JUN

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 key	Position(s)	DescriptionActions	Graphical view	Length
Siteⁱ	272	Necessary for synergistic transcriptional activity with SMAD3		1

GO - Molecular functionⁱ

cAMP response element binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 19861239
chromatin binding Source: Ensembl
DNA binding
Source: ProtInc
Traceable author statementⁱ
- 2825349
DNA-binding transcription activator activity, RNA polymerase II-specific
Source: BHF-UCL
Inferred from direct assayⁱ
- 19861239
DNA-binding transcription factor activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 9732876
DNA-binding transcription factor activity, RNA polymerase II-specific
Source: UniProtKB
Inferred from direct assayⁱ
- 2833704
enzyme binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 23382074
GTPase activator activity
Source: UniProtKB
Inferred from direct assayⁱ
- 11804590
HMG box domain binding Source: Ensembl
identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 20102225
- 25609649
protein heterodimerization activity
Source: CAFA
Inferred from direct assayⁱ
- 10508860
protein homodimerization activity
Source: CAFA
Inferred from direct assayⁱ
- 10508860
RNA binding
Source: UniProtKB
Inferred from high throughput direct assayⁱ
- 22681889
RNA polymerase II activating transcription factor binding
Source: CAFA
Inferred from physical interactionⁱ
- 10508860
RNA polymerase II distal enhancer sequence-specific DNA binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 19861239
RNA polymerase II proximal promoter sequence-specific DNA binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
R-SMAD binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 9732876
transcription coactivator activity
Source: UniProtKB
Inferred from direct assayⁱ
- 2833704
transcription factor binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 16007074
transcription regulatory region DNA binding
Source: UniProtKB
Inferred from direct assayⁱ
- 14645924
- 24623306
ubiquitin-like protein ligase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 27458189
ubiquitin protein ligase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 14739464

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

aging Source: Ensembl
angiogenesis Source: Ensembl
axon regeneration Source: Ensembl
cellular response to cadmium ion
Source: CAFA
Inferred from mutant phenotypeⁱ
- 26514923
cellular response to calcium ion Source: Ensembl
cellular response to hormone stimulus
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
cellular response to potassium ion starvation Source: Ensembl
cellular response to reactive oxygen species
Source: CAFA
Inferred from mutant phenotypeⁱ
- 26514923
circadian rhythm Source: Ensembl
eyelid development in camera-type eye Source: Ensembl
Fc-epsilon receptor signaling pathway Source: Reactome
leading edge cell differentiation Source: Ensembl
learning Source: Ensembl
liver development Source: Ensembl
membrane depolarization Source: Ensembl
microglial cell activation Source: Ensembl
monocyte differentiation Source: Ensembl
negative regulation by host of viral transcription
Source: UniProtKB
Inferred from direct assayⁱ
- 2833704
negative regulation of cell proliferation Source: Ensembl
negative regulation of DNA binding
Source: UniProtKB
Inferred from direct assayⁱ
- 14645924
negative regulation of neuron apoptotic process Source: Ensembl
negative regulation of protein autophosphorylation Source: Ensembl
negative regulation of transcription, DNA-templated
Source: UniProtKB
Inferred from direct assayⁱ
- 2833704
negative regulation of transcription by RNA polymerase II
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
negative regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress
Source: ParkinsonsUK-UCL
Inferred from mutant phenotypeⁱ
- 21113145
outflow tract morphogenesis Source: Ensembl
positive regulation by host of viral transcription
Source: UniProtKB
Inferred from direct assayⁱ
- 2833704
positive regulation of apoptotic process
Source: CAFA
Inferred from mutant phenotypeⁱ
- 10508860
positive regulation of cell differentiation
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
positive regulation of DNA replication Source: Ensembl
positive regulation of DNA-templated transcription, initiation
Source: CACAO
Inferred from direct assayⁱ
- 23027619
positive regulation of endothelial cell proliferation Source: Ensembl
positive regulation of epithelial cell migration Source: Ensembl
positive regulation of ERK1 and ERK2 cascade Source: Ensembl
positive regulation of fibroblast proliferation Source: Ensembl
positive regulation of monocyte differentiation Source: Ensembl
positive regulation of neuron apoptotic process Source: Ensembl
positive regulation of pri-miRNA transcription by RNA polymerase II
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 19962668
- 24375836
positive regulation of transcription, DNA-templated
Source: UniProtKB
Inferred from direct assayⁱ
- 2833704
positive regulation of transcription by RNA polymerase II
Source: UniProtKB
Inferred from direct assayⁱ
- 2833704
positive regulation of vascular smooth muscle cell proliferation
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 28701355
Ras protein signal transduction
Source: UniProtKB
Inferred from direct assayⁱ
- 24623306
regulation of cell cycle
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
regulation of DNA-binding transcription factor activity Source: Reactome
release of cytochrome c from mitochondria Source: Ensembl
response to cAMP
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
response to cytokine
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
response to drug
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
response to hydrogen peroxide Source: Ensembl
response to lipopolysaccharide
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
response to mechanical stimulus
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
response to muscle stretch Source: Ensembl
response to organic substance
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
response to radiation
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
SMAD protein signal transduction
Source: BHF-UCL
Inferred from direct assayⁱ
- 9732876
transcription by RNA polymerase II Source: Ensembl
transforming growth factor beta receptor signaling pathway
Source: BHF-UCL
Inferred from direct assayⁱ
- 9732876

