Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P01100

- FOS_HUMAN

UniProt

P01100 - FOS_HUMAN

Protein

Proto-oncogene c-Fos

Gene

FOS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 173 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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. In growing cells, activates phospholipid synthesis, possibly by activating CDS1 and PI4K2A. This activity requires Tyr-dephosphorylation and association with the endoplasmic reticulum.5 Publications

    GO - Molecular functioni

    1. double-stranded DNA binding Source: Ensembl
    2. protein binding Source: IntAct
    3. R-SMAD binding Source: BHF-UCL
    4. sequence-specific DNA binding Source: Ensembl
    5. sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    6. transcription regulatory region DNA binding Source: BHF-UCL

    GO - Biological processi

    1. aging Source: Ensembl
    2. cellular response to calcium ion Source: Ensembl
    3. cellular response to extracellular stimulus Source: Ensembl
    4. cellular response to hormone stimulus Source: Ensembl
    5. cellular response to reactive oxygen species Source: BHF-UCL
    6. conditioned taste aversion Source: Ensembl
    7. DNA methylation Source: ProtInc
    8. Fc-epsilon receptor signaling pathway Source: Reactome
    9. female pregnancy Source: Ensembl
    10. inflammatory response Source: ProtInc
    11. innate immune response Source: Reactome
    12. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    13. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    14. nervous system development Source: Ensembl
    15. positive regulation of osteoclast differentiation Source: Ensembl
    16. positive regulation of transcription, DNA-templated Source: BHF-UCL
    17. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    18. regulation of sequence-specific DNA binding transcription factor activity Source: Reactome
    19. regulation of transcription from RNA polymerase II promoter Source: ProtInc
    20. response to cAMP Source: Ensembl
    21. response to cold Source: Ensembl
    22. response to corticosterone Source: Ensembl
    23. response to cytokine Source: Ensembl
    24. response to drug Source: Ensembl
    25. response to gravity Source: Ensembl
    26. response to light stimulus Source: Ensembl
    27. response to lipopolysaccharide Source: Ensembl
    28. response to mechanical stimulus Source: Ensembl
    29. response to progesterone Source: Ensembl
    30. response to toxic substance Source: Ensembl
    31. skeletal muscle cell differentiation Source: Ensembl
    32. sleep Source: Ensembl
    33. SMAD protein signal transduction Source: BHF-UCL
    34. stress-activated MAPK cascade Source: Reactome
    35. toll-like receptor 10 signaling pathway Source: Reactome
    36. toll-like receptor 2 signaling pathway Source: Reactome
    37. toll-like receptor 3 signaling pathway Source: Reactome
    38. toll-like receptor 4 signaling pathway Source: Reactome
    39. toll-like receptor 5 signaling pathway Source: Reactome
    40. toll-like receptor 9 signaling pathway Source: Reactome
    41. toll-like receptor signaling pathway Source: Reactome
    42. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    43. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    44. transcription from RNA polymerase II promoter Source: ProtInc
    45. transforming growth factor beta receptor signaling pathway Source: BHF-UCL
    46. TRIF-dependent toll-like receptor signaling pathway Source: Reactome

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_163701. FCERI mediated MAPK activation.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_21326. Activation of the AP-1 family of transcription factors.
    SignaLinkiP01100.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proto-oncogene c-Fos
    Alternative name(s):
    Cellular oncogene fos
    G0/G1 switch regulatory protein 7
    Gene namesi
    Name:FOS
    Synonyms:G0S7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:3796. FOS.

    Subcellular locationi

    Nucleus. Endoplasmic reticulum. Cytoplasmcytosol
    Note: In quiescent cells, present in very small amounts in the cytosol. Following induction of cell growth, first localizes to the endoplasmic reticulum and only later to the nucleus. Localization at the endoplasmic reticulum requires dephosphorylation at Tyr-10 and Tyr-30.

