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 (By similarity). 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.By similarity5 Publications

GO - Molecular functionⁱ

chromatin binding
Source: MGI
Inferred from direct assayⁱ
- 20442316
DNA binding
Source: MGI
Inferred from direct assayⁱ
- 12486129
DNA binding transcription factor activity
Source: MGI
Inferred from direct assayⁱ
- 12220541
double-stranded DNA binding Source: MGI
protein heterodimerization activity Source: MGI
RNA polymerase II activating transcription factor binding Source: MGI
RNA polymerase II core promoter sequence-specific DNA binding Source: MGI
RNA polymerase II proximal promoter sequence-specific DNA binding
Source: NTNU_SB
Inferred from direct assayⁱ
- 11925568
R-SMAD binding Source: MGI
sequence-specific DNA binding Source: MGI
transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding
Source: NTNU_SB
Inferred from direct assayⁱ
- 11925568
transcriptional activator activity, RNA polymerase II transcription factor binding Source: MGI
transcription factor binding Source: MGI
transcription regulatory region DNA binding Source: MGI

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

aging Source: Ensembl
cellular response to cadmium ion Source: MGI
cellular response to calcium ion
Source: MGI
Inferred from direct assayⁱ
- 19365557
cellular response to extracellular stimulus
Source: MGI
Inferred from mutant phenotypeⁱ
- 9294610
cellular response to hormone stimulus Source: Ensembl
cellular response to reactive oxygen species Source: MGI
conditioned taste aversion Source: Ensembl
female pregnancy Source: Ensembl
nervous system development
Source: MGI
Inferred from mutant phenotypeⁱ
- 11925568
positive regulation of neuron death Source: MGI
positive regulation of osteoclast differentiation
Source: MGI
Inferred from direct assayⁱ
- 23395171
positive regulation of pri-miRNA transcription by RNA polymerase II Source: MGI
positive regulation of transcription, DNA-templated Source: MGI
positive regulation of transcription by RNA polymerase II
Source: NTNU_SB
Inferred from mutant phenotypeⁱ
- 11925568
regulation of transcription, DNA-templated
Source: MGI
Inferred from direct assayⁱ
- 12220541
response to cAMP Source: Ensembl
response to cold Source: Ensembl
response to corticosterone Source: Ensembl
response to cytokine Source: Ensembl
response to drug
Source: MGI
Inferred from direct assayⁱ
- 9098922
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: MGI
Inferred from direct assayⁱ
- 20442316
response to progesterone Source: Ensembl
response to toxic substance Source: Ensembl
skeletal muscle cell differentiation
Source: MGI
Inferred from mutant phenotypeⁱ
- 22147266
sleep Source: Ensembl
SMAD protein signal transduction Source: MGI
transcription by RNA polymerase II Source: MGI
transforming growth factor beta receptor signaling pathway Source: MGI

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	DNA-binding

Molecular function

DNA-binding

Enzyme and pathway databases

Reactomeⁱ	R-MMU-2559580 Oxidative Stress Induced Senescence R-MMU-2871796 FCERI mediated MAPK activation R-MMU-450341 Activation of the AP-1 family of transcription factors R-MMU-9018519 Estrogen-dependent gene expression

Reactomeⁱ

R-MMU-2559580 Oxidative Stress Induced Senescence
R-MMU-2871796 FCERI mediated MAPK activation
R-MMU-450341 Activation of the AP-1 family of transcription factors
R-MMU-9018519 Estrogen-dependent gene expression

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Proto-oncogene c-Fos Alternative name(s): Cellular oncogene fos
Gene namesⁱ	Name:Fos
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [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 › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Chromosome 12

Organism-specific databases

MGIⁱ	MGI:95574 Fos

Keywords - Cellular componentⁱ

Cytoplasm, Endoplasmic reticulum, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	139	K → N: No effect on activation of phospholipid synthesis. 1 Publication	1
Mutagenesisⁱ	144	R → N: No effect on activation of phospholipid synthesis, nor on CDS1-binding. 1 Publication	1
Mutagenesisⁱ	146	R → N: Complete loss of activation of phospholipid synthesis. No effect on CDS1-binding. 1 Publication	1
Mutagenesisⁱ	232	T → A: No effect on PDGF-stimulated enhancement of transcriptional activity. Completely abolishes PDGF-stimulated enhancement of transcriptional activity; when associated with A-325; A-331 and A-374. 1 Publication	1
Mutagenesisⁱ	325	T → A: Almost no EGF-mediated phosphorylation, greatly reduced cellular transformation, and reduced AP1 activity by 20%; when associated with A-331. No effect on PDGF-stimulated enhancement of transcriptional activity. Completely abolishes PDGF-stimulated enhancement of transcriptional activity; when associated with A-232; A-331 and A-374. 2 Publications	1
Mutagenesisⁱ	331	T → A: Almost no EGF-mediated phosphorylation, greatly reduced cellular transformation, and reduced AP1 activity by 20%; when associated with A-325. No effect on PDGF-stimulated enhancement of transcriptional activity. Completely abolishes PDGF-stimulated enhancement of transcriptional activity; when associated with A-232; A-325;and A-374. 2 Publications	1
Mutagenesisⁱ	343	F → A: Reduced phosphorylation by ERK. Reduced AP1 activity by 65%. 1 Publication	1
Mutagenesisⁱ	345	Y → A: Reduced phosphorylation by ERK. 1 Publication	1
Mutagenesisⁱ	362	S → D: Enhanced EGF- and RSK-mediated tranformation; when associated with D-374. 1 Publication	1
Mutagenesisⁱ	362	S → E: Increased enhancement of EGF- and RSK-mediated tranformation; when associated with E-374. 1 Publication	1
Mutagenesisⁱ	374	S → A: No effect on PDGF-stimulated enhancement of transcriptional activity. Completely abolishes PDGF-stimulated enhancement of transcriptional activity; when associated with A-232; A-325 and A-331. 2 Publications	1
Mutagenesisⁱ	374	S → D: Enhanced EGF- and RSK-mediated tranformation; when associated with D-362. 2 Publications	1
Mutagenesisⁱ	374	S → E: Enhanced EGF- and RSK-mediated tranformation; when associated with E-362. 2 Publications	1

Keywords - Diseaseⁱ

Proto-oncogene

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000076467	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	Phosphothreonine1 Publication	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 MAPK32 Publications	1
Modified residueⁱ	331	Phosphothreonine; by MAPK1 and MAPK32 Publications	1
Modified residueⁱ	362	Phosphoserine; by MAPK1, MAPK3 and RPS6KA33 Publications	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 (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.3 Publications

Keywords - PTMⁱ

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P01101
PaxDbⁱ	P01101
PRIDEⁱ	P01101

PTM databases

iPTMnetⁱ	P01101
PhosphoSitePlusⁱ	P01101

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSMUSG00000021250
CleanExⁱ	MM_FOS
Genevisibleⁱ	P01101 MM

Interactionⁱ

Subunit structureⁱ

Heterodimer; with JUN (By similarity). Interacts with MAFB. 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 (By similarity). Interacts with DSIPI; this interaction inhibits the binding of active AP1 to its target DNA. Interacts with CDS1 and PI4K2A, but not with CDIPT, nor PI4K2B.By similarity2 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
Esr2	O08537	2	EBI-4288185,EBI-2526214
Mafb	P54841	4	EBI-4288185,EBI-16093217
Mecom	P14404	2	EBI-4288185,EBI-1994523

Show more details

GO - Molecular functionⁱ

protein heterodimerization activity Source: MGI
RNA polymerase II activating transcription factor binding Source: MGI
R-SMAD binding Source: MGI
transcription factor binding Source: MGI

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	199726, 20 interactors
ComplexPortalⁱ	CPX-610 AP-1 transcription factor complex FOS-JUN-NFATC2 CPX-611 AP-1 transcription factor complex FOS-JUN
Database of interacting proteins More...DIPⁱ	DIP-1066N
ELMⁱ	P01101
IntActⁱ	P01101, 4 interactors
Molecular INTeraction database More...MINTⁱ	P01101
STRINGⁱ	10090.ENSMUSP00000021674

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Show more details

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Helixⁱ	139 – 199	Combined sources		61

3D structure databases

ProteinModelPortalⁱ	P01101
SMRⁱ	P01101
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-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	P01101
KEGG Orthology (KO) More...KOⁱ	K04379
OMAⁱ	HRPACKM
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0GGW
PhylomeDBⁱ	P01101
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

Sequenceⁱ

Sequence statusⁱ: Complete.

P01101-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MMFSGFNADY EASSSRCSSA SPAGDSLSYY HSPADSFSSM GSPVNTQDFC 
        60         70         80         90        100
ADLSVSSANF IPTVTAISTS PDLQWLVQPT LVSSVAPSQT RAPHPYGLPT 
       110        120        130        140        150
QSAGAYARAG MVKTVSGGRA QSIGRRGKVE QLSPEEEEKR RIRRERNKMA 
       160        170        180        190        200
AAKCRNRRRE LTDTLQAETD QLEDEKSALQ TEIANLLKEK EKLEFILAAH 
       210        220        230        240        250
RPACKIPDDL GFPEEMSVAS LDLTGGLPEA STPESEEAFT LPLLNDPEPK 
       260        270        280        290        300
PSLEPVKSIS NVELKAEPFD DFLFPASSRP SGSETSRSVP DVDLSGSFYA 
       310        320        330        340        350
ADWEPLHSNS LGMGPMVTEL EPLCTPVVTC TPGCTTYTSS FVFTYPEADS 
       360        370        380
FPSCAAAHRK GSSSNEPSSD SLSSPTLLAL

