FOS

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

Manual assertion based on experiment inⁱ

Ref.10
"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.
Ref.11
"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.
Ref.13
"Down-regulation of c-Fos/c-Jun AP-1 dimer activity by sumoylation."
Bossis G., Malnou C.E., Farras R., Andermarcher E., Hipskind R., Rodriguez M., Schmidt D., Muller S., Jariel-Encontre I., Piechaczyk M.
Mol. Cell. Biol. 25:6964-6979(2005) [PubMed] [Europe PMC] [Abstract]
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.
Ref.15
"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.
Ref.17
"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.

GO - Molecular functionⁱ

chromatin binding Source: Ensembl
DNA-binding transcription factor activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 9732876
protein heterodimerization activity
Source: CAFA
Inferred from direct assayⁱ
- 10508860
RNA polymerase II activating transcription factor binding
Source: CAFA
Inferred from physical interactionⁱ
- 10508860
RNA polymerase II core promoter sequence-specific DNA binding
Source: CAFA
Inferred from mutant phenotypeⁱ
- 10704222
RNA polymerase II proximal promoter sequence-specific DNA binding Source: Ensembl
RNA polymerase II transcription factor activity, sequence-specific DNA binding Source: NTNU_SB
R-SMAD binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 9732876
transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding Source: Ensembl
transcription factor binding
Source: ParkinsonsUK-UCL
Inferred from physical interactionⁱ
- 10523647
transcription regulatory region DNA binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 9732876

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

aging Source: Ensembl
cellular response to cadmium ion
Source: CAFA
Inferred from mutant phenotypeⁱ
- 26514923
cellular response to calcium ion Source: Ensembl
cellular response to extracellular stimulus Source: Ensembl
cellular response to hormone stimulus Source: Ensembl
cellular response to reactive oxygen species
Source: BHF-UCL
Inferred from direct assayⁱ
- 17217916
conditioned taste aversion Source: Ensembl
cytokine-mediated signaling pathway Source: Reactome
DNA methylation
Source: ProtInc
Traceable author statementⁱ
- 9888853
Fc-epsilon receptor signaling pathway Source: Reactome
female pregnancy Source: Ensembl
inflammatory response
Source: ProtInc
Traceable author statementⁱ
- 9443941
nervous system development Source: Ensembl
positive regulation of neuron death Source: ARUK-UCL
positive regulation of osteoclast differentiation Source: Ensembl
positive regulation of pri-miRNA transcription by RNA polymerase II Source: BHF-UCL
positive regulation of transcription, DNA-templated
Source: BHF-UCL
Inferred from direct assayⁱ
- 9732876
positive regulation of transcription by RNA polymerase II
Source: CAFA
Inferred from direct assayⁱ
- 10508860
regulation of DNA-binding transcription factor activity Source: Reactome
regulation of transcription by RNA polymerase II
Source: ProtInc
Traceable author statementⁱ
- 10918580
response to cAMP Source: Ensembl
response to cold Source: Ensembl
response to corticosterone Source: Ensembl
response to gravity Source: Ensembl
response to immobilization stress Source: Ensembl
response to light stimulus Source: Ensembl
response to lipopolysaccharide Source: Ensembl
response to muscle stretch Source: Ensembl
response to progesterone Source: Ensembl
response to toxic substance Source: Ensembl
skeletal muscle cell differentiation Source: Ensembl
sleep Source: Ensembl
SMAD protein signal transduction
Source: BHF-UCL
Inferred from direct assayⁱ
- 9732876
transcription by RNA polymerase II
Source: ProtInc
Traceable author statementⁱ
- 10918580
transforming growth factor beta receptor signaling pathway
Source: BHF-UCL
Inferred from direct assayⁱ
- 9732876

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	DNA-binding

Molecular function

DNA-binding

Enzyme and pathway databases

Reactomeⁱ	R-HSA-2559580 Oxidative Stress Induced Senescence R-HSA-2559582 Senescence-Associated Secretory Phenotype (SASP) R-HSA-2871796 FCERI mediated MAPK activation R-HSA-450341 Activation of the AP-1 family of transcription factors R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling R-HSA-6796648 TP53 Regulates Transcription of DNA Repair Genes R-HSA-9018519 Estrogen-dependent gene expression
SignaLinkⁱ	P01100
SIGNORⁱ	P01100

