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Protein

Proto-oncogene c-Fos

Gene

FOS

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 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

Enzyme and pathway databases

ReactomeiR-BTA-2559580. Oxidative Stress Induced Senescence.
R-BTA-2871796. FCERI mediated MAPK activation.
R-BTA-450341. Activation of the AP-1 family of transcription factors.

Names & Taxonomyi

Protein namesi
Recommended name:
Proto-oncogene c-Fos
Alternative name(s):
Cellular oncogene fos
Gene namesi
Name:FOS
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 10

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 dephosphorylation at Tyr-10 and Tyr-30 (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
Chaini1 – 380380Proto-oncogene c-FosPRO_0000076462Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei10 – 101Phosphotyrosine; by SRCBy similarity
Modified residuei30 – 301Phosphotyrosine; by SRCBy similarity
Cross-linki113 – 113Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki128 – 128Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei232 – 2321PhosphothreonineBy similarity
Cross-linki265 – 265Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki265 – 265Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei325 – 3251Phosphothreonine; by MAPK1 and MAPK3By similarity
Modified residuei331 – 3311Phosphothreonine; by MAPK1 and MAPK3By similarity
Modified residuei362 – 3621Phosphoserine; by MAPK1, MAPK3 and RPS6KA3By similarity
Modified residuei374 – 3741Phosphoserine; by MAPK1 and MAPK3By similarity

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 (By similarity).By similarity
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 (By similarity).By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO77628.
PRIDEiO77628.

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-binding 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 MAFB (By similarity). Interacts with CDS1 and PI4K2A (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000005660.

Structurei

3D structure databases

ProteinModelPortaliO77628.
SMRiO77628. Positions 140-192.
ModBaseiSearch...
MobiDBiSearch...

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-bindingPROSITE-ProRule annotationAdd
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

eggNOGiKOG1414. Eukaryota.
ENOG4111CH5. LUCA.
GeneTreeiENSGT00730000110541.
HOGENOMiHOG000234334.
HOVERGENiHBG005743.
InParanoidiO77628.
KOiK04379.
OMAiDWEPLYT.
OrthoDBiEOG7VTDN9.
TreeFamiTF326301.

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.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O77628-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMFSGFNADY EASSSRCSSA SPAGDSLSYY HSPADSFSSM GSPVNAQDYC
60 70 80 90 100
TDLAVSSANF IPTVTAISTS PDLQWLVQPT LVSSVAPSQT RAPHPYGVPT
110 120 130 140 150
PSAGAYSRAG VMKTMTGGRA QSIGRRGKVE QLSPEEEEKR RIRRERNKMA
160 170 180 190 200
AAKCRNRRRE LTDTLQAETD QLEDEKSALQ TEIANLLKEK EKLEFILAAH
210 220 230 240 250
RPACKIPDDL GFPEEMSVAS LDLSGGLPEA ATPESEEAFT LPLLNDPEPK
260 270 280 290 300
PSVEPVKSVG SMELKAEPFD DYMFPASSRP SGSETARSVP DMDLSGSFYA
310 320 330 340 350
ADWEPLHGGS LGMGPMATEL EPLCTPVVTC TPSCTTYTSS FVFTYPEADS
360 370 380
FPSCAAAHRK GSSSNEPSSD SLSSPTLLAL
Length:380
Mass (Da):40,737
Last modified:September 27, 2005 - v2
Checksum:i44AE951257F292B0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti268 – 2681P → L in AAC21577 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY322482 mRNA. Translation: AAP84343.1.
BT029837 mRNA. Translation: ABM21549.1.
BC118280 mRNA. Translation: AAI18281.1.
AF069515 mRNA. Translation: AAC21577.1.
RefSeqiNP_877587.1. NM_182786.2.
UniGeneiBt.52605.

Genome annotation databases

EnsembliENSBTAT00000005660; ENSBTAP00000005660; ENSBTAG00000004322.
GeneIDi280795.
KEGGibta:280795.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY322482 mRNA. Translation: AAP84343.1.
BT029837 mRNA. Translation: ABM21549.1.
BC118280 mRNA. Translation: AAI18281.1.
AF069515 mRNA. Translation: AAC21577.1.
RefSeqiNP_877587.1. NM_182786.2.
UniGeneiBt.52605.

3D structure databases

ProteinModelPortaliO77628.
SMRiO77628. Positions 140-192.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000005660.

Proteomic databases

PaxDbiO77628.
PRIDEiO77628.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000005660; ENSBTAP00000005660; ENSBTAG00000004322.
GeneIDi280795.
KEGGibta:280795.

Organism-specific databases

CTDi2353.

Phylogenomic databases

eggNOGiKOG1414. Eukaryota.
ENOG4111CH5. LUCA.
GeneTreeiENSGT00730000110541.
HOGENOMiHOG000234334.
HOVERGENiHBG005743.
InParanoidiO77628.
KOiK04379.
OMAiDWEPLYT.
OrthoDBiEOG7VTDN9.
TreeFamiTF326301.

Enzyme and pathway databases

ReactomeiR-BTA-2559580. Oxidative Stress Induced Senescence.
R-BTA-2871796. FCERI mediated MAPK activation.
R-BTA-450341. Activation of the AP-1 family of transcription factors.

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.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of c-Fos proto-oncogene in Korean native cattle (Hanwoo)."
    Yu S.L., Chung H.J., Jung K.C., Choi J.G., Na K.J., Lee J.H., Sang B.C.
    Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Fetal skin.
  4. "Stimulation of c-fos and c-jun mRNA in bovine luteal cells."
    Davis J.S., Fong H.W., Westfall S.W.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 165-290.
    Tissue: Brain.

Entry informationi

Entry nameiFOS_BOVIN
AccessioniPrimary (citable) accession number: O77628
Secondary accession number(s): A1L550, Q17QM0, Q7YRP7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: September 27, 2005
Last modified: July 6, 2016
This is version 112 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.