ID FOS_MOUSE Reviewed; 380 AA. AC P01101; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 27-MAR-2024, entry version 195. DE RecName: Full=Protein c-Fos {ECO:0000305}; DE AltName: Full=Cellular oncogene fos; DE AltName: Full=FBJ osteosarcoma oncogene {ECO:0000312|MGI:MGI:95574}; DE AltName: Full=Transcription factor AP-1 subunit c-Fos {ECO:0000305}; GN Name=Fos; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6301687; DOI=10.1016/0092-8674(83)90306-9; RA van Beveren C., van Straaten F., Curran T., Mueller R., Verma I.M.; RT "Analysis of FBJ-MuSV provirus and c-fos (mouse) gene reveals that viral RT and cellular fos gene products have different carboxy termini."; RL Cell 32:1241-1255(1983). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2991903; DOI=10.1073/pnas.82.15.4987; RA Meijlink F., Curran T., Miller A.D., Verma I.M.; RT "Removal of a 67-base-pair sequence in the noncoding region of RT protooncogene fos converts it to a transforming gene."; RL Proc. Natl. Acad. Sci. U.S.A. 82:4987-4991(1985). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP INTERACTION WITH TSC22D3. RX PubMed=11397794; DOI=10.1074/jbc.m101522200; RA Mittelstadt P.R., Ashwell J.D.; RT "Inhibition of AP-1 by the glucocorticoid-inducible protein GILZ."; RL J. Biol. Chem. 276:29603-29610(2001). RN [5] RP PHOSPHORYLATION AT THR-325; THR-331; SER-362 AND SER-374, FUNCTION, AND RP MUTAGENESIS OF THR-325; THR-331; PHE-343; TYR-345; SER-362 AND SER-374. RX PubMed=12134156; DOI=10.1038/ncb822; RA Murphy L.O., Smith S., Chen R.H., Fingar D.C., Blenis J.; RT "Molecular interpretation of ERK signal duration by immediate early gene RT products."; RL Nat. Cell Biol. 4:556-564(2002). RN [6] RP PHOSPHORYLATION AT THR-232; THR-325; THR-331; SER-362 AND SER-374, RP FUNCTION, AND MUTAGENESIS OF THR-232; THR-325; THR-331 AND SER-374. RX PubMed=12972619; DOI=10.1128/mcb.23.19.7030-7043.2003; RA Monje P., Marinissen M.J., Gutkind J.S.; RT "Phosphorylation of the carboxyl-terminal transactivation domain of c-Fos RT by extracellular signal-regulated kinase mediates the transcriptional RT activation of AP-1 and cellular transformation induced by platelet-derived RT growth factor."; RL Mol. Cell. Biol. 23:7030-7043(2003). RN [7] RP PHOSPHORYLATION AT SER-362, AND FUNCTION. RX PubMed=15719069; DOI=10.1172/jci22877; RA David J.-P., Mehic D., Bakiri L., Schilling A.F., Mandic V., Priemel M., RA Idarraga M.H., Reschke M.O., Hoffmann O., Amling M., Wagner E.F.; RT "Essential role of RSK2 in c-Fos-dependent osteosarcoma development."; RL J. Clin. Invest. 115:664-672(2005). RN [8] RP FUNCTION. RX PubMed=21998197; DOI=10.1091/mbc.e11-03-0259; RA Alfonso Pecchio A.R., Cardozo Gizzi A.M., Renner M.L., Molina-Calavita M., RA Caputto B.L.; RT "c-Fos activates and physically interacts with specific enzymes of the RT pathway of synthesis of polyphosphoinositides."; RL Mol. Biol. Cell 22:4716-4725(2011). RN [9] RP FUNCTION, INTERACTION WITH CDS1 AND PI4K2A, TYROSINE PHOSPHORYLATION BY RP SRC, AND MUTAGENESIS OF LYS-139; ARG-144 AND ARG-146. RX PubMed=22105363; DOI=10.1038/onc.2011.510; RA Ferrero G.O., Velazquez F.N., Caputto B.L.; RT "The kinase c-Src and the phosphatase TC45 coordinately regulate c-Fos RT tyrosine phosphorylation and c-Fos phospholipid synthesis activation RT capacity."; RL Oncogene 31:3381-3391(2012). RN [10] RP INTERACTION WITH SMARCB1; SMARCC2; SMARCD1; ARID1A AND JUN, AND MUTAGENESIS RP OF 165-LEU--LEU-193. RX PubMed=29272704; DOI=10.1016/j.molcel.2017.11.026; RA Vierbuchen T., Ling E., Cowley C.J., Couch C.H., Wang X., Harmin D.A., RA Roberts C.W.M., Greenberg M.E.; RT "AP-1 Transcription Factors and the BAF Complex Mediate Signal-Dependent RT Enhancer Selection."; RL Mol. Cell 68:1067-1082.e12(2017). CC -!