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Activator, DNA-binding
Biological process	Transcription, Transcription regulation

Enzyme and pathway databases

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
SignaLinkⁱ	P05412
SIGNORⁱ	P05412

Names & Taxonomyⁱ

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
Gene namesⁱ	Name:JUN
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 1

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000177606.6
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:6204 JUN
MIMⁱ	165160 gene
neXtProtⁱ	NX_P05412

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	2	T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-8; A-89; A-93; and A-286. 1 Publication	1
Mutagenesisⁱ	8	T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-89; A-93; and A-286. 1 Publication	1
Mutagenesisⁱ	63	S → 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 Publications	1
Mutagenesisⁱ	73	S → 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 Publications	1
Mutagenesisⁱ	89	T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-8; A-93; and A-286. 1 Publication	1
Mutagenesisⁱ	91	T → A: Abolishes interaction with FBXW7; when associated with A-63; A-73 and A-93. 1 Publication	1
Mutagenesisⁱ	93	T → A: Abolishes interaction with FBXW7; when associated with A-63; A-73 and A-91. 1 Publication	1
Mutagenesisⁱ	93	T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-8; A-89; and A-286. 1 Publication	1
Mutagenesisⁱ	243	S → A: Abolishes phosphorylation by DYRK2. Abolishes phosphorylation by GSK3B at Thr-239. 1 Publication	1
Mutagenesisⁱ	272	R → V: Abolishes the synergistic activity with SMAD3 to activate TGF-beta-mediated transcription. 1 Publication	1
Mutagenesisⁱ	286	T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-8; A-89; and A-93. 1 Publication	1

Keywords - Diseaseⁱ

Proto-oncogene

Organism-specific databases

DisGeNET More...DisGeNETⁱ	3725
Open Targets More...OpenTargetsⁱ	ENSG00000177606
PharmGKBⁱ	PA30006

Chemistry databases

ChEMBLⁱ	CHEMBL4977
Drug and drug target database More...DrugBankⁱ	DB01169 Arsenic trioxide DB01029 Irbesartan DB05785 LGD-1550 DB00852 Pseudoephedrine DB00570 Vinblastine

Polymorphism and mutation databases

BioMutaⁱ	JUN
DMDMⁱ	135298

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000076429	1 – 331	Transcription factor AP-1Add BLAST		331

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	2	Phosphothreonine; by PAK21 Publication	1
Modified residueⁱ	8	Phosphothreonine; by PAK21 Publication	1
Cross-linkⁱ	35	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linkⁱ	50	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residueⁱ	56	N6-acetyllysine; alternateBy similarity	1
Cross-linkⁱ	56	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residueⁱ	58	PhosphoserineCombined sources	1
Modified residueⁱ	63	Phosphoserine; by MAPK8 and PLK3Combined sources3 Publications	1
Cross-linkⁱ	70	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residueⁱ	73	Phosphoserine; by MAPK8 and PLK33 Publications	1
Modified residueⁱ	89	Phosphothreonine; by PAK21 Publication	1
Modified residueⁱ	91	Phosphothreonine1 Publication	1
Modified residueⁱ	93	Phosphothreonine; by PAK22 Publications	1
Cross-linkⁱ	226	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residueⁱ	239	Phosphothreonine; by GSK3-betaCombined sources1 Publication	1
Modified residueⁱ	243	Phosphoserine; by DYRK2 and GSK3-betaCombined sources2 Publications	1
Modified residueⁱ	249	Phosphoserine; by GSK3-beta2 Publications	1
Modified residueⁱ	271	N6-acetyllysine1 Publication	1
Modified residueⁱ	286	Phosphothreonine; by PAK21 Publication	1

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

EPDⁱ	P05412
jPOSTⁱ	P05412
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P05412
PaxDbⁱ	P05412
PeptideAtlas More...PeptideAtlasⁱ	P05412
PRIDEⁱ	P05412
ProteomicsDBⁱ	51836