    GO - Cellular componenti

    1. cytosol Source: UniProtKB-SubCell
    2. endoplasmic reticulum Source: UniProtKB-SubCell
    3. membrane Source: Ensembl
    4. neuron projection Source: Ensembl
    5. nucleoplasm Source: Reactome
    6. nucleus Source: HPA
    7. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi10 – 101Y → E: Loss of activation of phospholipid synthesis; when associated with E-30. 2 Publications
    Mutagenesisi10 – 101Y → F: Overall loss of Tyr-phosphorylation, including that of Y-30 phosphorylation. Localizes to the endoplasmic reticulum in quiescent cells. Activates phospholipid synthesis in growing cells. 2 Publications
    Mutagenesisi30 – 301Y → E: Loss of activation of phospholipid synthesis; when associated with E-10. 2 Publications
    Mutagenesisi30 – 301Y → F: Overall loss of Tyr-phosphorylation, including that of Y-10 phosphorylation. Localizes to the endoplasmic reticulum in quiescent cells. Activates phospholipid synthesis in growing cells. 2 Publications
    Mutagenesisi106 – 1061Y → F: No effect on Tyr-phosphorylation. Loss of endoplasmic reticulum localization in quiescent cells. 1 Publication
    Mutagenesisi128 – 1281K → R: No change in sumoylation. 1 Publication
    Mutagenesisi192 – 1921K → R: No change in sumoylation. 1 Publication
    Mutagenesisi232 – 2321T → D: Decreased sumoylation levels.
    Mutagenesisi265 – 2651K → R: Abolishes sumoylation. No change in nuclear location nor on protein stability. Increased AP1 transactivation activity when heterodimerized with cJUN. 1 Publication
    Mutagenesisi325 – 3251T → D: No change in sumoylation levels. 1 Publication
    Mutagenesisi331 – 3311T → D: No change in sumoylation levels. 1 Publication
    Mutagenesisi337 – 3371Y → F: No effect on Tyr-phosphorylation. Loss of endoplasmic reticulum localization in quiescent cells. 1 Publication
    Mutagenesisi362 – 3621S → A: Loss of protein stability. Reduced MOS/MAPK-mediated transforming ability; when associated with A-374. 2 Publications
    Mutagenesisi362 – 3621S → D: Increased protein stability. Increased MOS/MAPK-mediated transforming ability and no change in sumoylation levels; when associated with D-374. 2 Publications
    Mutagenesisi374 – 3741S → A: No change in sumoylation levels. Loss of protein stability. Reduced MOS/MAPK-mediated transforming ability; when associated with A-362. 2 Publications
    Mutagenesisi374 – 3741S → D: Increased protein stability. Increased MOS/MAPK-mediated transforming ability and no change in sumoylation levels; when associated with D-362. 2 Publications

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    Orphaneti528. Berardinelli-Seip congenital lipodystrophy.
    PharmGKBiPA28212.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 380380Proto-oncogene c-FosPRO_0000076465Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei10 – 101Phosphotyrosine; by SRC2 Publications
    Modified residuei30 – 301Phosphotyrosine; by SRC2 Publications
    Cross-linki113 – 113Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei232 – 2321PhosphothreonineBy similarity
    Cross-linki265 – 265Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei325 – 3251Phosphothreonine; by MAPK1 and MAPK31 Publication
    Modified residuei331 – 3311Phosphothreonine; by MAPK1 and MAPK31 Publication
    Modified residuei362 – 3621Phosphoserine; by MAPK1, MAPK3 and RPS6KA31 Publication
    Modified residuei374 – 3741Phosphoserine; by MAPK1 and MAPK32 Publications

    Post-translational modificationi

    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.By similarity
    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-232.2 Publications
    In quiescent cells, the small amount of FOS present is phosphorylated at Tyr-10 and Tyr-30 by SRC. This Tyr-phosphorylated form is cytosolic. In growing cells, dephosphorylated by PTPN2. Dephosphorylation leads to the association with endoplasmic reticulum membranes and activation of phospholipid synthesis.2 Publications

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP01100.
    PaxDbiP01100.
    PRIDEiP01100.

    PTM databases

    PhosphoSiteiP01100.

    Expressioni

    Developmental stagei

    Expressed at very low levels in quiescent cells. When cells are stimulated to reenter growth, they undergo 2 waves of expression, the first one peaks 7.5 minutes following FBS induction. At this stage, the protein is localized endoplasmic reticulum. The second wave of expression occurs at about 20 minutes after induction and peaks at 1 hour. At this stage, the protein becomes nuclear.1 Publication

    Gene expression databases

    ArrayExpressiP01100.
    BgeeiP01100.
    CleanExiHS_FOS.
    GenevestigatoriP01100.

    Organism-specific databases

    HPAiHPA018531.

    Interactioni

    Subunit structurei

    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. Interacts with CDS1 and PI4K2A By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    APPP050673EBI-852851,EBI-77613
    ATF2P153364EBI-852851,EBI-1170906
    CLUP109092EBI-852851,EBI-1104674
    COPS4Q9BT782EBI-852851,EBI-742413
    JUNP0541221EBI-852851,EBI-852823
    JUNBP172753EBI-852851,EBI-748062
    JUNDP175354EBI-852851,EBI-2682803
    ZNF133P527364EBI-852851,EBI-2687350

    Protein-protein interaction databases

    BioGridi108636. 84 interactions.
    DIPiDIP-1047N.
    IntActiP01100. 89 interactions.
    MINTiMINT-105814.
    STRINGi9606.ENSP00000306245.

    Structurei

    Secondary structure

    1
    380
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi141 – 19151

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A02X-ray2.70F138-193[»]
    1FOSX-ray3.05E/G139-200[»]
    1S9KX-ray3.10D140-192[»]
    DisProtiDP00078.
    ProteinModelPortaliP01100.
    SMRiP01100. Positions 138-200.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01100.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini137 – 20064bZIPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni139 – 15921Basic motif; required for the activation of phospholipid synthesis, but not for CDS1-bindingAdd
    BLAST
    Regioni165 – 19329Leucine-zipperPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the bZIP family. Fos subfamily.Curated
    Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG258795.
    HOGENOMiHOG000234334.
    HOVERGENiHBG005743.
    InParanoidiP01100.
    KOiK04379.
    OMAiTPTCTTY.
    OrthoDBiEOG7VTDN9.
    PhylomeDBiP01100.
    TreeFamiTF326301.

    Family and domain databases

    InterProiIPR004827. bZIP.
    IPR000837. Leuzip_Fos.
    [Graphical view]
    PfamiPF00170. bZIP_1. 1 hit.
    [Graphical view]
    PRINTSiPR00042. LEUZIPPRFOS.
    SMARTiSM00338. BRLZ. 1 hit.
    [Graphical view]
    PROSITEiPS50217. BZIP. 1 hit.
    PS00036. BZIP_BASIC. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P01100-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MMFSGFNADY EASSSRCSSA SPAGDSLSYY HSPADSFSSM GSPVNAQDFC    50
    TDLAVSSANF IPTVTAISTS PDLQWLVQPA LVSSVAPSQT RAPHPFGVPA 100
    PSAGAYSRAG VVKTMTGGRA QSIGRRGKVE QLSPEEEEKR RIRRERNKMA 150
    AAKCRNRRRE LTDTLQAETD QLEDEKSALQ TEIANLLKEK EKLEFILAAH 200
    RPACKIPDDL GFPEEMSVAS LDLTGGLPEV ATPESEEAFT LPLLNDPEPK 250
    PSVEPVKSIS SMELKTEPFD DFLFPASSRP SGSETARSVP DMDLSGSFYA 300
    ADWEPLHSGS LGMGPMATEL EPLCTPVVTC TPSCTAYTSS FVFTYPEADS 350
    FPSCAAAHRK GSSSNEPSSD SLSSPTLLAL 380
    Length:380
    Mass (Da):40,695
    Last modified:July 21, 1986 - v1
    Checksum:i9E3B2969347C90C8
    GO
    Isoform 2 (identifier: P01100-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-114: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:266
    Mass (Da):28,986
    Checksum:iC57F8C4E227FB777
    GO
    Isoform 3 (identifier: P01100-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         132-167: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:344
    Mass (Da):36,301
    Checksum:i5DD706220BEB00A1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti133 – 14412SPEEE…RRIRR → ISRRRREKENPK no nucleotide entry (PubMed:15489334)CuratedAdd
    BLAST

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 114114Missing in isoform 2. 1 PublicationVSP_055560Add
    BLAST
    Alternative sequencei132 – 16736Missing in isoform 3. 1 PublicationVSP_055561Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01512 Genomic DNA. Translation: CAA24756.1.
    K00650 Genomic DNA. Translation: AAA52471.1.
    AY212879 Genomic DNA. Translation: AAO21129.1.
    AK097379 mRNA. Translation: BAG53458.1.
    AK290907 mRNA. Translation: BAF83596.1.
    AK298659 mRNA. Translation: BAG60827.1.
    AF111167 Genomic DNA. Translation: AAC98315.1.
    CH471061 Genomic DNA. Translation: EAW81229.1.
    BC004490 mRNA. Translation: AAH04490.1.
    S65138 mRNA. Translation: AAB20306.1.
    CCDSiCCDS9841.1.
    PIRiA01342. TVHUF1.
    E34223.
    RefSeqiNP_005243.1. NM_005252.3.
    UniGeneiHs.25647.

    Genome annotation databases

    EnsembliENST00000303562; ENSP00000306245; ENSG00000170345. [P01100-1]
    ENST00000535987; ENSP00000442268; ENSG00000170345. [P01100-3]
    ENST00000555686; ENSP00000452590; ENSG00000170345. [P01100-2]
    GeneIDi2353.
    KEGGihsa:2353.
    UCSCiuc001xrn.3. human.

    Polymorphism databases

    DMDMi120470.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01512 Genomic DNA. Translation: CAA24756.1 .
    K00650 Genomic DNA. Translation: AAA52471.1 .
    AY212879 Genomic DNA. Translation: AAO21129.1 .
    AK097379 mRNA. Translation: BAG53458.1 .
    AK290907 mRNA. Translation: BAF83596.1 .
    AK298659 mRNA. Translation: BAG60827.1 .
    AF111167 Genomic DNA. Translation: AAC98315.1 .
    CH471061 Genomic DNA. Translation: EAW81229.1 .
    BC004490 mRNA. Translation: AAH04490.1 .
    S65138 mRNA. Translation: AAB20306.1 .
    CCDSi CCDS9841.1.
    PIRi A01342. TVHUF1.
    E34223.
    RefSeqi NP_005243.1. NM_005252.3.
    UniGenei Hs.25647.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A02 X-ray 2.70 F 138-193 [» ]
    1FOS X-ray 3.05 E/G 139-200 [» ]
    1S9K X-ray 3.10 D 140-192 [» ]
    DisProti DP00078.
    ProteinModelPortali P01100.
    SMRi P01100. Positions 138-200.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108636. 84 interactions.
    DIPi DIP-1047N.
    IntActi P01100. 89 interactions.
    MINTi MINT-105814.
    STRINGi 9606.ENSP00000306245.

    Chemistry

    BindingDBi P01100.
    ChEMBLi CHEMBL2111421.
    DrugBanki DB08813. Nadroparin.
    DB00852. Pseudoephedrine.

    PTM databases

    PhosphoSitei P01100.

    Polymorphism databases

    DMDMi 120470.

    Proteomic databases

    MaxQBi P01100.
    PaxDbi P01100.
    PRIDEi P01100.

    Protocols and materials databases

    DNASUi 2353.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000303562 ; ENSP00000306245 ; ENSG00000170345 . [P01100-1 ]
    ENST00000535987 ; ENSP00000442268 ; ENSG00000170345 . [P01100-3 ]
    ENST00000555686 ; ENSP00000452590 ; ENSG00000170345 . [P01100-2 ]
    GeneIDi 2353.
    KEGGi hsa:2353.
    UCSCi uc001xrn.3. human.

    Organism-specific databases

    CTDi 2353.
    GeneCardsi GC14P075745.
    HGNCi HGNC:3796. FOS.
    HPAi HPA018531.
    MIMi 164810. gene.
    neXtProti NX_P01100.
    Orphaneti 528. Berardinelli-Seip congenital lipodystrophy.
    PharmGKBi PA28212.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG258795.
    HOGENOMi HOG000234334.
    HOVERGENi HBG005743.
    InParanoidi P01100.
    KOi K04379.
    OMAi TPTCTTY.
    OrthoDBi EOG7VTDN9.
    PhylomeDBi P01100.
    TreeFami TF326301.

    Enzyme and pathway databases

    Reactomei REACT_163701. FCERI mediated MAPK activation.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_21326. Activation of the AP-1 family of transcription factors.
    SignaLinki P01100.

    Miscellaneous databases

    ChiTaRSi Fos. human.
    EvolutionaryTracei P01100.
    GeneWikii C-Fos.
    GenomeRNAii 2353.
    NextBioi 9543.
    PROi P01100.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P01100.
    Bgeei P01100.
    CleanExi HS_FOS.
    Genevestigatori P01100.

    Family and domain databases

    InterProi IPR004827. bZIP.
    IPR000837. Leuzip_Fos.
    [Graphical view ]
    Pfami PF00170. bZIP_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00042. LEUZIPPRFOS.
    SMARTi SM00338. BRLZ. 1 hit.
    [Graphical view ]
    PROSITEi PS50217. BZIP. 1 hit.
    PS00036. BZIP_BASIC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete nucleotide sequence of a human c-onc gene: deduced amino acid sequence of the human c-fos protein."
      van Straaten F., Mueller R., Curran T., Van Beveren C., Verma I.M.
      Proc. Natl. Acad. Sci. U.S.A. 80:3183-3187(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. NIEHS SNPs program
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
      Tissue: Colon.
    4. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Pancreas.
    7. "Retrovirus-mediated gene transfer of a human c-fos cDNA into mouse bone marrow stromal cells."
      Roux P., Verrier B., Klein B., Niccolino M., Marty L., Alexandre C., Piechaczyk M.
      Oncogene 6:2155-2160(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-6 (ISOFORM 1/2).
    8. "Transcription factor ATF cDNA clones: an extensive family of leucine zipper proteins able to selectively form DNA-binding heterodimers."
      Hai T., Liu F., Coukos W.J., Green M.R.
      Genes Dev. 3:2083-2090(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 133-200 (ISOFORM 1), DNA-BINDING, SUBUNIT.
    9. Erratum
      Hai T., Liu F., Coukos W.J., Green M.R.
      Genes Dev. 4:682-682(1990)
    10. "The basic region of Fos mediates specific DNA binding."
      Nakabeppu Y., Nathans D.
      EMBO J. 8:3833-3841(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING.
    11. "The Mos/MAP kinase pathway stabilizes c-Fos by phosphorylation and augments its transforming activity in NIH 3T3 cells."
      Okazaki K., Sagata N.
      EMBO J. 14:5048-5059(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-362 AND SER-374, FUNCTION, MUTAGENESIS OF SER-362 AND SER-374.
    12. "Smad3 and Smad4 cooperate with c-Jun/c-Fos to mediate TGF-beta-induced transcription."
      Zhang Y., Feng X.H., Derynck R.
      Nature 394:909-913(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION AS A COMPONENT OF THE SMAD3/SMAD4/JUN/FOS COMPLEX, FUNCTION, INTERACTION WITH SMAD3.
    13. "Molecular interpretation of ERK signal duration by immediate early gene products."
      Murphy L.O., Smith S., Chen R.H., Fingar D.C., Blenis J.
      Nat. Cell Biol. 4:556-564(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-325; THR-331 AND SER-374.
    14. Cited for: SUMOYLATION AT LYS-265, SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF LYS-128; LYS-192; LYS-265; THR-325; THR-331; SER-362 AND SER-374.
    15. "The proteomic reactor facilitates the analysis of affinity-purified proteins by mass spectrometry: application for identifying ubiquitinated proteins in human cells."
      Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M., Haines D.S., Figeys D.
      J. Proteome Res. 6:298-305(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-113.
      Tissue: Lung adenocarcinoma.
    16. "Ubc9 fusion-directed SUMOylation identifies constitutive and inducible SUMOylation."
      Jakobs A., Himstedt F., Funk M., Korn B., Gaestel M., Niedenthal R.
      Nucleic Acids Res. 35:E109-E109(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION.
    17. "N-Terminal c-Fos tyrosine phosphorylation regulates c-Fos/ER association and c-Fos-dependent phospholipid synthesis activation."
      Portal M.M., Ferrero G.O., Caputto B.L.
      Oncogene 26:3551-3558(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, PHOSPHORYLATION AT TYR-10 AND TYR-30, MUTAGENESIS OF TYR-10; TYR-30; TYR-106 AND TYR-337.
    18. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    19. "The kinase c-Src and the phosphatase TC45 coordinately regulate c-Fos tyrosine phosphorylation and c-Fos phospholipid synthesis activation capacity."
      Ferrero G.O., Velazquez F.N., Caputto B.L.
      Oncogene 31:3381-3391(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-10 AND TYR-30, MUTAGENESIS OF TYR-10 AND TYR-30.
    20. "Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA."
      Glover J.N., Harrison S.C.
      Nature 373:257-261(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 139-198 OF COMPLEX WITH JUN.

    Entry informationi

    Entry nameiFOS_HUMAN
    AccessioniPrimary (citable) accession number: P01100
    Secondary accession number(s): A8K4E2, B4DQ65, P18849
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 173 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3