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UniProtKB/Swiss-Prot entry P12841


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FOS_RAT
Primary accession number P12841
Secondary accession number Q4FDN1
Integrated into Swiss-Prot on October 1, 1989
Sequence was last modified on October 1, 1989 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 77)
Name and origin of the protein
Protein name Proto-oncogene protein c-fos
Synonym Cellular oncogene fos
Gene name
Name: Fos
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3325886 [NCBI, ExPASy, EBI, Israel, Japan]
Curran T., Gordon M.B., Rubino K.L., Sambucetti L.C.;
"Isolation and characterization of the c-fos(rat) cDNA and analysis of post-translational modification in vitro.";
Oncogene 2:79-84(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Sprague-Dawley;
TISSUE=Liver;
Weiler E.;
"cFOS expression in rat.";
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
[3]
DNA-BINDING.
DOI=10.1073/pnas.87.3.1032; PubMed=2105492 [NCBI, ExPASy, EBI, Israel, Japan]
Abate C., Luk D., Gentz R., Rauscher F.J. III, Curran T.;
"Expression and purification of the leucine zipper and DNA-binding domains of Fos and Jun: both Fos and Jun contact DNA directly.";
Proc. Natl. Acad. Sci. U.S.A. 87:1032-1036(1990).
[4]
INTERACTION WITH MAFB.
DOI=10.1006/bbrc.1998.8447; PubMed=9571165 [NCBI, ExPASy, EBI, Israel, Japan]
Matsushima-Hibiya Y., Nishi S., Sakai M.;
"Rat maf-related factors: the specificities of DNA binding and heterodimer formation.";
Biochem. Biophys. Res. Commun. 245:412-418(1998).
[5]
PHOSPHORYLATION AT THR-232, FUNCTION, AND MUTAGENESIS OF THR-232.
DOI=10.1093/nar/22.24.5173; PubMed=7816602 [NCBI, ExPASy, EBI, Israel, Japan]
Bannister A.J., Brown H.J., Sutherland J.A., Kouzarides T.;
"Phosphorylation of the c-Fos and c-Jun HOB1 motif stimulates its activation capacity.";
Nucleic Acids Res. 22:5173-5176(1994).
[6]
PHOSPHORYLATION AT THR-325; THR-331; SER-362 AND SER-374, FUNCTION, AND MUTAGENESIS OF THR-325; THR-331; 343-PHE--TYR-345; SER-362 AND SER-374.
DOI=10.1111/j.1471-4159.2006.04250.x; PubMed=17223854 [NCBI, ExPASy, EBI, Israel, Japan]
Pellegrino M.J., Stork P.J.;
"Sustained activation of extracellular signal-regulated kinase by nerve growth factor regulates c-fos protein stabilization and transactivation in PC12 cells.";
J. Neurochem. 99:1480-1493(2006).
Comments
  • FUNCTION: Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. Has a critical function in regulating the development of cells destined to form and maintain the skeleton. It is thought to have an important role in signal transduction, cell proliferation and differentiation.
  • SUBUNIT: Heterodimer. Interacts with DSIPI; this interaction inhibits the binding of active AP1 to its target DNA (By similarity). Interacts with MAFB.
  • SUBCELLULAR LOCATION: Nucleus.
  • PTM: Phosphorylated in the C-terminal upon stimulation by nerve growth factor (NGF) and epidermal growth factor (EGF). Phosphorylated, in vitro, by MAPK and RSK1. Phosphorylation on both Ser-362 and Ser-374 by MAPK1/2 and RSK1/2 leads to protein stabilization with phosphorylation on Ser-374 being the major site for protein stabilization on NGF stimulation. Phosphorylation on Ser-362 and Ser-374 primes further phosphorylations on Thr-325 and Thr-331 through promoting docking of MAPK to the DEF domain. Phosphorylation on Thr-232, induced by HA-RAS, activates the transcriptional activity and antagonizes sumoylation. Phosphorylation on Ser-362 by RSK2 in osteoblasts contributes to osteoblast transformation (By similarity).
  • PTM: Constitutively sumoylated by SUMO1, SUMO2 and SUMO3. Desumoylated by SENP2. Sumoylation requires heterodimerization with JUN and is enhanced by mitogen stimulation. Sumoylation inhibits the AP-1 transcriptional activity and is, itself, inhibited by Ras-activated phosphorylation on Thr-232 (By similarity).
  • SIMILARITY: Belongs to the bZIP family. Fos subfamily.
  • SIMILARITY: Contains 1 bZIP domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X06769; CAA29937.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ089699; AAZ13764.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00368000; -.
PIR A28263; TVRTFS.
RefSeq NP_071533.1; -.
UniGene Rn.103750
3D structure databases
HSSP P01100; 1FOS. [HSSP ENTRY / PDB]
SMR P12841; 139-198.
ModBase P12841.
Protein-protein interaction databases
DIP DIP:6001N; -.
PTM databases
PhosphoSite P12841; -.
Organism-specific databases
RGD 2626; Fos.
Gene expression databases
ArrayExpress P12841; -.
GermOnline ENSRNOG00000008015; Rattus norvegicus.
Ontologies
GO
GO:0019717; Cellular component: synaptosome (inferred from direct assay from RGD).
GO:0003690; Molecular function: double-stranded DNA binding (inferred from direct assay from RGD).
GO:0046982; Molecular function: protein heterodimerization activity (inferred from direct assay from RGD).
GO:0043565; Molecular function: sequence-specific DNA binding (inferred from direct assay from RGD).
GO:0003700; Molecular function: transcription factor activity (inferred from mutant phenotype from RGD).
GO:0007568; Biological process: aging (inferred from expression pattern from RGD).
