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Proto-oncogene c-Fos (Cellular oncogene fos)

 FOS_CHICK               Reviewed;         367 AA.
P11939;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
23-MAY-2018, entry version 108.
RecName: Full=Proto-oncogene c-Fos;
AltName: Full=Cellular oncogene fos;
Name=FOS;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3330781;
Moelders H., Jenuwein T., Adamkiewicz J., Mueller R.;
"Isolation and structural analysis of a biologically active chicken c-
fos cDNA: identification of evolutionarily conserved domains in fos
protein.";
Oncogene 1:377-385(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3316710;
Fujiwara K.T., Ashida K., Nishina H., Iba H., Miyajima N.,
Nishizawa M., Kawai S.;
"The chicken c-fos gene: cloning and nucleotide sequence analysis.";
J. Virol. 61:4012-4018(1987).
[3]
INTERACTION WITH MAFB.
PubMed=7935473; DOI=10.1128/MCB.14.11.7581;
Kataoka K., Fujiwara K.T., Noda M., Nishizawa M.;
"MafB,a new Maf family transcription activator that can associate with
Maf and Fos but not with Jun.";
Mol. Cell. Biol. 14:7581-7591(1994).
-!- FUNCTION: Nuclear phosphoprotein which forms a tight but non-
covalently linked complex with the JUN/AP-1 transcription factor.
FOS 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, may activate phospholipid
synthesis (By similarity). {ECO:0000250}.
-!- SUBUNIT: Heterodimer. Interacts with MAFB.
{ECO:0000269|PubMed:7935473}.
-!- SUBCELLULAR LOCATION: Nucleus. Endoplasmic reticulum
{ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=In quiescent
cells, may be present in very small amounts in the cytosol.
Following induction of cell growth, first localizes to the
endoplasmic reticulum and later to the nucleus (By similarity).
{ECO:0000250}.
-!- INDUCTION: Expression increases upon a variety of stimuli,
including growth factors, cytokines, neurotransmitters,
polypeptide hormones, stress and cell injury.
-!- PTM: May be Tyr-phosphorylated in quiescent cells and
dephosphorylated upon cell growth induction. {ECO:0000250}.
-!- SIMILARITY: Belongs to the bZIP family. Fos subfamily.
{ECO:0000305}.
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EMBL; M37000; AAA48670.1; -; mRNA.
EMBL; M18043; AAA76823.1; -; Genomic_DNA.
PIR; A28368; TVCHFS.
RefSeq; NP_990839.1; NM_205508.1.
UniGene; Gga.8709; -.
ProteinModelPortal; P11939; -.
SMR; P11939; -.
Ensembl; ENSGALT00000043488; ENSGALP00000041340; ENSGALG00000028037.
GeneID; 396512; -.
KEGG; gga:396512; -.
CTD; 2353; -.
HOVERGEN; HBG005743; -.
InParanoid; P11939; -.
KO; K04379; -.
PhylomeDB; P11939; -.
Reactome; R-GGA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-GGA-2871796; FCERI mediated MAPK activation.
Reactome; R-GGA-450341; Activation of the AP-1 family of transcription factors.
Reactome; R-GGA-9018519; Estrogen-dependent gene expression.
PRO; PR:P11939; -.
Proteomes; UP000000539; Chromosome 5.
ExpressionAtlas; P11939; baseline and differential.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0032993; C:protein-DNA complex; IEA:Ensembl.
GO; GO:0035976; C:transcription factor AP-1 complex; IEA:Ensembl.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0070412; F:R-SMAD binding; IEA:Ensembl.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IEA:Ensembl.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0001190; F:transcriptional activator activity, RNA polymerase II transcription factor binding; IEA:Ensembl.
GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl.
GO; GO:0031668; P:cellular response to extracellular stimulus; IEA:Ensembl.
GO; GO:0034614; P:cellular response to reactive oxygen species; IEA:Ensembl.
GO; GO:0007399; P:nervous system development; IEA:Ensembl.
GO; GO:0045672; P:positive regulation of osteoclast differentiation; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0035994; P:response to muscle stretch; IEA:Ensembl.
GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
GO; GO:0060395; P:SMAD protein signal transduction; IEA:Ensembl.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
InterPro; IPR000837; AP-1.
InterPro; IPR004827; bZIP.
InterPro; IPR029816; c-Fos/v-Fos.
PANTHER; PTHR23351; PTHR23351; 1.
PANTHER; PTHR23351:SF4; PTHR23351:SF4; 1.
Pfam; PF00170; bZIP_1; 1.
PRINTS; PR00042; LEUZIPPRFOS.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; DNA-binding; Endoplasmic reticulum;
Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome.
CHAIN 1 367 Proto-oncogene c-Fos.
/FTId=PRO_0000076471.
DOMAIN 136 199 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 138 158 Basic motif; required for the activation
of phospholipid synthesis.
{ECO:0000255|PROSITE-ProRule:PRU00978}.
REGION 164 192 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
MOD_RES 10 10 Phosphotyrosine; by SRC. {ECO:0000250}.
MOD_RES 30 30 Phosphotyrosine; by SRC. {ECO:0000250}.
SEQUENCE 367 AA; 39005 MW; CB7F2BF658713599 CRC64;
MMYQGFAGEY EAPSSRCSSA SPAGDSLTYY PSPADSFSSM GSPVNSQDFC TDLAVSSANF
VPTVTAISTS PDLQWLVQPT LISSVAPSQN RGHPYGVPAP APPAAYSRPA VLKAPGGRGQ
SIGRRGKVEQ LSPEEEEKRR IRRERNKMAA AKCRNRRREL TDTLQAETDQ LEEEKSALQA
EIANLLKEKE KLEFILAAHR PACKMPEELR FSEELAAATA LDLGAPSPAA AEEAFALPLM
TEAPPAVPPK EPSGSGLELK AEPFDELLFS AGPREASRSV PDMDLPGASS FYASDWEPLG
AGSGGELEPL CTPVVTCTPC PSTYTSTFVF TYPEADAFPS CAAAHRKGSS SNEPSSDSLS
SPTLLAL


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