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P01100 (FOS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 171. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proto-oncogene c-Fos
Alternative name(s):
Cellular oncogene fos
G0/G1 switch regulatory protein 7
Gene names
Name:FOS
Synonyms:G0S7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length380 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. In the heterodimer, FOS and JUN/AP-1 basic regions each seems to interact with symmetrical DNA half sites. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex at the AP1/SMAD-binding site to regulate TGF-beta-mediated signaling. 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. In growing cells, activates phospholipid synthesis, possibly by activating CDS1 and PI4K2A. This activity requires Tyr-dephosphorylation and association with the endoplasmic reticulum. Ref.9 Ref.10 Ref.12 Ref.15 Ref.17

Subunit structure

Heterodimer; with JUN By similarity. Interacts with MAFB By similarity. Component of the SMAD3/SMAD4/JUN/FOS complex required for syngernistic TGF-beta-mediated transcription at the AP1 promoter site. Interacts with SMAD3; the interaction is weak even on TGF-beta activation. Interacts with MAFB. Interacts with DSIPI; this interaction inhibits the binding of active AP1 to its target DNA. Interacts with CDS1 and PI4K2A By similarity. Ref.6 Ref.10

Subcellular location

Nucleus. Endoplasmic reticulum. Cytoplasmcytosol. Note: In quiescent cells, present in very small amounts in the cytosol. Following induction of cell growth, first localizes to the endoplasmic reticulum and only later to the nucleus. Localization at the endoplasmic reticulum requires dephosphorylation at Tyr-10 and Tyr-30. Ref.12 Ref.15 Ref.17

Developmental stage

Expressed at very low levels in quiescent cells. When cells are stimulated to reenter growth, they undergo 2 waves of expression, the first one peaks 7.5 minutes following FBS induction. At this stage, the protein is localized endoplasmic reticulum. The second wave of expression occurs at about 20 minutes after induction and peaks at 1 hour. At this stage, the protein becomes nuclear. Ref.15

Post-translational modification

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. Ref.9 Ref.11 Ref.15 Ref.17

Constitutively sumoylated with 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. Ref.12 Ref.14

In quiescent cells, the small amount of FOS present is phosphorylated at Tyr-10 and Tyr-30 by SRC. This Tyr-phosphorylated form is cytosolic. In growing cells, dephosphorylated by PTPN2. Dephosphorylation leads to the association with endoplasmic reticulum membranes and activation of phospholipid synthesis. Ref.9 Ref.11 Ref.15 Ref.17

Sequence similarities

Belongs to the bZIP family. Fos subfamily.

Contains 1 bZIP (basic-leucine zipper) domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Endoplasmic reticulum
Nucleus
   DiseaseProto-oncogene
   LigandDNA-binding
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA methylation

Traceable author statement PubMed 9888853. Source: ProtInc

Fc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

MyD88-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

MyD88-independent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

SMAD protein signal transduction

Inferred from direct assay Ref.10. Source: BHF-UCL

TRIF-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

aging

Inferred from electronic annotation. Source: Ensembl

cellular response to calcium ion

Inferred from electronic annotation. Source: Ensembl

cellular response to extracellular stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to hormone stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to reactive oxygen species

Inferred from direct assay PubMed 17217916. Source: BHF-UCL

conditioned taste aversion

Inferred from electronic annotation. Source: Ensembl

female pregnancy

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Traceable author statement PubMed 9443941. Source: ProtInc

innate immune response

Traceable author statement. Source: Reactome

nervous system development

Inferred from electronic annotation. Source: Ensembl

positive regulation of osteoclast differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.10. Source: BHF-UCL

regulation of sequence-specific DNA binding transcription factor activity

Traceable author statement. Source: Reactome

regulation of transcription from RNA polymerase II promoter

Traceable author statement PubMed 10918580. Source: ProtInc

response to cAMP

Inferred from electronic annotation. Source: Ensembl

response to cold

Inferred from electronic annotation. Source: Ensembl

response to corticosterone

Inferred from electronic annotation. Source: Ensembl

response to cytokine

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to gravity

Inferred from electronic annotation. Source: Ensembl

response to light stimulus

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

response to progesterone

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

skeletal muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

sleep

Inferred from electronic annotation. Source: Ensembl

stress-activated MAPK cascade

Traceable author statement. Source: Reactome

toll-like receptor 10 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 3 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 5 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 9 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR1:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR6:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Traceable author statement PubMed 10918580. Source: ProtInc