PTM databases

iPTMnetⁱ	P05412
PhosphoSitePlusⁱ	P05412

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000177606 Expressed in 238 organ(s), highest expression level in amniotic fluid
CleanExⁱ	HS_JUN
Genevisibleⁱ	P05412 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB003801 CAB007780 HPA059474

HPAⁱ

CAB003801
CAB007780
HPA059474

Interactionⁱ

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

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
itself		5	EBI-852823,EBI-852823
APLP2	Q06481	3	EBI-852823,EBI-79306
APP	P05067	2	EBI-852823,EBI-77613
ATF1	P18846	2	EBI-852823,EBI-852794
ATF2	P15336	14	EBI-852823,EBI-1170906
ATF3	P18847	7	EBI-852823,EBI-712767
ATF4	P18848	2	EBI-852823,EBI-492498
ATF7	P17544	6	EBI-852823,EBI-765623
BATF	Q16520	2	EBI-852823,EBI-749503
BATF2	Q8N1L9-1	3	EBI-852823,EBI-15746052
BATF3	Q9NR55	4	EBI-852823,EBI-10312707
BBS7	Q8IWZ6	3	EBI-852823,EBI-1806001
CITED1	Q99966	2	EBI-852823,EBI-2624951
CREB3	O43889	4	EBI-852823,EBI-625002
ETS1	P14921	3	EBI-852823,EBI-913209
FOS	P01100	36	EBI-852823,EBI-852851
FOSL1	P15407	8	EBI-852823,EBI-744510
FOSL2	P15408	9	EBI-852823,EBI-3893419
GOPC	Q9HD26	3	EBI-852823,EBI-349832
HBZ	P0C746	3	EBI-852823,EBI-10890294	From Human T-cell leukemia virus 1 (strain Japan ATK-1 subtype A).
HSP90AA1	P07900	4	EBI-852823,EBI-296047
HSPA8	P11142	3	EBI-852823,EBI-351896
jnk-1	Q8WQG9	3	EBI-852823,EBI-321822	From Caenorhabditis elegans.
KPNA2	P52292	4	EBI-852823,EBI-349938
MAPK10	P53779	4	EBI-852823,EBI-713543
MAPK8	P45983	5	EBI-852823,EBI-286483
MAPK8	P45983-1	2	EBI-852823,EBI-288687
MAPRE3	Q9UPY8	3	EBI-852823,EBI-726739
Maz	P56671	2	EBI-852823,EBI-1809712	From Mus musculus.
MDM2	Q00987	3	EBI-852823,EBI-389668
MDV005	Q9DGW5	3	EBI-852823,EBI-10889526	From Gallid herpesvirus 2 (strain Chicken/Md5/ATCC VR-987).
MTA1	Q13330	4	EBI-852823,EBI-714236
NEFM	P07197	2	EBI-852823,EBI-1105035
NFATC1	O95644	5	EBI-852823,EBI-6907210
NFATC2	Q13469-2	6	EBI-852823,EBI-10087113
PRRC2A	P48634	2	EBI-852823,EBI-347545
SMAD2	Q15796	3	EBI-852823,EBI-1040141
STRN4	Q9NRL3	3	EBI-852823,EBI-717245
TCL1A	P56279	6	EBI-852823,EBI-749995
TUBA1A	Q71U36	3	EBI-852823,EBI-302552
TUBB	P07437	3	EBI-852823,EBI-350864
VRK1	Q99986	5	EBI-852823,EBI-1769146

GO - Molecular functionⁱ

enzyme binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 23382074
HMG box domain binding Source: Ensembl
identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 20102225
- 25609649
protein heterodimerization activity
Source: CAFA
Inferred from direct assayⁱ
- 10508860
protein homodimerization activity
Source: CAFA
Inferred from direct assayⁱ
- 10508860
RNA polymerase II activating transcription factor binding
Source: CAFA
Inferred from physical interactionⁱ
- 10508860
R-SMAD binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 9732876
transcription factor binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 16007074
ubiquitin-like protein ligase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 27458189
ubiquitin protein ligase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 14739464

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	109928, 252 interactors
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
CORUMⁱ	P05412
Database of interacting proteins More...DIPⁱ	DIP-5961N
ELMⁱ	P05412
IntActⁱ	P05412, 1378 interactors
Molecular INTeraction database More...MINTⁱ	P05412
STRINGⁱ	9606.ENSP00000360266

Chemistry databases

BindingDBⁱ

P05412

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Helixⁱ	255 – 310	Combined sources		56