- FUNCTION: Nuclear phosphoprotein which forms a tight but non-covalently CC linked complex with the JUN/AP-1 transcription factor. On TGF-beta CC activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex, at the CC AP1/SMAD-binding site to regulate TGF-beta-mediated signaling (By CC similarity). Has a critical function in regulating the development of CC cells destined to form and maintain the skeleton. It is thought to have CC an important role in signal transduction, cell proliferation and CC differentiation. In growing cells, activates phospholipid synthesis, CC possibly by activating CDS1 and PI4K2A. This activity requires Tyr- CC dephosphorylation and association with the endoplasmic reticulum. CC {ECO:0000250, ECO:0000269|PubMed:12134156, ECO:0000269|PubMed:12972619, CC ECO:0000269|PubMed:15719069, ECO:0000269|PubMed:21998197, CC ECO:0000269|PubMed:22105363}. CC -!- SUBUNIT: Heterodimer; with JUN (PubMed:29272704). Component of the CC SMAD3/SMAD4/JUN/FOS complex required for synergistic TGF-beta-mediated CC transcription at the AP1 promoter site (By similarity). Interacts with CC SMAD3; the interaction is weak even on TGF-beta activation (By CC similarity). Interacts with MAFB (By similarity). Interacts with CC TSC22D3 (via N-terminus); this interaction inhibits the binding of CC active AP1 to its target DNA (PubMed:11397794). Interacts with CDS1 and CC PI4K2A, but not with CDIPT, nor PI4K2B (PubMed:22105363). Interacts CC (via bZIP domain and leucine-zipper region) with the multiprotein CC chromatin-remodeling complexes SWI/SNF: SWI/SNF-A (BAF) subunits CC SMARCB1, SMARCC2 and SMARCD1 (PubMed:29272704). Interacts (via bZIP CC domain and leucine-zipper region) with ARID1A (PubMed:29272704). CC {ECO:0000250|UniProtKB:P01100, ECO:0000250|UniProtKB:P12841, CC ECO:0000269|PubMed:11397794, ECO:0000269|PubMed:22105363, CC ECO:0000269|PubMed:29272704}. CC -!- INTERACTION: CC P01101; O08537: Esr2; NbExp=2; IntAct=EBI-4288185, EBI-2526214; CC P01101; P54841: Mafb; NbExp=4; IntAct=EBI-4288185, EBI-16093217; CC P01101; P14404: Mecom; NbExp=2; IntAct=EBI-4288185, EBI-1994523; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}. CC Endoplasmic reticulum {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. CC Note=In quiescent cells, present in very small amounts in the cytosol. CC Following induction of cell growth, first localizes to the endoplasmic CC reticulum and only later to the nucleus. Localization at the CC endoplasmic reticulum requires dephosphorylation at Tyr-10 and Tyr-30 CC (By similarity). {ECO:0000250}. CC -!- PTM: Phosphorylated in the C-terminal upon stimulation by nerve growth CC factor (NGF) and epidermal growth factor (EGF). Phosphorylated, in CC vitro, by MAPK and RSK1. Phosphorylation on both Ser-362 and Ser-374 by CC MAPK1/2 and RSK1/2 leads to protein stabilization with phosphorylation CC on Ser-374 being the major site for protein stabilization on NGF CC stimulation. Phosphorylation on Ser-362 and Ser-374 primes further CC phosphorylations on Thr-325 and Thr-331 through promoting docking of CC MAPK to the DEF domain. Phosphorylation on Thr-232, induced by HA-RAS, CC activates the transcriptional activity and antagonizes sumoylation. CC Phosphorylation on Ser-362 by RSK2 in osteoblasts contributes to CC osteoblast transformation (By similarity). {ECO:0000250}. CC -!- PTM: Constitutively sumoylated with SUMO1, SUMO2 and SUMO3. CC Desumoylated by SENP2. Sumoylation requires heterodimerization with JUN CC and is enhanced by mitogen stimulation. Sumoylation inhibits the AP-1 CC transcriptional activity and is, itself, inhibited by Ras-activated CC phosphorylation on Thr-232 (By similarity). {ECO:0000250}. CC -!- PTM: In quiescent cells, the small amount of FOS present is CC phosphorylated at Tyr-10 and Tyr-30 by SRC. This Tyr-phosphorylated CC form is cytosolic. In growing cells, dephosphorylated by PTPN2. CC Dephosphorylation leads to the association with endoplasmic reticulum CC membranes and activation of phospholipid synthesis. CC {ECO:0000269|PubMed:12134156, ECO:0000269|PubMed:12972619, CC ECO:0000269|PubMed:15719069}. CC -!- SIMILARITY: Belongs to the bZIP family. Fos subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; V00727; CAA24105.1; -; Genomic_DNA. DR EMBL; J00370; AAA96699.1; -; Genomic_DNA. DR EMBL; BC029814; AAH29814.1; -; mRNA. DR CCDS; CCDS26059.1; -. DR PIR; A01343; TVMSF. DR RefSeq; NP_034364.1; NM_010234.2. DR PDB; 2WT7; X-ray; 2.30 A; A=138-200. DR PDBsum; 2WT7; -. DR AlphaFoldDB; P01101; -. DR SMR; P01101; -. DR BioGRID; 199726; 41. DR ComplexPortal; CPX-610; AP-1 transcription factor complex FOS-JUN-NFATC2. DR ComplexPortal; CPX-611; bZIP transcription factor complex, Fos-Jun. DR DIP; DIP-1066N; -. DR ELM; P01101; -. DR IntAct; P01101; 4. DR MINT; P01101; -. DR STRING; 10090.ENSMUSP00000021674; -. DR ChEMBL; CHEMBL4105918; -. DR GlyGen; P01101; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; P01101; -. DR PhosphoSitePlus; P01101; -. DR MaxQB; P01101; -. DR PaxDb; 10090-ENSMUSP00000021674; -. DR ProteomicsDB; 267395; -. DR ABCD; P01101; 3 sequenced antibodies. DR Antibodypedia; 4375; 2337 antibodies from 51 providers. DR DNASU; 14281; -. DR Ensembl; ENSMUST00000021674.7; ENSMUSP00000021674.7; ENSMUSG00000021250.14. DR GeneID; 14281; -. DR KEGG; mmu:14281; -. DR UCSC; uc007oha.2; mouse. DR AGR; MGI:95574; -. DR CTD; 2353; -. DR MGI; MGI:95574; Fos. DR VEuPathDB; HostDB:ENSMUSG00000021250; -. DR eggNOG; KOG1414; Eukaryota. DR GeneTree; ENSGT00940000159276; -. DR HOGENOM; CLU_049742_2_0_1; -. DR InParanoid; P01101; -. DR OMA; FTYPEAE; -. DR OrthoDB; 4614365at2759; -. DR PhylomeDB; P01101; -. DR TreeFam; TF326301; -. DR Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence. DR Reactome; R-MMU-2871796; FCERI mediated MAPK activation. DR Reactome; R-MMU-450341; Activation of the AP-1 family of transcription factors. DR BioGRID-ORCS; 14281; 3 hits in 83 CRISPR screens. DR ChiTaRS; Fos; mouse. DR PRO; PR:P01101; -. DR Proteomes; UP000000589; Chromosome 12. DR RNAct; P01101; Protein. DR Bgee; ENSMUSG00000021250; Expressed in granulocyte and 251 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IDA:CACAO. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:CACAO. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:CACAO. DR GO; GO:0032993; C:protein-DNA complex; ISO:MGI. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI. DR GO; GO:0035976; C:transcription factor AP-1 complex; IPI:ComplexPortal. DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central. DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0070412; F:R-SMAD binding; ISO:MGI. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISO:MGI. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI. DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI. DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI. DR GO; GO:0001221; F:transcription coregulator binding; ISO:MGI. DR GO; GO:0071276; P:cellular response to cadmium ion; ISO:MGI. DR GO; GO:0071277; P:cellular response to calcium ion; IDA:MGI. DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl. DR GO; GO:0031668; P:cellular response to extracellular stimulus; IMP:MGI. DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl. DR GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IEA:Ensembl. DR GO; GO:1904628; P:cellular response to phorbol 13-acetate 12-myristate; IEA:Ensembl. DR GO; GO:1990646; P:cellular response to prolactin; IEA:Ensembl. DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:MGI. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl. DR GO; GO:0034224; P:cellular response to zinc ion starvation; IEA:Ensembl. DR GO; GO:0001661; P:conditioned taste aversion; IEA:Ensembl. DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl. DR GO; GO:1903131; P:mononuclear cell differentiation; IEA:Ensembl. DR GO; GO:0051450; P:myoblast proliferation; IEA:Ensembl. DR GO; GO:0007399; P:nervous system development; IMP:MGI. DR GO; GO:0030316; P:osteoclast differentiation; IDA:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:MGI. DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:MGI. DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; IDA:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:NTNU_SB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI. DR GO; GO:0014823; P:response to activity; IEA:Ensembl. DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl. DR GO; GO:0051412; P:response to corticosterone; IEA:Ensembl. DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl. DR GO; GO:0009629; P:response to gravity; IEA:Ensembl. DR GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl. DR GO; GO:0032868; P:response to insulin; IEA:Ensembl. DR GO; GO:0009416; P:response to light stimulus; IEA:Ensembl. DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0035994; P:response to muscle stretch; IDA:MGI. DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl. DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl. DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:MGI. DR GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI. DR GO; GO:0014856; P:skeletal muscle cell proliferation; IEA:Ensembl. DR GO; GO:0060395; P:SMAD protein signal transduction; ISO:MGI. DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:MGI. DR CDD; cd14721; bZIP_Fos; 1. DR Gene3D; 1.20.5.170; -; 1. DR IDEAL; IID50165; -. DR InterPro; IPR000837; AP-1. DR InterPro; IPR004827; bZIP. DR InterPro; IPR046347; bZIP_sf. DR PANTHER; PTHR23351; FOS TRANSCRIPTION FACTOR-RELATED; 1. DR PANTHER; PTHR23351:SF4; PROTEIN C-FOS; 1. DR Pfam; PF00170; bZIP_1; 1. DR PRINTS; PR00042; LEUZIPPRFOS. DR SMART; SM00338; BRLZ; 1. DR SUPFAM; SSF57959; Leucine zipper domain; 1. DR PROSITE; PS50217; BZIP; 1. DR PROSITE; PS00036; BZIP_BASIC; 1. DR Genevisible; P01101; MM. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; DNA-binding; Endoplasmic reticulum; KW Isopeptide bond; Nucleus; Phosphoprotein; Proto-oncogene; KW Reference proteome; Ubl conjugation. FT CHAIN 1..380 FT /note="Protein c-Fos" FT /id="PRO_0000076467" FT DOMAIN 137..200 FT /note="bZIP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT REGION 117..141 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 139..159 FT /note="Basic motif; required for the activation of FT phospholipid synthesis, but not for CDS1-binding" FT REGION 165..193 FT /note="Leucine-zipper" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT REGION 354..380 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 357..380 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 10 FT /note="Phosphotyrosine; by SRC" FT /evidence="ECO:0000250|UniProtKB:P01100" FT MOD_RES 30 FT /note="Phosphotyrosine; by SRC" FT /evidence="ECO:0000250|UniProtKB:P01100" FT MOD_RES 232 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:12972619" FT MOD_RES 325 FT /note="Phosphothreonine; by MAPK1 and MAPK3" FT /evidence="ECO:0000269|PubMed:12134156, FT ECO:0000269|PubMed:12972619" FT MOD_RES 331 FT /note="Phosphothreonine; by MAPK1 and MAPK3" FT /evidence="ECO:0000269|PubMed:12134156, FT ECO:0000269|PubMed:12972619" FT MOD_RES 362 FT /note="Phosphoserine; by MAPK1, MAPK3 and RPS6KA3" FT /evidence="ECO:0000269|PubMed:12134156, FT ECO:0000269|PubMed:12972619, ECO:0000269|PubMed:15719069" FT MOD_RES 374 FT /note="Phosphoserine; by MAPK1 and MAPK3" FT /evidence="ECO:0000269|PubMed:12134156, FT ECO:0000269|PubMed:12972619" FT CROSSLNK 113 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P01100" FT CROSSLNK 128 