GO:0032870; Biological process: cellular response to hormone stimulus (inferred from expression pattern from RGD).
GO:0001661; Biological process: conditioned taste aversion (inferred from expression pattern from RGD).
GO:0007565; Biological process: female pregnancy (inferred from expression pattern from RGD).
GO:0051591; Biological process: response to cAMP (inferred from expression pattern from RGD).
GO:0009409; Biological process: response to cold (inferred from expression pattern from RGD).
GO:0051412; Biological process: response to corticosterone stimulus (inferred from expression pattern from RGD).
GO:0034097; Biological process: response to cytokine stimulus (inferred from expression pattern from RGD).
GO:0042493; Biological process: response to drug (inferred from expression pattern from RGD).
GO:0009629; Biological process: response to gravity (inferred from expression pattern from RGD).
GO:0009416; Biological process: response to light stimulus (inferred from expression pattern from RGD).
GO:0032496; Biological process: response to lipopolysaccharide (inferred from expression pattern from RGD).
GO:0009612; Biological process: response to mechanical stimulus (inferred from expression pattern from RGD).
GO:0014070; Biological process: response to organic cyclic substance (inferred from expression pattern from RGD).
GO:0032570; Biological process: response to progesterone stimulus (inferred from expression pattern from RGD).
GO:0009636; Biological process: response to toxin (inferred from expression pattern from RGD).
GO:0030431; Biological process: sleep (inferred from expression pattern from RGD).
GO:0006366; Biological process: transcription from RNA polymerase II promoter (inferred from mutant phenotype from RGD).
QuickGo view.
Family and domain databases
InterPro IPR011616; bZIP_1.
IPR000837; Leuzip_Fos.
IPR004827; TF_bZIP.
Graphical view of domain structure.
Pfam PF00170; bZIP_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00042; LEUZIPPRFOS.
SMART SM00338; BRLZ; 1.
SMART graphical view of domain structure.
PROSITE PS50217; BZIP; 1.
PS00036; BZIP_BASIC; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
Ensembl ENSRNOG00000008015; Rattus norvegicus. [Contig view]
GeneID 314322; -.
KEGG rno:314322; -.
Phylogenomic databases
HOVERGEN P12841; -.
OMA P12841; TYTSSFV.
Other
NextBio 667476; -.
ProtoNet P12841.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Proto-oncogene; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   380  380     Proto-oncogene protein c-fos. PRO_0000076469
DOMAIN   165   193  29     Leucine-zipper. 
DNA_BIND   139   160  22     Basic motif. 
MOD_RES   232   232        Phosphothreonine. 
MOD_RES   325   325        Phosphothreonine. 
MOD_RES   331   331        Phosphothreonine. 
MOD_RES   362   362        Phosphoserine; by MAPK and RPS6KA3. 
MOD_RES   374   374        Phosphoserine; by MAPK. 
CROSSLNK   113   113        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) (By similarity). 
CROSSLNK   265   265        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) (By similarity). 
MUTAGEN   232   232        T->A: Abolishes HA-RAS-mediated activation. Loss of in vitro ERK2-mediated phosphorylation. No change in sumoylation levels. 
MUTAGEN   325   325        T->A: Loss of NGF-mediated phosphorylation; when associated with A-331. 
MUTAGEN   331   331        T->A: Loss of NGF-mediated phosphorylation; when associated with A-325. 
MUTAGEN   343   345        FTY->ATA: Decreased phosphorylation levels. Reduced NGF-mediated enhanced transactivation. 
MUTAGEN   362   362        S->A: Some loss of protein stabilization on NGF-treatment; when associated with D-374. 
MUTAGEN   362   362        S->D: Increased protein stabilization on NGF-treatment, but no increase when treated with MAPK-inhibitor; when associated with D-374. 
MUTAGEN   374   374        S->A: Greatly reduced protein stabilization on NGF stimulation. 
MUTAGEN   374   374        S->D: Increased protein stabilization on NGF-treatment, but no increase when treated with MAPK-inhibitor; when associated with D-362. Some loss of protein stablization on NGF-treatment; wnen associated with A-362. 
Sequence information
Length: 380 AA [This is the length of the unprocessed precursor] Molecular weight: 40927 Da [This is the MW of the unprocessed precursor] CRC64: E62D16A88CB2BEE9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MMFSGFNADY EASSSRCSSA SPAGDSLSYY HSPADSFSSM GSPVNTQDFC ADLSVSSANF 

        70         80         90        100        110        120 
IPTVTAISTS PDLQWLVQPT LVSSVAPSQT RAPHPYGLPT PSTGAYARAG VVKTMSGGRA 

       130        140        150        160        170        180 
QSIGRRGKVE QLSPEEEEKR RIRRERNKMA AAKCRNRRRE LTDTLQAETD QLEDEKSALQ 

       190        200        210        220        230        240 
TEIANLLKEK EKLEFILAAH RPACKIPNDL GFPEEMSVTS LDLTGGLPEA TTPESEEAFT 

       250        260        270        280        290        300 
LPLLNDPEPK PSLEPVKNIS NMELKAEPFD DFLFPASSRP SGSETARSVP DVDLSGSFYA 

       310        320        330        340        350        360 
ADWEPLHSSS LGMGPMVTEL EPLCTPVVTC TPSCTTYTSS FVFTYPEADS FPSCAAAHRK 

       370        380 
GSSSNEPSSD SLSSPTLLAL 

P12841 in FASTA format

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