FOS

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

DNA binding Source: UniProtKB-KW
transcription factor activity, sequence-specific DNA binding Source: InterPro

Complete GO annotation...

GO - Biological processⁱ

regulation of transcription from RNA polymerase II promoter Source: InterPro

Complete GO annotation...

Keywordsⁱ

Molecular function	DNA-binding

Molecular function

DNA-binding

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Proto-oncogene c-Fos Alternative name(s): Cellular oncogene fos
Gene namesⁱ	Name:FOS
Organismⁱ	Sus scrofa (Pig)
Taxonomic identifierⁱ	9823 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus
Proteomesⁱ	UP000008227 Componentⁱ: Unplaced

Subcellular locationⁱ

Nucleus
PROSITE-ProRule annotation
Manual assertion according to rulesⁱ
- PROSITE-ProRule:PRU00978
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

cytosol Source: UniProtKB-SubCell
endoplasmic reticulum Source: UniProtKB-SubCell
nucleus Source: UniProtKB-SubCell
transcription factor complex Source: InterPro

Complete GO annotation...

Keywords - Cellular componentⁱ

Cytoplasm, Endoplasmic reticulum, Nucleus

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

Proto-oncogene

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000076468	1 – 380	Proto-oncogene c-FosAdd BLAST		380

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	10	Phosphotyrosine; by SRCBy similarity	1
Modified residueⁱ	30	Phosphotyrosine; by SRCBy similarity	1
Cross-linkⁱ	113	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linkⁱ	128	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residueⁱ	232	PhosphothreonineBy similarity	1
Cross-linkⁱ	265	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linkⁱ	265	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residueⁱ	325	Phosphothreonine; by MAPK1 and MAPK3By similarity	1
Modified residueⁱ	331	Phosphothreonine; by MAPK1 and MAPK3By similarity	1
Modified residueⁱ	362	Phosphoserine; by MAPK1, MAPK3 and RPS6KA3By similarity	1
Modified residueⁱ	374	Phosphoserine; by MAPK1 and MAPK3By similarity	1

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

PaxDbⁱ	O97930.
PeptideAtlas More...PeptideAtlasⁱ	O97930.
PRIDEⁱ	O97930.

Expressionⁱ

Gene expression databases

Genevisibleⁱ	O97930. SS.

Genevisibleⁱ

O97930. 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

STRINGⁱ	9823.ENSSSCP00000002583.

STRINGⁱ

9823.ENSSSCP00000002583.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	O97930.
SMRⁱ	O97930.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	137 – 200	bZIPPROSITE-ProRule annotationAdd BLAST		64

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	139 – 159	Basic motif; required for the activation of phospholipid synthesis, but not for CDS1-bindingPROSITE-ProRule annotationAdd BLAST		21
Regionⁱ	165 – 193	Leucine-zipperPROSITE-ProRule annotationAdd BLAST		29

Sequence similaritiesⁱ

Belongs to the bZIP family. Fos subfamily.Curated

Phylogenomic databases

eggNOGⁱ	KOG1414. Eukaryota. ENOG4111CH5. LUCA.
HOGENOMⁱ	HOG000234334.
HOVERGENⁱ	HBG005743.
InParanoidⁱ	O97930.
KEGG Orthology (KO) More...KOⁱ	K04379.
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0GGW.
TreeFamⁱ	TF326301.

Family and domain databases

InterProⁱ	View protein in InterPro IPR000837. AP-1. IPR004827. bZIP. IPR029816. c-Fos/v-Fos.
PANTHERⁱ	PTHR23351. PTHR23351. 1 hit. PTHR23351:SF31. PTHR23351:SF31. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00170. bZIP_1. 1 hit.
PRINTSⁱ	PR00042. LEUZIPPRFOS.
SMARTⁱ	View protein in SMART SM00338. BRLZ. 1 hit.
PROSITEⁱ	View protein in PROSITE PS50217. BZIP. 1 hit. PS00036. BZIP_BASIC. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

O97930-1 [UniParc]FASTA Add 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 key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	58	V → A in CAB40144 (Ref. 2) Curated	1
Sequence conflictⁱ	69	I → T in CAB40144 (Ref. 2) Curated	1
Sequence conflictⁱ	111	A → V in CAB40144 (Ref. 2) Curated	1
Sequence conflictⁱ	258	K → N in CAB40144 (Ref. 2) Curated	1
Sequence conflictⁱ	336	A → T in CAB40144 (Ref. 2) Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	Y14808 Genomic DNA. Translation: CAB39278.1. AJ132510 Genomic DNA. Translation: CAB40144.1.
NCBI Reference Sequences More...RefSeqⁱ	NP_001116585.1. NM_001123113.1.
UniGeneⁱ	Ssc.1555.