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
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [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 › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 14

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000170345.9
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:3796 FOS
MIMⁱ	164810 gene
neXtProtⁱ	NX_P01100

Keywords - Cellular componentⁱ

Cytoplasm, Endoplasmic reticulum, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	10	Y → E: Loss of activation of phospholipid synthesis; when associated with E-30. 2 Publications	1
Mutagenesisⁱ	10	Y → 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	1
Mutagenesisⁱ	30	Y → E: Loss of activation of phospholipid synthesis; when associated with E-10. 2 Publications	1
Mutagenesisⁱ	30	Y → 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	1
Mutagenesisⁱ	106	Y → F: No effect on Tyr-phosphorylation. Loss of endoplasmic reticulum localization in quiescent cells. 1 Publication	1
Mutagenesisⁱ	128	K → R: No change in sumoylation. 1 Publication	1
Mutagenesisⁱ	192	K → R: No change in sumoylation. 1 Publication	1
Mutagenesisⁱ	232	T → D: Decreased sumoylation levels.	1
Mutagenesisⁱ	265	K → R: Abolishes sumoylation. No change in nuclear location nor on protein stability. Increased AP1 transactivation activity when heterodimerized with cJUN. 1 Publication	1
Mutagenesisⁱ	325	T → D: No change in sumoylation levels. 1 Publication	1
Mutagenesisⁱ	331	T → D: No change in sumoylation levels. 1 Publication	1
Mutagenesisⁱ	337	Y → F: No effect on Tyr-phosphorylation. Loss of endoplasmic reticulum localization in quiescent cells. 1 Publication	1
Mutagenesisⁱ	362	S → A: Loss of protein stability. Reduced MOS/MAPK-mediated transforming ability; when associated with A-374. 2 Publications	1
Mutagenesisⁱ	362	S → D: Increased protein stability. Increased MOS/MAPK-mediated transforming ability and no change in sumoylation levels; when associated with D-374. 2 Publications	1
Mutagenesisⁱ	374	S → A: No change in sumoylation levels. Loss of protein stability. Reduced MOS/MAPK-mediated transforming ability; when associated with A-362. 2 Publications	1
Mutagenesisⁱ	374	S → D: Increased protein stability. Increased MOS/MAPK-mediated transforming ability and no change in sumoylation levels; when associated with D-362. 2 Publications	1

Keywords - Diseaseⁱ

Proto-oncogene

Organism-specific databases

DisGeNET More...DisGeNETⁱ	2353
Open Targets More...OpenTargetsⁱ	ENSG00000170345
Orphanetⁱ	528 Berardinelli-Seip congenital lipodystrophy
PharmGKBⁱ	PA28212

Chemistry databases

ChEMBLⁱ	CHEMBL2111421
Drug and drug target database More...DrugBankⁱ	DB08813 Nadroparin DB00852 Pseudoephedrine

Polymorphism and mutation databases

BioMutaⁱ	FOS
DMDMⁱ	120470

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000076465	1 – 380	Proto-oncogene c-FosAdd BLAST		380

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	10	Phosphotyrosine; by SRC2 Publications	1
Modified residueⁱ	30	Phosphotyrosine; by SRC2 Publications	1
Cross-linkⁱ	113	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linkⁱ	128	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residueⁱ	232	PhosphothreonineBy similarity	1
Cross-linkⁱ	265	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residueⁱ	325	Phosphothreonine; by MAPK1 and MAPK31 Publication	1
Modified residueⁱ	331	Phosphothreonine; by MAPK1 and MAPK31 Publication	1
Modified residueⁱ	362	Phosphoserine; by MAPK1, MAPK3 and RPS6KA31 Publication	1
Modified residueⁱ	374	Phosphoserine; by MAPK1 and MAPK32 Publications	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-232.2 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

EPDⁱ	P01100
PaxDbⁱ	P01100
PeptideAtlas More...PeptideAtlasⁱ	P01100
PRIDEⁱ	P01100
ProteomicsDBⁱ	51317

