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Protein

Transcription factor AP-1

Gene

JUN

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

Transcription factor that recognizes and binds to the enhancer heptamer motif 5'-TGA[CG]TCA-3'. Promotes activity of NR5A1 when phosphorylated by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation. Involved in activated KRAS-mediated transcriptional activation of USP28 in colorectal cancer (CRC) cells (PubMed:24623306). Binds to the USP28 promoter in colorectal cancer (CRC) cells (PubMed:24623306).3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei272Necessary for synergistic transcriptional activity with SMAD31

<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

GO - Biological processi

<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 functionActivator, DNA-binding
Biological processTranscription, Transcription regulation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-1912408 Pre-NOTCH Transcription and Translation
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-5617472 Activation of anterior HOX genes in hindbrain development during early embryogenesis
R-HSA-5687128 MAPK6/MAPK4 signaling
R-HSA-6796648 TP53 Regulates Transcription of DNA Repair Genes
R-HSA-8862803 Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models
R-HSA-8943724 Regulation of PTEN gene transcription
R-HSA-9018519 Estrogen-dependent gene expression

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

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SignaLinki
P05412

SIGNOR Signaling Network Open Resource

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SIGNORi
P05412

<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:
Transcription factor AP-1
Alternative name(s):
Activator protein 1
Short name:
AP1
Proto-oncogene c-Jun
V-jun avian sarcoma virus 17 oncogene homolog
p39
<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:JUN
<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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000177606.6

Human Gene Nomenclature Database

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HGNCi
HGNC:6204 JUN

Online Mendelian Inheritance in Man (OMIM)

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MIMi
165160 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P05412

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

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>Mutagenesisi2T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-8; A-89; A-93; and A-286. 1 Publication1
Mutagenesisi8T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-89; A-93; and A-286. 1 Publication1
Mutagenesisi63S → A: Greatly reduced ATF7-mediated transcriptional activity; when associated with A-73. Abolishes interaction with FBXW7; when associated with A-73; A-91 and A-93. 2 Publications1
Mutagenesisi73S → A: Greatly reduced ATF7-mediated transcriptional activity; when associated with A-63. Abolishes interaction with FBXW7; when associated with A-63; A-91 and A-93. 2 Publications1
Mutagenesisi89T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-8; A-93; and A-286. 1 Publication1
Mutagenesisi91T → A: Abolishes interaction with FBXW7; when associated with A-63; A-73 and A-93. 1 Publication1
Mutagenesisi93T → A: Abolishes interaction with FBXW7; when associated with A-63; A-73 and A-91. 1 Publication1
Mutagenesisi93T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-8; A-89; and A-286. 1 Publication1
Mutagenesisi243S → A: Abolishes phosphorylation by DYRK2. Abolishes phosphorylation by GSK3B at Thr-239. 1 Publication1
Mutagenesisi272R → V: Abolishes the synergistic activity with SMAD3 to activate TGF-beta-mediated transcription. 1 Publication1
Mutagenesisi286T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-8; A-89; and A-93. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNET

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DisGeNETi
3725

Open Targets

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OpenTargetsi
ENSG00000177606

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA30006

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL4977

Drug and drug target database

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DrugBanki
DB01169 Arsenic trioxide
DB01029 Irbesartan
DB05785 LGD-1550
DB00852 Pseudoephedrine
DB00570 Vinblastine

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
JUN

Domain mapping of disease mutations (DMDM)

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DMDMi
135298

<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_00000764291 – 331Transcription factor AP-1Add BLAST331

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 residuei2Phosphothreonine; by PAK21 Publication1
Modified residuei8Phosphothreonine; by PAK21 Publication1
<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-linki35Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki50Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei56N6-acetyllysine; alternateBy similarity1
Cross-linki56Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei58PhosphoserineCombined sources1
Modified residuei63Phosphoserine; by MAPK8 and PLK3Combined sources3 Publications1
Cross-linki70Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei73Phosphoserine; by MAPK8 and PLK33 Publications1
Modified residuei89Phosphothreonine; by PAK21 Publication1
Modified residuei91Phosphothreonine1 Publication1
Modified residuei93Phosphothreonine; by PAK22 Publications1
Cross-linki226Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei239Phosphothreonine; by GSK3-betaCombined sources1 Publication1
Modified residuei243Phosphoserine; by DYRK2 and GSK3-betaCombined sources2 Publications1
Modified residuei249Phosphoserine; by GSK3-beta2 Publications1
Modified residuei271N6-acetyllysine1 Publication1
Modified residuei286Phosphothreonine; by PAK21 Publication1

<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

Ubiquitinated by the SCF(FBXW7), leading to its degradation (PubMed:14739463, PubMed:27458189). Ubiquitination takes place following phosphorylation, that promotes interaction with FBXW7 (PubMed:14739463).2 Publications
Phosphorylated by CaMK4 and PRKDC; phosphorylation enhances the transcriptional activity. Phosphorylated by HIPK3. Phosphorylated by DYRK2 at Ser-243; this primes the protein for subsequent phosphorylation by GSK3B at Thr-239. Phosphorylated at Thr-239, Ser-243 and Ser-249 by GSK3B; phosphorylation reduces its ability to bind DNA. Phosphorylated by PAK2 at Thr-2, Thr-8, Thr-89, Thr-93 and Thr-286 thereby promoting JUN-mediated cell proliferation and transformation. Phosphorylated by PLK3 following hypoxia or UV irradiation, leading to increase DNA-binding activity.9 Publications
Acetylated at Lys-271 by EP300.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P05412

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P05412

MaxQB - The MaxQuant DataBase

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MaxQBi
P05412

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

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PaxDbi
P05412

PeptideAtlas

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PeptideAtlasi
P05412

PRoteomics IDEntifications database

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PRIDEi
P05412

ProteomicsDB human proteome resource

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ProteomicsDBi
51836

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P05412

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

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PhosphoSitePlusi
P05412

<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

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000177606 Expressed in 238 organ(s), highest expression level in amniotic fluid

CleanEx database of gene expression profiles

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CleanExi
HS_JUN

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P05412 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB003801
CAB007780
HPA059474

<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 either FOS or BATF3 or ATF7 (PubMed:10376527, PubMed:12087103, PubMed:15467742). The ATF7/JUN heterodimer is essential for ATF7 transactivation activity (PubMed:10376527). Interacts with DSIPI; the interaction inhibits the binding of active AP1 to its target DNA (By similarity). Interacts with HIVEP3 and MYBBP1A (By similarity). Interacts with SP1, SPIB and TCF20 (PubMed:10196196, PubMed:16478997, PubMed:8663478). Interacts with COPS5; the interaction leads indirectly to its phosphorylation (PubMed:8837781). Component of the SMAD3/SMAD4/JUN/FOS/complex which forms at the AP1 promoter site (PubMed:10995748). The SMAD3/SMAD4 heterodimer acts synergistically with the JUN/FOS heterodimer to activate transcription in response to TGF-beta (PubMed:9732876). Interacts (via its basic DNA binding and leucine zipper domains) with SMAD3 (via an N-terminal domain); the interaction is required for TGF-beta-mediated transactivation of the SMAD3/SMAD4/JUN/FOS/complex (PubMed:10995748). Interacts with methylated RNF187 (PubMed:20852630, PubMed:23624934). Binds to HIPK3. Interacts (when phosphorylated) with FBXW7 (PubMed:14739463). Found in a complex with PRR7 and FBXW7 (PubMed:27458189). Interacts with PRR7 and FBXW7; the interaction inhibits ubiquitination-mediated JUN degradation promoting its phosphorylation and transcriptional activity (PubMed:27458189). Interacts with RBM39 (By similarity).By similarity13 Publications

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
109928, 252 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-480 AP-1 transcription factor complex FOS-JUN-NFATC2
CPX-486 AP-1 transcription factor complex FOS-JUN
CPX-490 AP-1 transcription factor complex JUN dimer

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P05412

Database of interacting proteins

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DIPi
DIP-5961N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P05412

Protein interaction database and analysis system

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IntActi
P05412, 1378 interactors

Molecular INTeraction database

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MINTi
P05412

STRING: functional protein association networks

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STRINGi
9606.ENSP00000360266

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P05412

<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

1331
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A02X-ray2.70J253-308[»]
1FOSX-ray3.05F/H254-315[»]
1JNMX-ray2.20A/B254-315[»]
1JUNNMR-A/B276-314[»]
1S9KX-ray3.10E257-308[»]
1T2KX-ray3.00C254-314[»]
5FV8X-ray1.99D/E277-308[»]
5T01X-ray1.89A/B254-315[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P05412

