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Protein

Proto-oncogene c-Fos

Gene

FOS

Organism
Ovis aries (Sheep)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. 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 (By similarity). In growing cells, activates phospholipid synthesis, possibly by activating CDS1 and PI4K2A. This activity requires Tyr-dephosphorylation and association with the endoplasmic reticulum (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Proto-oncogene c-Fos
Alternative name(s):
Cellular oncogene fos
Gene namesi
Name:FOS
OrganismiOvis aries (Sheep)
Taxonomic identifieri9940 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis
Proteomesi
  • UP000002356 Componenti: Unplaced

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation
  • Endoplasmic reticulum By similarity
  • Cytoplasmcytosol By similarity

  • 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 Tyr-dephosphorylation (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›195›195Proto-oncogene c-FosPRO_0000076470Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei88 – 881PhosphothreonineBy similarity
Cross-linki121 – 121Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki121 – 121Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei181 – 1811Phosphothreonine; by MAPK1 and MAPK3By similarity
Modified residuei187 – 1871Phosphothreonine; by MAPK1 and MAPK3By similarity

Post-translational modificationi

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-88 (By similarity).By similarity
In quiescent cells, the small amount of FOS present is phosphorylated 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 (By similarity).By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Expressioni

Inductioni

Expression increases upon a variety of stimuli, including growth factors, cytokines, neurotransmitters, polypeptide hormones, stress and cell injury.

Interactioni

Subunit structurei

Heterodimer; with JUN (By similarity). Component of the SMAD3/SMAD4/JUN/FOS complex required for synergistic TGF-beta-mediated transcription at the AP1 promoter site. Interacts with SMAD3; the interaction is weak even on TGF-beta activation. Interacts with DSIPI; this interaction inhibits the binding of active AP1 to its target DNA. Interacts with MAFB (By similarity). Interacts with CDS1 and PI4K2A (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliO02761.
SMRiO02761. Positions 1-48.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 5656bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni‹1 – 15›15Basic motif; required for the activation of phospholipid synthesis, but not for CDS1-bindingPROSITE-ProRule annotationAdd
BLAST
Regioni21 – 4929Leucine-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

HOVERGENiHBG005743.

Family and domain databases

InterProiIPR000837. AP-1.
IPR004827. bZIP.
IPR029816. c-Fos/v-Fos.
[Graphical view]
PANTHERiPTHR23351. PTHR23351. 1 hit.
PTHR23351:SF4. PTHR23351:SF4. 1 hit.
PfamiPF00170. bZIP_1. 1 hit.
[Graphical view]
PRINTSiPR00042. LEUZIPPRFOS.
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

O02761-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ERNKMAAAKC RNRRRELTDT LQAETDQLED EKSALQTEIA NLLKEKEKLE
60 70 80 90 100
FILAAHRPAC KIPDDLGFPE EMSVASLDLS GGLPEAATPE SEEAFTLPLL
110 120 130 140 150
NDPEPKPSLE PVKSISNVEL KAEPFDDFLF PASSRPSGSE TSRSVPDVDL
160 170 180 190
SGSFYAADWE PLHSNSLGMG PMVTELEPLC TPVVTCTPGC TTYTS
Length:195
Mass (Da):21,255
Last modified:May 30, 2000 - v2
Checksum:i7ED1084BA002848B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei195 – 1951

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y15747 Genomic DNA. Translation: CAA75757.1.
U94719 mRNA. Translation: AAB57839.1.
UniGeneiOar.1016.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y15747 Genomic DNA. Translation: CAA75757.1.
U94719 mRNA. Translation: AAB57839.1.
UniGeneiOar.1016.

3D structure databases

ProteinModelPortaliO02761.
SMRiO02761. Positions 1-48.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG005743.

Family and domain databases

InterProiIPR000837. AP-1.
IPR004827. bZIP.
IPR029816. c-Fos/v-Fos.
[Graphical view]
PANTHERiPTHR23351. PTHR23351. 1 hit.
PTHR23351:SF4. PTHR23351:SF4. 1 hit.
PfamiPF00170. bZIP_1. 1 hit.
[Graphical view]
PRINTSiPR00042. LEUZIPPRFOS.
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFOS_SHEEP
AccessioniPrimary (citable) accession number: O02761
Secondary accession number(s): O97787
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 30, 2000
Last modified: October 14, 2015
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.