ID   FOS_HUMAN               Reviewed;         380 AA.
AC   P01100; P18849;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   24-JUL-2007, entry version 93.
DE   Proto-oncogene protein c-fos (Cellular oncogene fos) (G0/G1 switch
DE   regulatory protein 7).
GN   Name=FOS; Synonyms=G0S7;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=83221560; PubMed=6574479;
RA   van Straaten F., Mueller R., Curran T., Van Beveren C., Verma I.M.;
RT   "Complete nucleotide sequence of a human c-onc gene: deduced amino
RT   acid sequence of the human c-fos protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:3183-3187(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 133-200.
RX   MEDLINE=90185187; PubMed=2516827;
RA   Hai T., Liu F., Coukos W.J., Green M.R.;
RT   "Transcription factor ATF cDNA clones: an extensive family of leucine
RT   zipper proteins able to selectively form DNA-binding heterodimers.";
RL   Genes Dev. 3:2083-2090(1989).
RN   [3]
RP   ERRATUM.
RA   Hai T., Liu F., Coukos W.J., Green M.R.;
RL   Genes Dev. 4:682-682(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Rieder M.J., Livingston R.J., Daniels M.R., Montoya M.A., Chung M.-W.,
RA   Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D.,
RA   Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.;
RT   "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department
RT   of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22459283; PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA   Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA   Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA   Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA   Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA   Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA   Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA   Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA   Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA   Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA   Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA   Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA   Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA   Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA   Quetier F., Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreas;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-6.
RX   MEDLINE=92050815; PubMed=1658710;
RA   Roux P., Verrier B., Klein B., Niccolino M., Marty L., Alexandre C.,
RA   Piechaczyk M.;
RT   "Retrovirus-mediated gene transfer of a human c-fos cDNA into mouse
RT   bone marrow stromal cells.";
RL   Oncogene 6:2155-2160(1991).
RN   [8]
RP   DNA-BINDING.
RX   MEDLINE=90059986; PubMed=2511004;
RA   Nakabeppu Y., Nathans D.;
RT   "The basic region of Fos mediates specific DNA binding.";
RL   EMBO J. 8:3833-3841(1989).
RN   [9]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-113, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Lung adenocarcinoma;
RX   PubMed=17203973; DOI=10.1021/pr060438j;
RA   Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M.,
RA   Haines D.S., Figeys D.;
RT   "The proteomic reactor facilitates the analysis of affinity-purified
RT   proteins by mass spectrometry: application for identifying
RT   ubiquitinated proteins in human cells.";
RL   J. Proteome Res. 6:298-305(2007).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 139-198 OF COMPLEX WITH JUN.
RX   MEDLINE=95115802; PubMed=7816143; DOI=10.1038/373257a0;
RA   Glover J.N., Harrison S.C.;
RT   "Crystal structure of the heterodimeric bZIP transcription factor c-
RT   Fos-c-Jun bound to DNA.";
RL   Nature 373:257-261(1995).
CC   -!- FUNCTION: Nuclear phosphoprotein which forms a tight but non-
CC       covalently linked complex with the JUN/AP-1 transcription factor.
CC       In the heterodimer, c-fos and JUN/AP-1 basic regions each seems to
CC       interact with symmetrical DNA half sites. Has a critical function
CC       in regulating the development of cells destined to form and
CC       maintain the skeleton. It is thought to have an important role in
CC       signal transduction, cell proliferation and differentiation.
CC   -!- SUBUNIT: Heterodimer with JUN. Interacts with DSIPI; this
CC       interaction inhibits the binding of active AP1 to its target DNA.
CC       Interacts with MAFB (By similarity).
CC   -!- INTERACTION:
CC       O60869-1:EDF1; NbExp=1; IntAct=EBI-852851, EBI-781310;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- INDUCTION: C-fos expression increases upon a variety of stimuli,
CC       including growth factors, cytokines, neurotransmitters,
CC       polypeptide hormones, stress and cell injury.
CC   -!- SIMILARITY: Belongs to the bZIP family. Fos subfamily.
CC   -!- SIMILARITY: Contains 1 bZIP domain.
