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UniProtKB - P01100 (FOS_HUMAN)

Entry version 224 (31 Jul 2019)
Sequence version 1 (21 Jul 1986)
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Protein

Proto-oncogene c-Fos

Gene

FOS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

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

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...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
R-HSA-9634638 Estrogen-dependent nuclear events downstream of ESR-membrane signaling

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P01100

SIGNOR Signaling Network Open Resource

More...SIGNORi		P01100

<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 subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Proto-oncogene c-Fos
Alternative name(s):
Cellular oncogene fos
G0/G1 switch regulatory protein 7
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:FOS
Synonyms:G0S7
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 14

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:3796 FOS

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		164810 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P01100

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Nucleus

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi10Y → E: Loss of activation of phospholipid synthesis; when associated with E-30. 2 Publications1
Mutagenesisi10Y → 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 Publications1
Mutagenesisi30Y → E: Loss of activation of phospholipid synthesis; when associated with E-10. 2 Publications1
Mutagenesisi30Y → 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 Publications1
Mutagenesisi106Y → F: No effect on Tyr-phosphorylation. Loss of endoplasmic reticulum localization in quiescent cells. 1 Publication1
Mutagenesisi128K → R: No change in sumoylation. 1 Publication1
Mutagenesisi192K → R: No change in sumoylation. 1 Publication1
Mutagenesisi232T → D: Decreased sumoylation levels. 1
Mutagenesisi265K → R: Abolishes sumoylation. No change in nuclear location nor on protein stability. Increased AP1 transactivation activity when heterodimerized with cJUN. 1 Publication1
Mutagenesisi325T → D: No change in sumoylation levels. 1 Publication1
Mutagenesisi331T → D: No change in sumoylation levels. 1 Publication1
Mutagenesisi337Y → F: No effect on Tyr-phosphorylation. Loss of endoplasmic reticulum localization in quiescent cells. 1 Publication1
Mutagenesisi362S → A: Loss of protein stability. Reduced MOS/MAPK-mediated transforming ability; when associated with A-374. 2 Publications1
Mutagenesisi362S → D: Increased protein stability. Increased MOS/MAPK-mediated transforming ability and no change in sumoylation levels; when associated with D-374. 2 Publications1
Mutagenesisi374S → A: No change in sumoylation levels. Loss of protein stability. Reduced MOS/MAPK-mediated transforming ability; when associated with A-362. 2 Publications1
Mutagenesisi374S → D: Increased protein stability. Increased MOS/MAPK-mediated transforming ability and no change in sumoylation levels; when associated with D-362. 2 Publications1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNET

More...DisGeNETi		2353

Open Targets

More...OpenTargetsi		ENSG00000170345

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		528 Berardinelli-Seip congenital lipodystrophy

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA28212

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2111421

Drug and drug target database

More...DrugBanki		DB08813 Nadroparin
DB00852 Pseudoephedrine

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		FOS

Domain mapping of disease mutations (DMDM)

More...DMDMi		120470

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000764651 – 380Proto-oncogene c-FosAdd BLAST380

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei10Phosphotyrosine; by SRC2 Publications1
Modified residuei30Phosphotyrosine; by SRC2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki113Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki128Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei232PhosphothreonineBy similarity1
Cross-linki265Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei325Phosphothreonine; by MAPK1 and MAPK31 Publication1
Modified residuei331Phosphothreonine; by MAPK1 and MAPK31 Publication1
Modified residuei362Phosphoserine; by MAPK1, MAPK3 and RPS6KA31 Publication1
Modified residuei374Phosphoserine; by MAPK1 and MAPK32 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

More...EPDi		P01100

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P01100

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P01100

PeptideAtlas

More...PeptideAtlasi		P01100

PRoteomics IDEntifications database

More...PRIDEi		P01100

ProteomicsDB human proteome resource

More...ProteomicsDBi		1860
4848
51317 [P01100-1]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P01100

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P01100

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000170345 Expressed in 237 organ(s), highest expression level in mucosa of stomach

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P01100 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P01100 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA018531

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		108636, 145 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-480 AP-1 transcription factor complex FOS-JUN-NFATC2
CPX-486 AP-1 transcription factor complex FOS-JUN

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P01100

Database of interacting proteins

More...DIPi		DIP-1047N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P01100

Protein interaction database and analysis system

More...IntActi		P01100, 144 interactors

Molecular INTeraction database

More...MINTi		P01100

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000306245

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P01100

<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

1380
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P01100

Database of comparative protein structure models

More...ModBasei		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P01100

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini137 – 200bZIPPROSITE-ProRule annotationAdd BLAST64

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni139 – 159Basic motif; required for the activation of phospholipid synthesis, but not for CDS1-bindingAdd BLAST21
Regioni165 – 193Leucine-zipperPROSITE-ProRule annotationAdd BLAST29

<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

Belongs to the bZIP family. Fos subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1414 Eukaryota
ENOG4111CH5 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000159276

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000234334

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P01100

KEGG Orthology (KO)

More...KOi		K04379

Identification of Orthologs from Complete Genome Data

More...OMAi		HRPACKM

Database of Orthologous Groups

More...OrthoDBi		1221590at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P01100

TreeFam database of animal gene trees

More...TreeFami		TF326301

Family and domain databases

Database of protein disorder

More...DisProti		DP00078

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000837 AP-1
IPR004827 bZIP
IPR029816 c-Fos/v-Fos

The PANTHER Classification System

More...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

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00042 LEUZIPPRFOS

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00338 BRLZ, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50217 BZIP, 1 hit
PS00036 BZIP_BASIC, 1 hit

<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 <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

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

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

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i9E3B2969347C90C8
GO
Isoform 2 (identifier: P01100-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:266
Mass (Da):28,986
Checksum:iC57F8C4E227FB777
GO
Isoform 3 (identifier: P01100-3) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:344
Mass (Da):36,301
Checksum:i5DD706220BEB00A1
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V2V7G3V2V7_HUMAN
Proto-oncogene c-Fos
FOS
232Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3V5N7G3V5N7_HUMAN
Proto-oncogene c-Fos
FOS
142Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3V5N9G3V5N9_HUMAN
Proto-oncogene c-Fos
FOS
137Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0YJM3H0YJM3_HUMAN
Proto-oncogene c-Fos
FOS
83Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3V5J9G3V5J9_HUMAN
Proto-oncogene c-Fos
FOS
176Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3V289G3V289_HUMAN
Proto-oncogene c-Fos
FOS
170Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti133 – 144SPEEE…RRIRR → ISRRRREKENPK no nucleotide entry (PubMed:15489334).CuratedAdd BLAST12

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0555601 – 114Missing in isoform 2. 1 PublicationAdd BLAST114
Alternative sequenceiVSP_055561132 – 167Missing in isoform 3. 1 PublicationAdd BLAST36

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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]

Protein sequence database of the Protein Information Resource

More...PIRi		A01342 TVHUF1
E34223

NCBI Reference Sequences

More...RefSeqi		NP_005243.1, NM_005252.3 [P01100-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000303562; ENSP00000306245; ENSG00000170345 [P01100-1]
ENST00000535987; ENSP00000442268; ENSG00000170345 [P01100-3]
ENST00000555686; ENSP00000452590; ENSG00000170345 [P01100-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2353

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:2353

UCSC genome browser

More...UCSCi		uc010asi.4 human [P01100-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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
CCDSiCCDS9841.1 [P01100-1]
PIRiA01342 TVHUF1
E34223
RefSeqiNP_005243.1, NM_005252.3 [P01100-1]

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 entryMethodResolution (Å)ChainPositionsPDBsum
1A02X-ray2.70F138-193[»]
1FOSX-ray3.05E/G139-200[»]
1S9KX-ray3.10D140-192[»]
SMRiP01100
ModBaseiSearch...

Protein-protein interaction databases

BioGridi108636, 145 interactors
ComplexPortaliCPX-480 AP-1 transcription factor complex FOS-JUN-NFATC2
CPX-486 AP-1 transcription factor complex FOS-JUN
CORUMiP01100
DIPiDIP-1047N
ELMiP01100
IntActiP01100, 144 interactors
MINTiP01100
STRINGi9606.ENSP00000306245

Chemistry databases

BindingDBiP01100
ChEMBLiCHEMBL2111421
DrugBankiDB08813 Nadroparin
DB00852 Pseudoephedrine

PTM databases

iPTMnetiP01100
PhosphoSitePlusiP01100

Polymorphism and mutation databases

BioMutaiFOS
DMDMi120470

Proteomic databases

EPDiP01100
jPOSTiP01100
PaxDbiP01100
PeptideAtlasiP01100
PRIDEiP01100
ProteomicsDBi1860
4848
51317 [P01100-1]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		2353
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000303562; ENSP00000306245; ENSG00000170345 [P01100-1]
ENST00000535987; ENSP00000442268; ENSG00000170345 [P01100-3]
ENST00000555686; ENSP00000452590; ENSG00000170345 [P01100-2]
GeneIDi2353
KEGGihsa:2353
UCSCiuc010asi.4 human [P01100-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2353
DisGeNETi2353

GeneCards: human genes, protein and diseases

More...GeneCardsi		FOS
HGNCiHGNC:3796 FOS
HPAiHPA018531
MIMi164810 gene
neXtProtiNX_P01100
OpenTargetsiENSG00000170345
Orphaneti528 Berardinelli-Seip congenital lipodystrophy
PharmGKBiPA28212

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1414 Eukaryota
ENOG4111CH5 LUCA
GeneTreeiENSGT00940000159276
HOGENOMiHOG000234334
InParanoidiP01100
KOiK04379
OMAiHRPACKM
OrthoDBi1221590at2759
PhylomeDBiP01100
TreeFamiTF326301

Enzyme and pathway databases

ReactomeiR-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
R-HSA-9634638 Estrogen-dependent nuclear events downstream of ESR-membrane signaling
SignaLinkiP01100
SIGNORiP01100

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		FOS human
EvolutionaryTraceiP01100

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		C-Fos

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		2353

Protein Ontology

More...PROi		PR:P01100

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000170345 Expressed in 237 organ(s), highest expression level in mucosa of stomach
ExpressionAtlasiP01100 baseline and differential
GenevisibleiP01100 HS

Family and domain databases

DisProtiDP00078
InterProiView protein in InterPro
IPR000837 AP-1
IPR004827 bZIP
IPR029816 c-Fos/v-Fos
PANTHERiPTHR23351 PTHR23351, 1 hit
PTHR23351:SF4 PTHR23351:SF4, 1 hit
PfamiView protein in Pfam
PF00170 bZIP_1, 1 hit
PRINTSiPR00042 LEUZIPPRFOS
SMARTiView protein in SMART
SM00338 BRLZ, 1 hit
PROSITEiView protein in PROSITE
PS50217 BZIP, 1 hit
PS00036 BZIP_BASIC, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<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 subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFOS_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P01100
Secondary accession number(s): A8K4E2, B4DQ65, P18849
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 31, 2019
This is version 224 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

<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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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