Description: Homo sapiens FBJ murine osteosarcoma viral oncogene homolog (FOS), mRNA. RefSeq Summary (NM_005252): The Fos gene family consists of 4 members: FOS, FOSB, FOSL1, and FOSL2. These genes encode leucine zipper proteins that can dimerize with proteins of the JUN family, thereby forming the transcription factor complex AP-1. As such, the FOS proteins have been implicated as regulators of cell proliferation, differentiation, and transformation. In some cases, expression of the FOS gene has also been associated with apoptotic cell death. [provided by RefSeq, Jul 2008]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Transcript (Including UTRs) Position: hg19 chr14:75,745,481-75,748,937 Size: 3,457 Total Exon Count: 4 Strand: + Coding Region Position: hg19 chr14:75,745,686-75,748,127 Size: 2,442 Coding Exon Count: 4
ID:FOS_HUMAN DESCRIPTION: RecName: Full=Proto-oncogene c-Fos; AltName: Full=Cellular oncogene fos; AltName: Full=G0/G1 switch regulatory protein 7; 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. SUBUNIT: 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. INTERACTION: P05067:APP; NbExp=3; IntAct=EBI-852851, EBI-77613; P15336:ATF2; NbExp=4; IntAct=EBI-852851, EBI-1170906; P10909:CLU; NbExp=2; IntAct=EBI-852851, EBI-1104674; Q9BT78:COPS4; NbExp=2; IntAct=EBI-852851, EBI-742413; P05412:JUN; NbExp=6; IntAct=EBI-852851, EBI-852823; P17535:JUND; NbExp=3; IntAct=EBI-852851, EBI-2682803; P52736:ZNF133; NbExp=4; IntAct=EBI-852851, EBI-2687350; 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 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. SIMILARITY: Belongs to the bZIP family. Fos subfamily. SIMILARITY: Contains 1 bZIP (basic-leucine zipper) domain. WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/fos/";
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P01100
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Gene Ontology (GO) Annotations with Structured Vocabulary
Molecular Function: GO:0000978 RNA polymerase II core promoter proximal region sequence-specific DNA binding GO:0000979 RNA polymerase II core promoter sequence-specific DNA binding GO:0000981 RNA polymerase II transcription factor activity, sequence-specific DNA binding GO:0001077 transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding GO:0001102 RNA polymerase II activating transcription factor binding GO:0001190 transcriptional activator activity, RNA polymerase II transcription factor binding GO:0003677 DNA binding GO:0003682 chromatin binding GO:0003690 double-stranded DNA binding GO:0003700 transcription factor activity, sequence-specific DNA binding GO:0005515 protein binding GO:0008134 transcription factor binding GO:0043565 sequence-specific DNA binding GO:0044212 transcription regulatory region DNA binding GO:0046982 protein heterodimerization activity GO:0070412 R-SMAD binding
Biological Process: GO:0001661 conditioned taste aversion GO:0006306 DNA methylation GO:0006355 regulation of transcription, DNA-templated GO:0006357 regulation of transcription from RNA polymerase II promoter GO:0006366 transcription from RNA polymerase II promoter GO:0006954 inflammatory response GO:0007179 transforming growth factor beta receptor signaling pathway GO:0007399 nervous system development GO:0007565 female pregnancy GO:0007568 aging GO:0009409 response to cold GO:0009416 response to light stimulus GO:0009612 response to mechanical stimulus GO:0009629 response to gravity GO:0009636 response to toxic substance GO:0014070 response to organic cyclic compound GO:0019221 cytokine-mediated signaling pathway GO:0030431 sleep GO:0031668 cellular response to extracellular stimulus GO:0032496 response to lipopolysaccharide GO:0032570 response to progesterone GO:0032870 cellular response to hormone stimulus GO:0034097 response to cytokine GO:0034614 cellular response to reactive oxygen species GO:0035902 response to immobilization stress GO:0035914 skeletal muscle cell differentiation GO:0035994 response to muscle stretch GO:0038095 Fc-epsilon receptor signaling pathway GO:0042493 response to drug GO:0045672 positive regulation of osteoclast differentiation GO:0045893 positive regulation of transcription, DNA-templated GO:0045944 positive regulation of transcription from RNA polymerase II promoter GO:0051090 regulation of sequence-specific DNA binding transcription factor activity GO:0051412 response to corticosterone GO:0051591 response to cAMP GO:0060395 SMAD protein signal transduction GO:0071276 cellular response to cadmium ion GO:0071277 cellular response to calcium ion GO:1901216 positive regulation of neuron death GO:1902895 positive regulation of pri-miRNA transcription from RNA polymerase II promoter