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P01100" FT CROSSLNK 265 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT /evidence="ECO:0000250" FT CROSSLNK 265 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P01100" FT MUTAGEN 139 FT /note="K->N: No effect on activation of phospholipid FT synthesis." FT /evidence="ECO:0000269|PubMed:22105363" FT MUTAGEN 144 FT /note="R->N: No effect on activation of phospholipid FT synthesis, nor on CDS1-binding." FT /evidence="ECO:0000269|PubMed:22105363" FT MUTAGEN 146 FT /note="R->N: Complete loss of activation of phospholipid FT synthesis. No effect on CDS1-binding." FT /evidence="ECO:0000269|PubMed:22105363" FT MUTAGEN 165..193 FT /note="LQAETDQLEDEKSALQTEIANLLKEKEKL->AQAETDQAEDEKSAAQTEIAN FT AAKEKEKA: Disrupts interaction with SMARCB1, SMARCD1, FT ARID1A and JUN." FT /evidence="ECO:0000269|PubMed:29272704" FT MUTAGEN 232 FT /note="T->A: No effect on PDGF-stimulated enhancement of FT transcriptional activity. Completely abolishes FT PDGF-stimulated enhancement of transcriptional activity; FT when associated with A-325; A-331 and A-374." FT /evidence="ECO:0000269|PubMed:12972619" FT MUTAGEN 325 FT /note="T->A: Almost no EGF-mediated phosphorylation, FT greatly reduced cellular transformation, and reduced AP1 FT activity by 20%; when associated with A-331. No effect on FT PDGF-stimulated enhancement of transcriptional activity. FT Completely abolishes PDGF-stimulated enhancement of FT transcriptional activity; when associated with A-232; A-331 FT and A-374." FT /evidence="ECO:0000269|PubMed:12134156, FT ECO:0000269|PubMed:12972619" FT MUTAGEN 331 FT /note="T->A: Almost no EGF-mediated phosphorylation, FT greatly reduced cellular transformation, and reduced AP1 FT activity by 20%; when associated with A-325. No effect on FT PDGF-stimulated enhancement of transcriptional activity. FT Completely abolishes PDGF-stimulated enhancement of FT transcriptional activity; when associated with A-232; FT A-325;and A-374." FT /evidence="ECO:0000269|PubMed:12134156, FT ECO:0000269|PubMed:12972619" FT MUTAGEN 343 FT /note="F->A: Reduced phosphorylation by ERK. Reduced AP1 FT activity by 65%." FT /evidence="ECO:0000269|PubMed:12134156" FT MUTAGEN 345 FT /note="Y->A: Reduced phosphorylation by ERK." FT /evidence="ECO:0000269|PubMed:12134156" FT MUTAGEN 362 FT /note="S->D: Enhanced EGF- and RSK-mediated transformation; FT when associated with D-374." FT /evidence="ECO:0000269|PubMed:12134156" FT MUTAGEN 362 FT /note="S->E: Increased enhancement of EGF- and RSK-mediated FT transformation; when associated with E-374." FT /evidence="ECO:0000269|PubMed:12134156" FT MUTAGEN 374 FT /note="S->A: No effect on PDGF-stimulated enhancement of FT transcriptional activity. Completely abolishes FT PDGF-stimulated enhancement of transcriptional activity; FT when associated with A-232; A-325 and A-331." FT /evidence="ECO:0000269|PubMed:12134156, FT ECO:0000269|PubMed:12972619" FT MUTAGEN 374 FT /note="S->D: Enhanced EGF- and RSK-mediated transformation; FT when associated with D-362." FT /evidence="ECO:0000269|PubMed:12134156, FT ECO:0000269|PubMed:12972619" FT MUTAGEN 374 FT /note="S->E: Enhanced EGF- and RSK-mediated transformation; FT when associated with E-362." FT /evidence="ECO:0000269|PubMed:12134156, FT ECO:0000269|PubMed:12972619" FT HELIX 139..199 FT /evidence="ECO:0007829|PDB:2WT7" SQ SEQUENCE 380 AA; 40838 MW; 475966265952B624 CRC64; MMFSGFNADY EASSSRCSSA SPAGDSLSYY HSPADSFSSM GSPVNTQDFC ADLSVSSANF IPTVTAISTS PDLQWLVQPT LVSSVAPSQT RAPHPYGLPT QSAGAYARAG MVKTVSGGRA QSIGRRGKVE QLSPEEEEKR RIRRERNKMA AAKCRNRRRE LTDTLQAETD QLEDEKSALQ TEIANLLKEK EKLEFILAAH RPACKIPDDL GFPEEMSVAS LDLTGGLPEA STPESEEAFT LPLLNDPEPK PSLEPVKSIS NVELKAEPFD DFLFPASSRP SGSETSRSVP DVDLSGSFYA ADWEPLHSNS LGMGPMVTEL EPLCTPVVTC TPGCTTYTSS FVFTYPEADS FPSCAAAHRK GSSSNEPSSD SLSSPTLLAL //