PTM databases

iPTMnetⁱ	P01100
PhosphoSitePlusⁱ	P01100

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

Bgeeⁱ	ENSG00000170345 Expressed in 237 organ(s), highest expression level in mucosa of stomach
CleanExⁱ	HS_FOS
ExpressionAtlasⁱ	P01100 baseline and differential
Genevisibleⁱ	P01100 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA018531

HPAⁱ

HPA018531

Interactionⁱ

Subunit structureⁱ

Heterodimer; with JUN (By similarity). Interacts with MAFB (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 CDS1 and PI4K2A (By similarity).By similarity

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
APP	P05067	3	EBI-852851,EBI-77613
ATF2	P15336	9	EBI-852851,EBI-1170906
ATF4	P18848	3	EBI-852851,EBI-492498
ATF7	P17544	4	EBI-852851,EBI-765623
CLU	P10909	2	EBI-852851,EBI-1104674
COPS4	Q9BT78	2	EBI-852851,EBI-742413
JUN	P05412	36	EBI-852851,EBI-852823
JUNB	P17275	8	EBI-852851,EBI-748062
JUND	P17535	9	EBI-852851,EBI-2682803
Maz	P56671	2	EBI-852851,EBI-1809712	From Mus musculus.
MECOM	Q03112	4	EBI-852851,EBI-1384862
PPP1R12A	O14974	2	EBI-852851,EBI-351726
STAT1	P42224	6	EBI-852851,EBI-1057697
TCL1A	P56279	4	EBI-852851,EBI-749995
ZNF133	P52736	4	EBI-852851,EBI-2687350

GO - Molecular functionⁱ

protein heterodimerization activity
Source: CAFA
Inferred from direct assayⁱ
- 10508860
RNA polymerase II activating transcription factor binding
Source: CAFA
Inferred from physical interactionⁱ
- 10508860
R-SMAD binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 9732876
transcription factor binding
Source: ParkinsonsUK-UCL
Inferred from physical interactionⁱ
- 10523647

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	108636, 135 interactors
ComplexPortalⁱ	CPX-480 AP-1 transcription factor complex FOS-JUN-NFATC2 CPX-486 AP-1 transcription factor complex FOS-JUN
CORUMⁱ	P01100
Database of interacting proteins More...DIPⁱ	DIP-1047N
ELMⁱ	P01100
IntActⁱ	P01100, 143 interactors
Molecular INTeraction database More...MINTⁱ	P01100
STRINGⁱ	9606.ENSP00000306245

Chemistry databases

BindingDBⁱ

P01100

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Helixⁱ	141 – 191	Combined sources		51

Show more details

3D structure databases

Database of protein disorder More...DisProtⁱ	DP00078
ProteinModelPortalⁱ	P01100
SMRⁱ	P01100
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P01100

EvolutionaryTraceⁱ

P01100

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-bindingAdd 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
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00730000110541
HOGENOMⁱ	HOG000234334
HOVERGENⁱ	HBG005743
InParanoidⁱ	P01100
KEGG Orthology (KO) More...KOⁱ	K04379
OMAⁱ	HRPACKM
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0GGW
PhylomeDBⁱ	P01100
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:SF4 PTHR23351:SF4, 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

Sequences (3+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 3 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 3 described isoforms and 6 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: P01100-1) [UniParc]FASTA Add 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]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-114: Missing.

« Hide

        10         20         30         40         50
MTGGRAQSIG RRGKVEQLSP EEEEKRRIRR ERNKMAAAKC RNRRRELTDT 
        60         70         80         90        100
LQAETDQLED EKSALQTEIA NLLKEKEKLE FILAAHRPAC KIPDDLGFPE 
       110        120        130        140        150
EMSVASLDLT GGLPEVATPE SEEAFTLPLL NDPEPKPSVE PVKSISSMEL 
       160        170        180        190        200
KTEPFDDFLF PASSRPSGSE TARSVPDMDL SGSFYAADWE PLHSGSLGMG 
       210        220        230        240        250
PMATELEPLC TPVVTCTPSC TAYTSSFVFT YPEADSFPSC AAAHRKGSSS 
       260 
NEPSSDSLSS PTLLAL

Note: No experimental confirmation available.

Show »

Length:266

Mass (Da):28,986

Checksum:ⁱC57F8C4E227FB777

GO

Isoform 3 (identifier: P01100-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
132-167: Missing.