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

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SMRi
P05412

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P05412

<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>Domaini252 – 315bZIPPROSITE-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>Regioni252 – 279Basic motifPROSITE-ProRule annotationAdd BLAST28
Regioni280 – 308Leucine-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. Jun subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0837 Eukaryota
ENOG410XRWH LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000162061

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000006648

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG001722

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P05412

KEGG Orthology (KO)

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KOi
K04448

Identification of Orthologs from Complete Genome Data

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OMAi
PVYEDLN

Database of Orthologous Groups

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OrthoDBi
1090460at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P05412

TreeFam database of animal gene trees

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TreeFami
TF323952

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR004827 bZIP
IPR015558 C_Jun/v-Jun
IPR005643 JNK
IPR002112 Leuzip_Jun
IPR008917 TF_DNA-bd_sf

The PANTHER Classification System

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PANTHERi
PTHR11462:SF8 PTHR11462:SF8, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00170 bZIP_1, 1 hit
PF03957 Jun, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00043 LEUZIPPRJUN

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00338 BRLZ, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47454 SSF47454, 1 hit

PROSITE; a protein domain and family database

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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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<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.

P05412-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTAKMETTFY DDALNASFLP SESGPYGYSN PKILKQSMTL NLADPVGSLK
60 70 80 90 100
PHLRAKNSDL LTSPDVGLLK LASPELERLI IQSSNGHITT TPTPTQFLCP
110 120 130 140 150
KNVTDEQEGF AEGFVRALAE LHSQNTLPSV TSAAQPVNGA GMVAPAVASV
160 170 180 190 200
AGGSGSGGFS ASLHSEPPVY ANLSNFNPGA LSSGGGAPSY GAAGLAFPAQ
210 220 230 240 250
PQQQQQPPHH LPQQMPVQHP RLQALKEEPQ TVPEMPGETP PLSPIDMESQ
260 270 280 290 300
ERIKAERKRM RNRIAASKCR KRKLERIARL EEKVKTLKAQ NSELASTANM
310 320 330
LREQVAQLKQ KVMNHVNSGC QLMLTQQLQT F
Length:331
Mass (Da):35,676
Last modified:October 1, 1989 - v2
<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:i0695E23AC4D33561
GO

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 conflicti11D → G AA sequence (PubMed:2825349).Curated1
Sequence conflicti14L → F AA sequence (PubMed:2825349).Curated1
Sequence conflicti80I → V AA sequence (PubMed:2825349).Curated1
Sequence conflicti151A → S in CAG46525 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_012070297T → M. Corresponds to variant dbSNP:rs9989Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
J04111 Genomic DNA Translation: AAA59197.1
CR541724 mRNA Translation: CAG46525.1
BT019759 mRNA Translation: AAV38564.1
AY217548 Genomic DNA Translation: AAO22993.1
AL136985 Genomic DNA No translation available.
BC002646 mRNA No translation available.
BC006175 mRNA Translation: AAH06175.1
BC009874 mRNA Translation: AAH09874.2
BC068522 mRNA Translation: AAH68522.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS610.1

Protein sequence database of the Protein Information Resource

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PIRi
A31264 TVHUJN

NCBI Reference Sequences

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RefSeqi
NP_002219.1, NM_002228.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.696684

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000371222; ENSP00000360266; ENSG00000177606

Database of genes from NCBI RefSeq genomes

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GeneIDi
3725

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:3725

UCSC genome browser

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UCSCi
uc001cze.4 human

Keywords - Coding sequence diversityi

Polymorphism

<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

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04111 Genomic DNA Translation: AAA59197.1
CR541724 mRNA Translation: CAG46525.1
BT019759 mRNA Translation: AAV38564.1
AY217548 Genomic DNA Translation: AAO22993.1
AL136985 Genomic DNA No translation available.
BC002646 mRNA No translation available.
BC006175 mRNA Translation: AAH06175.1
BC009874 mRNA Translation: AAH09874.2
BC068522 mRNA Translation: AAH68522.1
CCDSiCCDS610.1
PIRiA31264 TVHUJN
RefSeqiNP_002219.1, NM_002228.3
UniGeneiHs.696684