transforming growth factor beta receptor signaling pathway

Inferred from direct assay Ref.10. Source: BHF-UCL

   Cellular_componentcytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from electronic annotation. Source: Ensembl

neuron projection

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionR-SMAD binding

Inferred from physical interaction Ref.10. Source: BHF-UCL

double-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 16511568PubMed 20195357PubMed 20936779PubMed 21199371PubMed 23602568PubMed 24029232. Source: IntAct

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.10. Source: BHF-UCL

transcription regulatory region DNA binding

Inferred from direct assay Ref.10. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 380380Proto-oncogene c-Fos
PRO_0000076465

Regions

Domain137 – 20064bZIP
Region139 – 15921Basic motif; required for the activation of phospholipid synthesis, but not for CDS1-binding
Region165 – 19329Leucine-zipper By similarity

Amino acid modifications

Modified residue101Phosphotyrosine; by SRC Ref.15 Ref.17
Modified residue301Phosphotyrosine; by SRC Ref.15 Ref.17
Modified residue2321Phosphothreonine By similarity
Modified residue3251Phosphothreonine; by MAPK1 and MAPK3 Ref.11
Modified residue3311Phosphothreonine; by MAPK1 and MAPK3 Ref.11
Modified residue3621Phosphoserine; by MAPK1, MAPK3 and RPS6KA3 Ref.9
Modified residue3741Phosphoserine; by MAPK1 and MAPK3 Ref.9 Ref.11
Cross-link113Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.13
Cross-link265Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Experimental info

Mutagenesis101Y → E: Loss of activation of phospholipid synthesis; when associated with E-30. Ref.15 Ref.17
Mutagenesis101Y → F: Overall loss of Tyr-phosphorylation, including that of Y-30 phosphorylation. Localizes to the endoplasmic reticulum in quiescent cells. Activates phospholipid synthesis in growing cells. Ref.15 Ref.17
Mutagenesis301Y → E: Loss of activation of phospholipid synthesis; when associated with E-10. Ref.15 Ref.17
Mutagenesis301Y → F: Overall loss of Tyr-phosphorylation, including that of Y-10 phosphorylation. Localizes to the endoplasmic reticulum in quiescent cells. Activates phospholipid synthesis in growing cells. Ref.15 Ref.17
Mutagenesis1061Y → F: No effect on Tyr-phosphorylation. Loss of endoplasmic reticulum localization in quiescent cells. Ref.15
Mutagenesis1281K → R: No change in sumoylation. Ref.12
Mutagenesis1921K → R: No change in sumoylation. Ref.12
Mutagenesis2321T → D: Decreased sumoylation levels.
Mutagenesis2651K → R: Abolishes sumoylation. No change in nuclear location nor on protein stability. Increased AP1 transactivation activity when heterodimerized with cJUN. Ref.12
Mutagenesis3251T → D: No change in sumoylation levels. Ref.12
Mutagenesis3311T → D: No change in sumoylation levels. Ref.12
Mutagenesis3371Y → F: No effect on Tyr-phosphorylation. Loss of endoplasmic reticulum localization in quiescent cells. Ref.15
Mutagenesis3621S → A: Loss of protein stability. Reduced MOS/MAPK-mediated transforming ability; when associated with A-374. Ref.9 Ref.12
Mutagenesis3621S → D: Increased protein stability. Increased MOS/MAPK-mediated transforming ability and no change in sumoylation levels; when associated with D-374. Ref.9 Ref.12
Mutagenesis3741S → A: No change in sumoylation levels. Loss of protein stability. Reduced MOS/MAPK-mediated transforming ability; when associated with A-362. Ref.9 Ref.12
Mutagenesis3741S → D: Increased protein stability. Increased MOS/MAPK-mediated transforming ability and no change in sumoylation levels; when associated with D-362. Ref.9 Ref.12
Sequence conflict133 – 14412SPEEE…RRIRR → ISRRRREKENPK no nucleotide entry Ref.6