« 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 QETDQLEDEK SALQTEIANL 
       160        170        180        190        200
LKEKEKLEFI LAAHRPACKI PDDLGFPEEM SVASLDLTGG LPEVATPESE 
       210        220        230        240        250
EAFTLPLLND PEPKPSVEPV KSISSMELKT EPFDDFLFPA SSRPSGSETA 
       260        270        280        290        300
RSVPDMDLSG SFYAADWEPL HSGSLGMGPM ATELEPLCTP VVTCTPSCTA 
       310        320        330        340 
YTSSFVFTYP EADSFPSCAA AHRKGSSSNE PSSDSLSSPT LLAL

Note: No experimental confirmation available.

Show »

Length:344

Mass (Da):36,301

Checksum:ⁱ5DD706220BEB00A1

GO

Computationally mapped potential isoform sequencesⁱ

There are 6 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

G3V2V7	G3V2V7_HUMAN	Proto-oncogene c-Fos Proto-oncogene c-Fos	FOS	232	Annotation score:
G3V5J9	G3V5J9_HUMAN	Proto-oncogene c-Fos Proto-oncogene c-Fos	FOS	176	Annotation score:
G3V5N7	G3V5N7_HUMAN	Proto-oncogene c-Fos Proto-oncogene c-Fos	FOS	142	Annotation score:
H0YJM3	H0YJM3_HUMAN	Proto-oncogene c-Fos Proto-oncogene c-Fos	FOS	83	Annotation score:
G3V289	G3V289_HUMAN	Proto-oncogene c-Fos Proto-oncogene c-Fos	FOS	170	Annotation score:
G3V5N9	G3V5N9_HUMAN	Proto-oncogene c-Fos Proto-oncogene c-Fos	FOS	137	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	133 – 144	SPEEE…RRIRR → ISRRRREKENPK no nucleotide entry (PubMed:15489334).CuratedAdd BLAST		12

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_055560	1 – 114	Missing in isoform 2. 1 PublicationAdd BLAST		114
Alternative sequenceⁱVSP_055561	132 – 167	Missing in isoform 3. 1 PublicationAdd BLAST		36

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ 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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS9841.1 [P01100-1]
PIRⁱ	A01342 TVHUF1 E34223
NCBI Reference Sequences More...RefSeqⁱ	NP_005243.1, NM_005252.3 [P01100-1]
UniGeneⁱ	Hs.25647

Genome annotation databases

Ensemblⁱ	ENST00000303562; ENSP00000306245; ENSG00000170345 [P01100-1] ENST00000535987; ENSP00000442268; ENSG00000170345 [P01100-3] ENST00000555686; ENSP00000452590; ENSG00000170345 [P01100-2]
GeneIDⁱ	2353
KEGGⁱ	hsa:2353
UCSC genome browser More...UCSCⁱ	uc010asi.4 human [P01100-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P01100	FOS protein		HUMAN		380	UniRef100_P01100
FOS isoform 10		PANTR		232
Cellular oncogene c-fos (Fragment)		HUMAN		213
Proto-oncogene c-Fos		HUMAN		232
FOS/MBNL1 fusion protein (Fragment)		HUMAN		119
+2

Protein	Similar proteins		Species	Score	Length	Source
P01100	Proto-oncogene c-Fos		PHORO		381	UniRef90_P01100
Proto-oncogene c-Fos		PHOCM		381
Proto-oncogene c-Fos		FELCA		381
Proto-oncogene c-Fos		CRIGR		381
Proto-oncogene c-Fos		RAT		380
+135
P01100-3	Uncharacterized protein		PROCO		345	UniRef90_P01100-3
FOS isoform 4		PANTR		344
Uncharacterized protein		PANPA		344
Fos proto-oncogene, AP-1 transcription factor subunit		GORGO		344
Proto-oncogene c-Fos (Fragment)		HUMAN		142
+31

Protein	Similar proteins		Species	Score	Length	Source
P01100	Proto-oncogene c-Fos		PHOCM		381	UniRef50_P01100
Proto-oncogene c-Fos		CRIGR		381
Proto-oncogene c-Fos		FELCA		381
Proto-oncogene c-Fos		PHORO		381
Proto-oncogene c-Fos		BOVIN		380
+143
P01100-3	Uncharacterized protein		PROCO		345	UniRef50_P01100-3
FOS isoform 4		PONAB		344
Uncharacterized protein		Cebus capucinus imitator		344
Uncharacterized protein		NOMLE		344
Fos proto-oncogene, AP-1 transcription factor subunit		CALJA		344
+48