Length:380

Mass (Da):40,838

Last modified:July 21, 1986 - v1

Checksum:ⁱ475966265952B624

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	V00727 Genomic DNA Translation: CAA24105.1 J00370 Genomic DNA Translation: AAA96699.1 BC029814 mRNA Translation: AAH29814.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS26059.1
PIRⁱ	A01343 TVMSF
NCBI Reference Sequences More...RefSeqⁱ	NP_034364.1, NM_010234.2
UniGeneⁱ	Mm.246513

Genome annotation databases

Ensemblⁱ	ENSMUST00000021674; ENSMUSP00000021674; ENSMUSG00000021250
GeneIDⁱ	14281
KEGGⁱ	mmu:14281
UCSC genome browser More...UCSCⁱ	uc007oha.2 mouse

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length
P01101	FBJ osteosarcoma oncogene (Fragment)		MOUSE		79
Proto-oncogene c-FOS (Fragment)		RAT		47

Protein	Similar proteins		Species	Score	Length
P01101	Proto-oncogene c-Fos	)	HUMAN		380
FOS isoform 10		PANTR		232
Fos proto-oncogene, AP-1 transcription factor subunit		MUSPF		446
Proto-oncogene protein cFOS (Fragment)		FELCA		14
Proto-oncogene c-FOS (Fragment)		RAT		18
+132

Protein	Similar proteins		Species	Score	Length
P01101	Proto-oncogene c-Fos	)	HUMAN		380
FOS isoform 10		PANTR		232
Fos proto-oncogene, AP-1 transcription factor subunit		MUSPF		446
Proto-oncogene protein cFOS (Fragment)		FELCA		14
Proto-oncogene c-FOS (Fragment)		RAT		18
+172

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	V00727 Genomic DNA Translation: CAA24105.1 J00370 Genomic DNA Translation: AAA96699.1 BC029814 mRNA Translation: AAH29814.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS26059.1
PIRⁱ	A01343 TVMSF
NCBI Reference Sequences More...RefSeqⁱ	NP_034364.1, NM_010234.2
UniGeneⁱ	Mm.246513

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
	2WT7	X-ray	2.30	A	138-200	[»]
ProteinModelPortalⁱ	P01101
SMRⁱ	P01101
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	199726, 20 interactors
ComplexPortalⁱ	CPX-610 AP-1 transcription factor complex FOS-JUN-NFATC2 CPX-611 AP-1 transcription factor complex FOS-JUN
Database of interacting proteins More...DIPⁱ	DIP-1066N
ELMⁱ	P01101
IntActⁱ	P01101, 4 interactors
Molecular INTeraction database More...MINTⁱ	P01101
STRINGⁱ	10090.ENSMUSP00000021674

PTM databases

iPTMnetⁱ	P01101
PhosphoSitePlusⁱ	P01101

Proteomic databases

MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P01101
PaxDbⁱ	P01101
PRIDEⁱ	P01101

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSMUST00000021674; ENSMUSP00000021674; ENSMUSG00000021250
GeneIDⁱ	14281
KEGGⁱ	mmu:14281
UCSC genome browser More...UCSCⁱ	uc007oha.2 mouse

Organism-specific databases

CTDⁱ	2353
MGIⁱ	MGI:95574 Fos

Phylogenomic databases

eggNOGⁱ	KOG1414 Eukaryota ENOG4111CH5 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00730000110541
HOGENOMⁱ	HOG000234334
HOVERGENⁱ	HBG005743
InParanoidⁱ	P01101
KEGG Orthology (KO) More...KOⁱ	K04379
OMAⁱ	HRPACKM
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0GGW
PhylomeDBⁱ	P01101
TreeFamⁱ	TF326301

Enzyme and pathway databases

Reactomeⁱ	R-MMU-2559580 Oxidative Stress Induced Senescence R-MMU-2871796 FCERI mediated MAPK activation R-MMU-450341 Activation of the AP-1 family of transcription factors R-MMU-9018519 Estrogen-dependent gene expression

Reactomeⁱ

R-MMU-2559580 Oxidative Stress Induced Senescence
R-MMU-2871796 FCERI mediated MAPK activation
R-MMU-450341 Activation of the AP-1 family of transcription factors
R-MMU-9018519 Estrogen-dependent gene expression

Miscellaneous databases

ChiTaRSⁱ	Fos mouse
Protein Ontology More...PROⁱ	PR:P01101
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSMUSG00000021250
CleanExⁱ	MM_FOS
Genevisibleⁱ	P01101 MM

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
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	FOS_MOUSE
Accessionⁱ	P01101Primary (citable) accession number: P01101
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
	Last sequence update:	July 21, 1986
	Last modified:	June 20, 2018
	This is version 162 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families

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UniProtKB - P01101 (FOS_MOUSE)

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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

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

Nucleus

Cytosol

Endoplasmic reticulum

Cytosol

Endoplasmic reticulum

Nucleus

Other locations

<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

<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

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

<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>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

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

Secondary structure

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

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

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous 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

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