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UniProtKB - O97930 (FOS_PIG)

UniProt

O97930 - FOS_PIG

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Protein

Proto-oncogene c-Fos

Gene

FOS

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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

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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation
  • Endoplasmic reticulum By similarity
  • Cytoplasm › cytosol 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_0000076468Add
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

PaxDbiO97930.
PeptideAtlasiO97930.

Expressioni

Gene expression databases

BgeeiENSSSCG00000002383.
GenevisibleiO97930. SS.

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 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

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000002583.

Structurei

3D structure databases

ProteinModelPortaliO97930.
SMRiO97930. 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.
HOGENOMiHOG000234334.
HOVERGENiHBG005743.
InParanoidiO97930.
KOiK04379.
OrthoDBiEOG091G0GGW.
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]

Sequencei

Sequence statusi: Complete.

O97930-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMFSGFNADY EASSSRCSSA SPAGDSLSYY HSPADSFSSM GSPVNAQDFC 
        60         70         80         90        100
TDLAVSSVNF IPTVTAISIS PDLQWLVQPT LVSSVAPSQT RAPHPYGVPT 
       110        120        130        140        150
PSAGAYSRAG AVKTMPGGRA 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
PSVEPVKKVS SMELKAEPFD DFLFPASSRP GGSETARSVP DMDLSGSFYA 
       310        320        330        340        350
ADWEPLHGGS LGMGPMATEL EPLCTPVVTC TPSCTAYTSS FVFTYPEADS 
       360        370        380
FPSCAAAHRK GSSSNEPSSD SLSSPTLLAL
Length:380
Mass (Da):40,674
Last modified:May 1, 2000 - v2
Checksum:i33EEF3C4475599A8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti58 – 581V → A in CAB40144 (Ref. 2) Curated
Sequence conflicti69 – 691I → T in CAB40144 (Ref. 2) Curated
Sequence conflicti111 – 1111A → V in CAB40144 (Ref. 2) Curated
Sequence conflicti258 – 2581K → N in CAB40144 (Ref. 2) Curated
Sequence conflicti336 – 3361A → T in CAB40144 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y14808 Genomic DNA. Translation: CAB39278.1.
AJ132510 Genomic DNA. Translation: CAB40144.1.
RefSeqiNP_001116585.1. NM_001123113.1.
UniGeneiSsc.1555.

Genome annotation databases

GeneIDi100144486.
KEGGissc:100144486.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y14808 Genomic DNA. Translation: CAB39278.1.
AJ132510 Genomic DNA. Translation: CAB40144.1.
RefSeqiNP_001116585.1. NM_001123113.1.
UniGeneiSsc.1555.

3D structure databases

ProteinModelPortaliO97930.
SMRiO97930. Positions 140-192.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000002583.

Proteomic databases

PaxDbiO97930.
PeptideAtlasiO97930.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100144486.
KEGGissc:100144486.

Organism-specific databases

CTDi2353.

Phylogenomic databases

eggNOGiKOG1414. Eukaryota.
ENOG4111CH5. LUCA.
HOGENOMiHOG000234334.
HOVERGENiHBG005743.
InParanoidiO97930.
KOiK04379.
OrthoDBiEOG091G0GGW.
TreeFamiTF326301.

Gene expression databases

BgeeiENSSSCG00000002383.
GenevisibleiO97930. SS.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiFOS_PIG
AccessioniPrimary (citable) accession number: O97930
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 21, 2003
Last sequence update: May 1, 2000
Last modified: September 7, 2016
This is version 101 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.