Secondary structure

... 380
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01100 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 9E3B2969347C90C8

FASTA38040,695
        10         20         30         40         50         60 
MMFSGFNADY EASSSRCSSA SPAGDSLSYY HSPADSFSSM GSPVNAQDFC TDLAVSSANF 

        70         80         90        100        110        120 
IPTVTAISTS PDLQWLVQPA LVSSVAPSQT RAPHPFGVPA PSAGAYSRAG VVKTMTGGRA 

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

       190        200        210        220        230        240 
TEIANLLKEK EKLEFILAAH RPACKIPDDL GFPEEMSVAS LDLTGGLPEV ATPESEEAFT 

       250        260        270        280        290        300 
LPLLNDPEPK PSVEPVKSIS SMELKTEPFD DFLFPASSRP SGSETARSVP DMDLSGSFYA 

       310        320        330        340        350        360 
ADWEPLHSGS LGMGPMATEL EPLCTPVVTC TPSCTAYTSS FVFTYPEADS FPSCAAAHRK 

       370        380 
GSSSNEPSSD SLSSPTLLAL 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of a human c-onc gene: deduced amino acid sequence of the human c-fos protein."
van Straaten F., Mueller R., Curran T., Van Beveren C., Verma I.M.
Proc. Natl. Acad. Sci. U.S.A. 80:3183-3187(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]NIEHS SNPs program
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pancreas.
[5]"Retrovirus-mediated gene transfer of a human c-fos cDNA into mouse bone marrow stromal cells."
Roux P., Verrier B., Klein B., Niccolino M., Marty L., Alexandre C., Piechaczyk M.
Oncogene 6:2155-2160(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-6.
[6]"Transcription factor ATF cDNA clones: an extensive family of leucine zipper proteins able to selectively form DNA-binding heterodimers."
Hai T., Liu F., Coukos W.J., Green M.R.
Genes Dev. 3:2083-2090(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 133-200, DNA-BINDING, SUBUNIT.
[7]Erratum
Hai T., Liu F., Coukos W.J., Green M.R.
Genes Dev. 4:682-682(1990)
[8]"The basic region of Fos mediates specific DNA binding."
Nakabeppu Y., Nathans D.
EMBO J. 8:3833-3841(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING.
[9]"The Mos/MAP kinase pathway stabilizes c-Fos by phosphorylation and augments its transforming activity in NIH 3T3 cells."
Okazaki K., Sagata N.
EMBO J. 14:5048-5059(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-362 AND SER-374, FUNCTION, MUTAGENESIS OF SER-362 AND SER-374.
[10]"Smad3 and Smad4 cooperate with c-Jun/c-Fos to mediate TGF-beta-induced transcription."
Zhang Y., Feng X.H., Derynck R.
Nature 394:909-913(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A COMPONENT OF THE SMAD3/SMAD4/JUN/FOS COMPLEX, FUNCTION, INTERACTION WITH SMAD3.
[11]"Molecular interpretation of ERK signal duration by immediate early gene products."
Murphy L.O., Smith S., Chen R.H., Fingar D.C., Blenis J.
Nat. Cell Biol. 4:556-564(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-325; THR-331 AND SER-374.
[12]"Down-regulation of c-Fos/c-Jun AP-1 dimer activity by sumoylation."
Bossis G., Malnou C.E., Farras R., Andermarcher E., Hipskind R., Rodriguez M., Schmidt D., Muller S., Jariel-Encontre I., Piechaczyk M.
Mol. Cell. Biol. 25:6964-6979(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-265, SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF LYS-128; LYS-192; LYS-265; THR-325; THR-331; SER-362 AND SER-374.
[13]"The proteomic reactor facilitates the analysis of affinity-purified proteins by mass spectrometry: application for identifying ubiquitinated proteins in human cells."
Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M., Haines D.S., Figeys D.
J. Proteome Res. 6:298-305(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-113.
Tissue: Lung adenocarcinoma.
[14]"Ubc9 fusion-directed SUMOylation identifies constitutive and inducible SUMOylation."
Jakobs A., Himstedt F., Funk M., Korn B., Gaestel M., Niedenthal R.
Nucleic Acids Res. 35:E109-E109(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION.
[15]"N-Terminal c-Fos tyrosine phosphorylation regulates c-Fos/ER association and c-Fos-dependent phospholipid synthesis activation."
Portal M.M., Ferrero G.O., Caputto B.L.
Oncogene 26:3551-3558(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, PHOSPHORYLATION AT TYR-10 AND TYR-30, MUTAGENESIS OF TYR-10; TYR-30; TYR-106 AND TYR-337.
[16]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"The kinase c-Src and the phosphatase TC45 coordinately regulate c-Fos tyrosine phosphorylation and c-Fos phospholipid synthesis activation capacity."
Ferrero G.O., Velazquez F.N., Caputto B.L.
Oncogene 31:3381-3391(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-10 AND TYR-30, MUTAGENESIS OF TYR-10 AND TYR-30.
[18]"Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA."
Glover J.N., Harrison S.C.
Nature 373:257-261(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 139-198 OF COMPLEX WITH JUN.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01512 Genomic DNA. Translation: CAA24756.1.
K00650 Genomic DNA. Translation: AAA52471.1.
AY212879 Genomic DNA. Translation: AAO21129.1.
AF111167 Genomic DNA. Translation: AAC98315.1.
BC004490 mRNA. Translation: AAH04490.1.
S65138 mRNA. Translation: AAB20306.1.
CCDSCCDS9841.1.
PIRTVHUF1. A01342.
E34223.
RefSeqNP_005243.1. NM_005252.3.
UniGeneHs.25647.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A02X-ray2.70F138-193[»]
1FOSX-ray3.05E/G139-200[»]
1S9KX-ray3.10D140-192[»]
DisProtDP00078.
ProteinModelPortalP01100.
SMRP01100. Positions 138-200.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108636. 84 interactions.
DIPDIP-1047N.
IntActP01100. 86 interactions.
MINTMINT-105814.
STRING9606.ENSP00000306245.