Genome annotation databases

GeneIDⁱ	100144486.
KEGGⁱ	ssc:100144486.

Similar proteinsⁱ

Entry	Cluster members	Organisms	Length	Cluster ID	Cluster name	Size
O97930	P12841 Q5U874 Q5G6W3 Q5G6W2 M3YCL9 M1EMS4 Q5U7E3 Q5XQC6 Q3HL95 UPI0003C90382 +117	Rattus norvegicus (Rat) Mustela putorius furo (European domestic ferret) (Mustela furo) Felis catus (Cat) (Felis silvestris catus) Tupaia chinensis (Chinese tree shrew) Peromyscus maniculatus bairdii (prairie deer mouse) Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) Phodopus campbelli (Campbell's dwarf Russian hamster) Phodopus sungorus (Striped hairy-footed hamster) (Djungarian hamster) Phodopus roborovskii (Roborovski's desert hamster) (Cricetulus roborovskii) Panthera pardus (Leopard) (Felis pardus) And more	380	UniRef90_P12841	Cluster: Proto-oncogene c-Fos	128

Entry	Cluster members	Organisms	Length	Cluster ID	Cluster name	Size
O97930	P12841 Q5U874 Q5G6W3 Q5G6W2 M3YCL9 M1EMS4 Q5U7E3 Q5XQC6 Q3HL95 UPI0003C90382 +127	Rattus norvegicus (Rat) Mustela putorius furo (European domestic ferret) (Mustela furo) Felis catus (Cat) (Felis silvestris catus) Tupaia chinensis (Chinese tree shrew) Peromyscus maniculatus bairdii (prairie deer mouse) Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi coquereli) Phodopus campbelli (Campbell's dwarf Russian hamster) Phodopus sungorus (Striped hairy-footed hamster) (Djungarian hamster) Jaculus jaculus (Lesser Egyptian jerboa) Panthera pardus (Leopard) (Felis pardus) And more	380	UniRef50_P12841	Cluster: Proto-oncogene c-Fos	138

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.
NCBI Reference Sequences More...RefSeqⁱ	NP_001116585.1. NM_001123113.1.
UniGeneⁱ	Ssc.1555.

3D structure databases

ProteinModelPortalⁱ	O97930.
SMRⁱ	O97930.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

STRINGⁱ	9823.ENSSSCP00000002583.

STRINGⁱ

9823.ENSSSCP00000002583.

Proteomic databases

PaxDbⁱ	O97930.
PeptideAtlas More...PeptideAtlasⁱ	O97930.
PRIDEⁱ	O97930.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

GeneIDⁱ	100144486.
KEGGⁱ	ssc:100144486.

Organism-specific databases

CTDⁱ	2353.

CTDⁱ

2353.

Phylogenomic databases

eggNOGⁱ	KOG1414. Eukaryota. ENOG4111CH5. LUCA.
HOGENOMⁱ	HOG000234334.
HOVERGENⁱ	HBG005743.
InParanoidⁱ	O97930.
KEGG Orthology (KO) More...KOⁱ	K04379.
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0GGW.
TreeFamⁱ	TF326301.

Gene expression databases

Genevisibleⁱ	O97930. SS.

Genevisibleⁱ

O97930. SS.

Family and domain databases

InterProⁱ	View protein in InterPro IPR000837. AP-1. IPR004827. bZIP. IPR029816. c-Fos/v-Fos.
PANTHERⁱ	PTHR23351. PTHR23351. 1 hit. PTHR23351:SF31. PTHR23351:SF31. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00170. bZIP_1. 1 hit.
PRINTSⁱ	PR00042. LEUZIPPRFOS.
SMARTⁱ	View protein in SMART SM00338. BRLZ. 1 hit.
PROSITEⁱ	View protein in PROSITE PS50217. BZIP. 1 hit. PS00036. BZIP_BASIC. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	FOS_PIG
Accessionⁱ	O97930Primary (citable) accession number: O97930
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 21, 2003
	Last sequence update:	May 1, 2000
	Last modified:	August 30, 2017
	This is version 109 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

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UniProtKB - O97930 (FOS_PIG)

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Proto-oncogene c-Fos

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