sequence: SYSTPGMSGYSSGGASGSGGPSTSGTTSGP | ||||||
Compositional bias | 140-163 | Basic and acidic residues | ||||
Sequence: ARPRRPREETLTPEEEEKRRVRRE | ||||||
Domain | 155-218 | bZIP | ||||
Sequence: EEKRRVRRERNKLAAAKCRNRRRELTDRLQAETDQLEEEKAELESEIAELQKEKERLEFVLVAH | ||||||
Region | 157-182 | Basic motif | ||||
Sequence: KRRVRRERNKLAAAKCRNRRRELTDR | ||||||
Compositional bias | 172-190 | Basic and acidic residues | ||||
Sequence: CRNRRRELTDRLQAETDQL | ||||||
Region | 183-211 | Leucine-zipper | ||||
Sequence: LQAETDQLEEEKAELESEIAELQKEKERL | ||||||
Region | 222-276 | Disordered | ||||
Sequence: CKIPYEEGPGPGPLAEVRDLPGSAPAKEDGFSWLLPPPPPPPLPFQTSQDAPPNL | ||||||
Compositional bias | 253-269 | Pro residues | ||||
Sequence: SWLLPPPPPPPLPFQTS | ||||||
Region | 316-338 | Disordered | ||||
Sequence: GAQRTSGSDQPSDPLNSPSLLAL |
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).
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 statusComplete
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.
- Name1
- SynonymsFosB-L
- Length338
- Mass (Da)35,928
- Last updated1996-10-01 v1
- ChecksumDDFF827C5047850F
P53539-2
- Name2
- Differences from canonical
- 150-185: Missing
P53539-3
- Name3
- Differences from canonical
- 42-80: Missing
P53539-4
- Name4
- Differences from canonical
- 238-284: Missing
P53539-5
- Name5
P53539-6
- Name6
P53539-7
- Name7
P53539-8
- Name8
- Differences from canonical
- 43-185: Missing
P53539-9
- Name9
P53539-10
- Name10
- Differences from canonical
- 1-49: Missing
P53539-11
- Name11
- SynonymsdeltaFosB
- Differences from canonical
- 238-338: Missing
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_055562 | 1-49 | in isoform 10 | |||
Sequence: Missing | ||||||
Compositional bias | 10-38 | Polar residues | ||||
Sequence: DSGSRCSSSPSAESQYLSSVDSFGSPPTA | ||||||
Alternative sequence | VSP_055563 | 42-80 | in isoform 3, isoform 5 and isoform 7 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_055564 | 43-185 | in isoform 8 and isoform 9 | |||
Sequence: Missing | ||||||
Compositional bias | 103-132 | Polar residues | ||||
Sequence: SYSTPGMSGYSSGGASGSGGPSTSGTTSGP | ||||||
Compositional bias | 140-163 | Basic and acidic residues | ||||
Sequence: ARPRRPREETLTPEEEEKRRVRRE | ||||||
Alternative sequence | VSP_046167 | 150-185 | in isoform 2, isoform 5 and isoform 6 | |||
Sequence: Missing | ||||||
Compositional bias | 172-190 | Basic and acidic residues | ||||
Sequence: CRNRRRELTDRLQAETDQL | ||||||
Alternative sequence | VSP_055565 | 238-284 | in isoform 4, isoform 6, isoform 7 and isoform 9 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_061374 | 238-338 | in isoform 11 | |||
Sequence: Missing | ||||||
Compositional bias | 253-269 | Pro residues | ||||
Sequence: SWLLPPPPPPPLPFQTS | ||||||
Sequence conflict | 338 | in Ref. 2; AAB53946 and 3; ABW34730/ABW34731/ABW34732/ABW34733/ABW34734/ABW34735/ABW34736/ABW34737 | ||||
Sequence: L → R |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |