[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0092-8674(83)90306-9; PubMed=6301687 [NCBI, ExPASy, EBI, Israel, Japan] van Beveren C., van Straaten F., Curran T., Mueller R., Verma I.M.; "Analysis of FBJ-MuSV provirus and c-fos (mouse) gene reveals that viral and cellular fos gene products have different carboxy termini."; Cell 32:1241-1255(1983).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1073/pnas.82.15.4987; PubMed=2991903 [NCBI, ExPASy, EBI, Israel, Japan] Meijlink F., Curran T., Miller A.D., Verma I.M.; "Removal of a 67-base-pair sequence in the noncoding region of protooncogene fos converts it to a transforming gene."; Proc. Natl. Acad. Sci. U.S.A. 82:4987-4991(1985).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=FVB/N; TISSUE=Mammary gland; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	INTERACTION WITH DSIPI. DOI=10.1074/jbc.M101522200; PubMed=11397794 [NCBI, ExPASy, EBI, Israel, Japan] Mittelstadt P.R., Ashwell J.D.; "Inhibition of AP-1 by the glucocorticoid-inducible protein GILZ."; J. Biol. Chem. 276:29603-29610(2001).
[5]	PHOSPHORYLATION AT THR-325; THR-331; SER-362 AND SER-374, FUNCTION, AND MUTAGENESIS OF THR-325; THR-331; PHE-343; TYR-345; SER-362 AND SER-374. PubMed=12134156 [NCBI, ExPASy, EBI, Israel, Japan] Murphy L.O., Smith S., Chen R.H., Fingar D.C., Blenis J.; "Molecular interpretation of ERK signal duration by immediate early gene products."; Nat. Cell Biol. 4:556-564(2002).
[6]	PHOSPHORYLATION AT THR-232; THR-325; THR-331; SER-362 AND SER-374, FUNCTION, AND MUTAGENESIS OF THR-232; THR-325; THR-331 AND SER-374. DOI=10.1128/MCB.23.19.7030-7043.2003; PubMed=12972619 [NCBI, ExPASy, EBI, Israel, Japan] Monje P., Marinissen M.J., Gutkind J.S.; "Phosphorylation of the carboxyl-terminal transactivation domain of c-Fos by extracellular signal-regulated kinase mediates the transcriptional activation of AP-1 and cellular transformation induced by platelet-derived growth factor."; Mol. Cell. Biol. 23:7030-7043(2003).
[7]	PHOSPHORYLATION AT SER-362, AND FUNCTION. PubMed=15719069 [NCBI, ExPASy, EBI, Israel, Japan] David J.-P., Mehic D., Bakiri L., Schilling A.F., Mandic V., Priemel M., Idarraga M.H., Reschke M.O., Hoffmann O., Amling M., Wagner E.F.; "Essential role of RSK2 in c-Fos-dependent osteosarcoma development."; J. Clin. Invest. 115:664-672(2005).

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. Interacts with MAFB (By similarity).
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

V00727; CAA24105.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J00370; AAA96699.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC029814; AAH29814.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00131985; -.

A01343; TVMSF.

NP_034364.1; -.

3D structure databases

HSSP

P01100; 1FOS. [HSSP ENTRY / PDB]

SMR

P01101; 139-198.

ModBase

P01101.

Protein-protein interaction databases

DIP

DIP:1066N; -.

PTM databases

PhosphoSite

P01101; -.

Organism-specific databases

MGI

MGI:95574; Fos.

Gene expression databases

P01101; -.

P01101; -.

MM_FOS; -.

ENSMUSG00000021250; Mus musculus.

Ontologies

GO:0005667;	Cellular component: transcription factor complex (inferred from direct assay from MGI).
GO:0043565;	Molecular function: sequence-specific DNA binding (inferred from electronic annotation from InterPro).
GO:0003700;	Molecular function: transcription factor activity (inferred from direct assay from MGI).
GO:0031668;	Biological process: cellular response to extracellular stimulus (inferred from mutant phenotype from MGI).
GO:0007399;	Biological process: nervous system development (inferred from mutant phenotype from MGI).
GO:0045944;	Biological process: positive regulation of transcription from RNA polymerase II promoter (inferred from mutant phenotype from MGI).
GO:0042493;	Biological process: response to drug (inferred from direct assay from MGI).
GO:0051789;	Biological process: response to protein stimulus (inferred from direct assay from MGI).
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).

Proteomic databases

PRIDE

P01101; -.

Genome annotation databases

Ensembl

ENSMUSG00000021250; Mus musculus. [Contig view]

GeneID

14281; -.

KEGG

mmu:14281; -.

Phylogenomic databases

HOGENOM

P01101; -.

HOVERGEN

P01101; -.

OMA

P01101; TYTSSFV.

Other

285657; -.

Fos; Mus musculus.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Proto-oncogene; Ubl conjugation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 380`	`380`	`Proto-oncogene protein c-fos.`	`PRO_0000076467`
`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: No effect on PDGF-stimulated enhancement of transcriptional activity. Completely abolishes PDGF-stimulated enhancement of transcriptional activity; when associated with A-325; A-331 and A-374.`
`MUTAGEN`	`325 325`		`T->A: Almost no EGF-mediated phosphorylation, greatly reduced cellular transformation, and reduced AP1 activity by 20%; when associated with A-331. No effect on PDGF-stimulated enhancement of transcriptional activity. Completely abolishes PDGF-stimulated enhancement of transcriptional activity; when associated with A-232; A-331 and A-374.`
`MUTAGEN`	`331 331`		`T->A: Almost no EGF-mediated phosphorylation, greatly reduced cellular transformation, and reduced AP1 activity by 20%; when associated with A-325. No effect on PDGF-stimulated enhancement of transcriptional activity. Completely abolishes PDGF-stimulated enhancement of transcriptional activity; when associated with A-232; A-325;and A-374.`
`MUTAGEN`	`343 343`		`F->A: Reduced phosphorylation by ERK. Reduced AP1 activity by 65%.`
`MUTAGEN`	`345 345`		`Y->A: Reduced phosphorylation by ERK.`
`MUTAGEN`	`362 362`		`S->D: Enhanced EGF- and RSK-mediated tranformation; when associated with D-374.`
`MUTAGEN`	`362 362`		`S->E: Increased enhancement of EGF- and RSK-mediated tranformation; when associated with E-374.`
`MUTAGEN`	`374 374`		`S->A: No effect on PDGF-stimulated enhancement of transcriptional activity. Completely abolishes PDGF-stimulated enhancement of transcriptional activity; when associated with A-232; A-325 and A-331.`
`MUTAGEN`	`374 374`		`S->D: Enhanced EGF- and RSK-mediated tranformation; when associated with D-362.`
`MUTAGEN`	`374 374`		`S->E: Increased enhanced EGF- and RSK-mediated tranformation; when associated with E-362.`

Sequence information

Length: 380 AA [This is the length of the unprocessed precursor]

Molecular weight: 40838 Da [This is the MW of the unprocessed precursor]

CRC64: 475966265952B624 [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 QSAGAYARAG MVKTVSGGRA 

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

       190        200        210        220        230        240 
TEIANLLKEK EKLEFILAAH RPACKIPDDL GFPEEMSVAS LDLTGGLPEA STPESEEAFT 

       250        260        270        280        290        300 
LPLLNDPEPK PSLEPVKSIS NVELKAEPFD DFLFPASSRP SGSETSRSVP DVDLSGSFYA 

       310        320        330        340        350        360 
ADWEPLHSNS LGMGPMVTEL EPLCTPVVTC TPGCTTYTSS FVFTYPEADS FPSCAAAHRK 

       370        380 
GSSSNEPSSD SLSSPTLLAL

P01101 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools