FOS_MOUSE
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 03-AUG-2022, entry version 186.
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 DSIPI.
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/jci200522877;
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 DSIPI;
CC this interaction inhibits the binding of active AP1 to its target DNA
CC (PubMed:11397794). Interacts with CDS1 and PI4K2A, but not with CDIPT,
CC nor PI4K2B (PubMed:22105363). Interacts (via bZIP domain and leucine-
CC zipper region) with the multiprotein chromatin-remodeling complexes
CC SWI/SNF: SWI/SNF-A (BAF) subunits SMARCB1, SMARCC2 and SMARCD1
CC (PubMed:29272704). Interacts (via bZIP domain and leucine-zipper
CC region) with ARID1A (PubMed:29272704). {ECO:0000250|UniProtKB:P01100,
CC ECO:0000250|UniProtKB:P12841, ECO:0000269|PubMed:11397794,
CC ECO:0000269|PubMed:22105363, 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}.
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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; 40.
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 iPTMnet; P01101; -.
DR PhosphoSitePlus; P01101; -.
DR MaxQB; P01101; -.
DR PaxDb; P01101; -.
DR PRIDE; P01101; -.
DR ProteomicsDB; 267395; -.
DR ABCD; P01101; 3 sequenced antibodies.
DR Antibodypedia; 4375; 1944 antibodies from 51 providers.
DR DNASU; 14281; -.
DR Ensembl; ENSMUST00000021674; ENSMUSP00000021674; ENSMUSG00000021250.
DR GeneID; 14281; -.
DR KEGG; mmu:14281; -.
DR UCSC; uc007oha.2; mouse.
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; 1221590at2759; -.
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 Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR BioGRID-ORCS; 14281; 3 hits in 78 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 248 other tissues.
DR Genevisible; P01101; MM.
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:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
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:0007568; P:aging; IEA:Ensembl.
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:0031668; P:cellular response to extracellular stimulus; IMP:MGI.
DR GO; GO:0071456; P:cellular response to hypoxia; 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:0001661; P:conditioned taste aversion; IEA:Ensembl.
DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR GO; GO:0007399; P:nervous system development; IMP:MGI.
DR GO; GO:0030316; P:osteoclast differentiation; IDA:MGI.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:MGI.
DR GO; GO:1901216; P:positive regulation of neuron death; 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:0045893; P:positive regulation of transcription, DNA-templated; ISO: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:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR GO; GO:0009409; P:response to cold; IEA:Ensembl.
DR GO; GO:0051412; P:response to corticosterone; IEA:Ensembl.
DR GO; GO:0034097; P:response to cytokine; 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: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:0030431; P:sleep; 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 IDEAL; IID50165; -.
DR InterPro; IPR000837; AP-1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR029816; c-Fos/v-Fos.
DR PANTHER; PTHR23351; PTHR23351; 1.
DR PANTHER; PTHR23351:SF4; PTHR23351:SF4; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR PRINTS; PR00042; LEUZIPPRFOS.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
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 PDGF-
FT stimulated enhancement of transcriptional activity; when
FT 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; A-
FT 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 PDGF-
FT stimulated enhancement of transcriptional activity; when
FT 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