Chemistry

BindingDBP01100.
ChEMBLCHEMBL2111421.

PTM databases

PhosphoSiteP01100.

Polymorphism databases

DMDM120470.

Proteomic databases

MaxQBP01100.
PaxDbP01100.
PRIDEP01100.

Protocols and materials databases

DNASU2353.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000303562; ENSP00000306245; ENSG00000170345.
GeneID2353.
KEGGhsa:2353.
UCSCuc001xrn.3. human.

Organism-specific databases

CTD2353.
GeneCardsGC14P075745.
HGNCHGNC:3796. FOS.
HPAHPA018531.
MIM164810. gene.
neXtProtNX_P01100.
Orphanet528. Berardinelli-Seip congenital lipodystrophy.
PharmGKBPA28212.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG258795.
HOGENOMHOG000234334.
HOVERGENHBG005743.
InParanoidP01100.
KOK04379.
OMATPTCTTY.
OrthoDBEOG7VTDN9.
PhylomeDBP01100.
TreeFamTF326301.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.
SignaLinkP01100.

Gene expression databases

ArrayExpressP01100.
BgeeP01100.
CleanExHS_FOS.
GenevestigatorP01100.

Family and domain databases

InterProIPR004827. bZIP.
IPR000837. Leuzip_Fos.
[Graphical view]
PfamPF00170. bZIP_1. 1 hit.
[Graphical view]
PRINTSPR00042. LEUZIPPRFOS.
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFos. human.
EvolutionaryTraceP01100.
GeneWikiC-Fos.
GenomeRNAi2353.
NextBio9543.
PROP01100.
SOURCESearch...

Entry information

Entry nameFOS_HUMAN
AccessionPrimary (citable) accession number: P01100
Secondary accession number(s): P18849
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 171 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM