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P01100

- FOS_HUMAN

UniProt

P01100 - FOS_HUMAN

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Protein

Proto-oncogene c-Fos

Gene

FOS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. RNA polymerase II core promoter sequence-specific DNA binding Source: Ensembl
  3. R-SMAD binding Source: BHF-UCL
  4. sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  5. 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
Complete GO annotation...

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. endoplasmic reticulum Source: UniProtKB-KW
  2. membrane Source: Ensembl
  3. neuron projection Source: Ensembl
  4. nucleoplasm Source: Reactome
  5. nucleus Source: HPA
  6. transcription factor complex Source: Ensembl
Complete GO annotation...

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

BgeeiP01100.
CleanExiHS_FOS.
ExpressionAtlasiP01100. baseline and differential.
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. 91 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.
GeneTreeiENSGT00730000110541.
HOGENOMiHOG000234334.
HOVERGENiHBG005743.
InParanoidiP01100.
KOiK04379.
OMAiTPTCTTY.
OrthoDBiEOG7VTDN9.
PhylomeDBiP01100.
TreeFamiTF326301.

Family and domain databases

InterProiIPR000837. AP-1.
IPR004827. bZIP.
[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

        10         20         30         40         50
MMFSGFNADY EASSSRCSSA SPAGDSLSYY HSPADSFSSM GSPVNAQDFC
60 70 80 90 100
TDLAVSSANF IPTVTAISTS PDLQWLVQPA LVSSVAPSQT RAPHPFGVPA
110 120 130 140 150
PSAGAYSRAG VVKTMTGGRA QSIGRRGKVE QLSPEEEEKR RIRRERNKMA
160 170 180 190 200
AAKCRNRRRE LTDTLQAETD QLEDEKSALQ TEIANLLKEK EKLEFILAAH
210 220 230 240 250
RPACKIPDDL GFPEEMSVAS LDLTGGLPEV ATPESEEAFT LPLLNDPEPK
260 270 280 290 300
PSVEPVKSIS SMELKTEPFD DFLFPASSRP SGSETARSVP DMDLSGSFYA
310 320 330 340 350
ADWEPLHSGS LGMGPMATEL EPLCTPVVTC TPSCTAYTSS FVFTYPEADS
360 370 380
FPSCAAAHRK GSSSNEPSSD SLSSPTLLAL
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. [P01100-1]
PIRiA01342. TVHUF1.
E34223.
RefSeqiNP_005243.1. NM_005252.3. [P01100-1]
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. [P01100-1]

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. [P01100-1 ]
PIRi A01342. TVHUF1.
E34223.
RefSeqi NP_005243.1. NM_005252.3. [P01100-1 ]
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. 91 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. [P01100-1 ]

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.
GeneTreei ENSGT00730000110541.
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 35464113.
PROi P01100.
SOURCEi Search...

Gene expression databases

Bgeei P01100.
CleanExi HS_FOS.
ExpressionAtlasi P01100. baseline and differential.
Genevestigatori P01100.

Family and domain databases

InterProi IPR000837. AP-1.
IPR004827. bZIP.
[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

« Hide 'large scale' publications
  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 29, 2014
This is version 174 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