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DR   EMBL; V01512; CAA24756.1; -; Genomic_DNA.
DR   EMBL; K00650; AAA52471.1; -; Genomic_DNA.
DR   EMBL; AY212879; AAO21129.1; -; Genomic_DNA.
DR   EMBL; AF111167; AAC98315.1; -; Genomic_DNA.
DR   EMBL; BC004490; AAH04490.1; -; mRNA.
DR   EMBL; S65138; AAB20306.1; -; mRNA.
DR   PIR; A01342; TVHUF1.
DR   PIR; E34223; E34223.
DR   UniGene; Hs.25647; -.
DR   PDB; 1A02; X-ray; F=139-193.
DR   PDB; 1FOS; X-ray; E=139-198, G=140-198.
DR   PDB; 1S9K; X-ray; D=140-192.
DR   DisProt; DP00078; -.
DR   DIP; DIP:1047N; -.
DR   IntAct; P01100; -.
DR   TRANSFAC; T00123; -.
DR   Ensembl; ENSG00000170345; Homo sapiens.
DR   KEGG; hsa:2353; -.
DR   H-InvDB; HIX0011826; -.
DR   HGNC; HGNC:3796; FOS.
DR   HPA; CAB000461; -.
DR   MIM; 164810; gene.
DR   PharmGKB; PA134953249; -.
DR   LinkHub; P01100; -.
DR   ArrayExpress; P01100; -.
DR   GermOnline; ENSG00000170345; Homo sapiens.
DR   RZPD-ProtExp; B0247; -.
DR   RZPD-ProtExp; IOH27255; -.
DR   RZPD-ProtExp; RZPDo834H0326; -.
DR   RZPD-ProtExp; RZPDo834H0730; -.
DR   RZPD-ProtExp; T1225; -.
DR   GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0003704; F:specific RNA polymerase II transcription fa...; TAS:ProtInc.
DR   GO; GO:0006306; P:DNA methylation; TAS:ProtInc.
DR   GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR   GO; GO:0006357; P:regulation of transcription from RNA polyme...; TAS:ProtInc.
DR   InterPro; IPR011700; bZIP_2.
DR   InterPro; IPR000837; Leuzip_Fos.
DR   InterPro; IPR004827; TF_bZIP.
DR   Pfam; PF07716; bZIP_2; 1.
DR   PRINTS; PR00042; LEUZIPPRFOS.
DR   SMART; SM00338; BRLZ; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Nucleus; Phosphorylation; Proto-oncogene;
KW   Ubl conjugation.
FT   CHAIN         1    380       Proto-oncogene protein c-fos.
FT                                /FTId=PRO_0000076465.
FT   DOMAIN      165    193       Leucine-zipper.
FT   DNA_BIND    139    160       Basic motif.
FT   CROSSLNK    113    113       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   CONFLICT    133    144       SPEEEEKRRIRR -> ISRRRREKENPK (in Ref. 2).
FT   HELIX       141    191
SQ   SEQUENCE   380 AA;  40695 MW;  9E3B2969347C90C8 CRC64;
     MMFSGFNADY EASSSRCSSA SPAGDSLSYY HSPADSFSSM GSPVNAQDFC TDLAVSSANF
     IPTVTAISTS PDLQWLVQPA LVSSVAPSQT RAPHPFGVPA PSAGAYSRAG VVKTMTGGRA
     QSIGRRGKVE QLSPEEEEKR RIRRERNKMA AAKCRNRRRE LTDTLQAETD QLEDEKSALQ
     TEIANLLKEK EKLEFILAAH RPACKIPDDL GFPEEMSVAS LDLTGGLPEV ATPESEEAFT
     LPLLNDPEPK PSVEPVKSIS SMELKTEPFD DFLFPASSRP SGSETARSVP DMDLSGSFYA
     ADWEPLHSGS LGMGPMATEL EPLCTPVVTC TPSCTAYTSS FVFTYPEADS FPSCAAAHRK
     GSSSNEPSSD SLSSPTLLAL
//