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A02X-ray2.70J253-308[»]
1FOSX-ray3.05F/H254-315[»]
1JNMX-ray2.20A/B254-315[»]
1JUNNMR-A/B276-314[»]
1S9KX-ray3.10E257-308[»]
1T2KX-ray3.00C254-314[»]
5FV8X-ray1.99D/E277-308[»]
5T01X-ray1.89A/B254-315[»]
ProteinModelPortaliP05412
SMRiP05412
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109928, 252 interactors
ComplexPortaliCPX-480 AP-1 transcription factor complex FOS-JUN-NFATC2
CPX-486 AP-1 transcription factor complex FOS-JUN
CPX-490 AP-1 transcription factor complex JUN dimer
CORUMiP05412
DIPiDIP-5961N
ELMiP05412
IntActiP05412, 1378 interactors
MINTiP05412
STRINGi9606.ENSP00000360266

Chemistry databases

BindingDBiP05412
ChEMBLiCHEMBL4977
DrugBankiDB01169 Arsenic trioxide
DB01029 Irbesartan
DB05785 LGD-1550
DB00852 Pseudoephedrine
DB00570 Vinblastine

PTM databases

iPTMnetiP05412
PhosphoSitePlusiP05412

Polymorphism and mutation databases

BioMutaiJUN
DMDMi135298

Proteomic databases

EPDiP05412
jPOSTiP05412
MaxQBiP05412
PaxDbiP05412
PeptideAtlasiP05412
PRIDEiP05412
ProteomicsDBi51836

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
3725
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371222; ENSP00000360266; ENSG00000177606
GeneIDi3725
KEGGihsa:3725
UCSCiuc001cze.4 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
3725
DisGeNETi3725
EuPathDBiHostDB:ENSG00000177606.6

GeneCards: human genes, protein and diseases

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GeneCardsi
JUN

H-Invitational Database, human transcriptome db

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H-InvDBi
HIX0000635
HGNCiHGNC:6204 JUN
HPAiCAB003801
CAB007780
HPA059474
MIMi165160 gene
neXtProtiNX_P05412
OpenTargetsiENSG00000177606
PharmGKBiPA30006

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0837 Eukaryota
ENOG410XRWH LUCA
GeneTreeiENSGT00940000162061
HOGENOMiHOG000006648
HOVERGENiHBG001722
InParanoidiP05412
KOiK04448
OMAiPVYEDLN
OrthoDBi1090460at2759
PhylomeDBiP05412
TreeFamiTF323952

Enzyme and pathway databases

ReactomeiR-HSA-1912408 Pre-NOTCH Transcription and Translation
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-5617472 Activation of anterior HOX genes in hindbrain development during early embryogenesis
R-HSA-5687128 MAPK6/MAPK4 signaling
R-HSA-6796648 TP53 Regulates Transcription of DNA Repair Genes
R-HSA-8862803 Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models
R-HSA-8943724 Regulation of PTEN gene transcription
R-HSA-9018519 Estrogen-dependent gene expression
SignaLinkiP05412
SIGNORiP05412

Miscellaneous databases

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

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ChiTaRSi
JUN human
EvolutionaryTraceiP05412

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
C-jun

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

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GenomeRNAii
3725

Protein Ontology

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PROi
PR:P05412

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000177606 Expressed in 238 organ(s), highest expression level in amniotic fluid
CleanExiHS_JUN
GenevisibleiP05412 HS

Family and domain databases

InterProiView protein in InterPro
IPR004827 bZIP
IPR015558 C_Jun/v-Jun
IPR005643 JNK
IPR002112 Leuzip_Jun
IPR008917 TF_DNA-bd_sf
PANTHERiPTHR11462:SF8 PTHR11462:SF8, 1 hit
PfamiView protein in Pfam
PF00170 bZIP_1, 1 hit
PF03957 Jun, 1 hit
PRINTSiPR00043 LEUZIPPRJUN
SMARTiView protein in SMART
SM00338 BRLZ, 1 hit
SUPFAMiSSF47454 SSF47454, 1 hit
PROSITEiView protein in PROSITE
PS50217 BZIP, 1 hit
PS00036 BZIP_BASIC, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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 nameiJUN_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: P05412
Secondary accession number(s): Q6FHM7, Q96G93
<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: November 1, 1988
Last sequence update: October 1, 1989
Last modified: January 16, 2019
This is version 239 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

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