Cross-referencesⁱ

Web resourcesⁱ

NIEHS-SNPs

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ 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: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	108636, 135 interactors
ComplexPortalⁱ	CPX-480 AP-1 transcription factor complex FOS-JUN-NFATC2 CPX-486 AP-1 transcription factor complex FOS-JUN
CORUMⁱ	P01100
DIPⁱ	DIP-1047N
ELMⁱ	P01100
IntActⁱ	P01100, 143 interactors
MINTⁱ	P01100
STRINGⁱ	9606.ENSP00000306245

Chemistry databases

BindingDBⁱ	P01100
ChEMBLⁱ	CHEMBL2111421
DrugBankⁱ	DB08813 Nadroparin DB00852 Pseudoephedrine

PTM databases

iPTMnetⁱ	P01100
PhosphoSitePlusⁱ	P01100

Polymorphism and mutation databases

BioMutaⁱ	FOS
DMDMⁱ	120470

Proteomic databases

EPDⁱ	P01100
PaxDbⁱ	P01100
PeptideAtlasⁱ	P01100
PRIDEⁱ	P01100
ProteomicsDBⁱ	51317

Protocols and materials databases

The DNASU plasmid repository More...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	uc010asi.4 human [P01100-1]

Organism-specific databases

CTDⁱ	2353
DisGeNETⁱ	2353
EuPathDBⁱ	HostDB:ENSG00000170345.9
GeneCardsⁱ	FOS
HGNCⁱ	HGNC:3796 FOS
HPAⁱ	HPA018531
MIMⁱ	164810 gene
neXtProtⁱ	NX_P01100
OpenTargetsⁱ	ENSG00000170345
Orphanetⁱ	528 Berardinelli-Seip congenital lipodystrophy
PharmGKBⁱ	PA28212
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG1414 Eukaryota ENOG4111CH5 LUCA
GeneTreeⁱ	ENSGT00730000110541
HOGENOMⁱ	HOG000234334
HOVERGENⁱ	HBG005743
InParanoidⁱ	P01100
KOⁱ	K04379
OMAⁱ	HRPACKM
OrthoDBⁱ	EOG091G0GGW
PhylomeDBⁱ	P01100
TreeFamⁱ	TF326301

Enzyme and pathway databases

Reactomeⁱ	R-HSA-2559580 Oxidative Stress Induced Senescence R-HSA-2559582 Senescence-Associated Secretory Phenotype (SASP) R-HSA-2871796 FCERI mediated MAPK activation R-HSA-450341 Activation of the AP-1 family of transcription factors R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling R-HSA-6796648 TP53 Regulates Transcription of DNA Repair Genes R-HSA-9018519 Estrogen-dependent gene expression
SignaLinkⁱ	P01100
SIGNORⁱ	P01100

Miscellaneous databases

ChiTaRSⁱ	FOS human
EvolutionaryTraceⁱ	P01100
GeneWikiⁱ	C-Fos
GenomeRNAiⁱ	2353
Protein Ontology More...PROⁱ	PR:P01100
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000170345 Expressed in 237 organ(s), highest expression level in mucosa of stomach
CleanExⁱ	HS_FOS
ExpressionAtlasⁱ	P01100 baseline and differential
Genevisibleⁱ	P01100 HS

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:SF4 PTHR23351:SF4, 1 hit
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_HUMAN
Accessionⁱ	P01100Primary (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 10, 2018
	This is version 216 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

SIMILARITY comments
Index of protein domains and families
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human chromosome 14
Human chromosome 14: entries, gene names and cross-references to MIM
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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UniProtKB - P01100 (FOS_HUMAN)

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Proto-oncogene c-Fos

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<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

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GO - Biological processi

Enzyme and pathway databases

<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

Organism-specific databases

<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

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Keywords - Cellular componenti

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<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

Keywords - PTMi

Proteomic databases

PTM 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

Organism-specific 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

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<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

Secondary structure

3D structure databases

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<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

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Keywords - Coding sequence diversityi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