Show more details

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1A02	X-ray	2.70	J	253-308	[»]
	1FOS	X-ray	3.05	F/H	254-315	[»]
	1JNM	X-ray	2.20	A/B	254-315	[»]
	1JUN	NMR	-	A/B	276-314	[»]
	1S9K	X-ray	3.10	E	257-308	[»]
	1T2K	X-ray	3.00	C	254-314	[»]
	5FV8	X-ray	1.99	D/E	277-308	[»]
	5T01	X-ray	1.89	A/B	254-315	[»]
ProteinModelPortalⁱ	P05412
SMRⁱ	P05412
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P05412

EvolutionaryTraceⁱ

P05412

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	252 – 315	bZIPPROSITE-ProRule annotationAdd BLAST		64

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	252 – 279	Basic motifPROSITE-ProRule annotationAdd BLAST		28
Regionⁱ	280 – 308	Leucine-zipperPROSITE-ProRule annotationAdd BLAST		29

Sequence similaritiesⁱ

Belongs to the bZIP family. Jun subfamily.Curated

Phylogenomic databases

eggNOGⁱ	KOG0837 Eukaryota ENOG410XRWH LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000162061
HOGENOMⁱ	HOG000006648
HOVERGENⁱ	HBG001722
InParanoidⁱ	P05412
KEGG Orthology (KO) More...KOⁱ	K04448
OMAⁱ	PVYEDLN
Database of Orthologous Groups More...OrthoDBⁱ	1090460at2759
PhylomeDBⁱ	P05412
TreeFamⁱ	TF323952

Family and domain databases

InterProⁱ	View protein in InterPro IPR004827 bZIP IPR015558 C_Jun/v-Jun IPR005643 JNK IPR002112 Leuzip_Jun IPR008917 TF_DNA-bd_sf
PANTHERⁱ	PTHR11462:SF8 PTHR11462:SF8, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00170 bZIP_1, 1 hit PF03957 Jun, 1 hit
PRINTSⁱ	PR00043 LEUZIPPRJUN
SMARTⁱ	View protein in SMART SM00338 BRLZ, 1 hit
SUPFAMⁱ	SSF47454 SSF47454, 1 hit
PROSITEⁱ	View protein in PROSITE PS50217 BZIP, 1 hit PS00036 BZIP_BASIC, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P05412-1 [UniParc]FASTA Add 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

Checksum:ⁱ0695E23AC4D33561

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	11	D → G AA sequence (PubMed:2825349).Curated	1
Sequence conflictⁱ	14	L → F AA sequence (PubMed:2825349).Curated	1
Sequence conflictⁱ	80	I → V AA sequence (PubMed:2825349).Curated	1
Sequence conflictⁱ	151	A → S in CAG46525 (Ref. 3) Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_012070	297	T → M. Corresponds to variant dbSNP:rs9989Ensembl.		1

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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS610.1
PIRⁱ	A31264 TVHUJN
NCBI Reference Sequences More...RefSeqⁱ	NP_002219.1, NM_002228.3
UniGeneⁱ	Hs.696684

Genome annotation databases

Ensemblⁱ	ENST00000371222; ENSP00000360266; ENSG00000177606
GeneIDⁱ	3725
KEGGⁱ	hsa:3725
UCSC genome browser More...UCSCⁱ	uc001cze.4 human

Keywords - Coding sequence diversityⁱ

Polymorphism

Protein	Similar proteins		Species	Score	Length	Source
P05412	JUN isoform 1		PANTR		331	UniRef100_P05412

Protein	Similar proteins		Species	Score	Length	Source
P05412	JUN isoform 1		PANTR		331	UniRef90_P05412
transcription factor AP-1		DELLE		343
transcription factor AP-1		TURTR		342
Jun proto-oncogene, AP-1 transcription factor subunit		CANLF		341
transcription factor AP-1		PHYCD		338
+73

Protein	Similar proteins		Species	Score	Length	Source
P05412	JUN isoform 1		PANTR		331	UniRef50_P05412
transcription factor AP-1		DELLE		343
transcription factor AP-1		TURTR		342
Jun proto-oncogene, AP-1 transcription factor subunit		CANLF		341
transcription factor AP-1		PHYCD		338
+172

Cross-referencesⁱ

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
CCDSⁱ	CCDS610.1
PIRⁱ	A31264 TVHUJN
RefSeqⁱ	NP_002219.1, NM_002228.3
UniGeneⁱ	Hs.696684

3D structure databases

Select the link destinations: PDBeⁱ RCSB PDBⁱ PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1A02	X-ray	2.70	J	253-308	[»]
	1FOS	X-ray	3.05	F/H	254-315	[»]
	1JNM	X-ray	2.20	A/B	254-315	[»]
	1JUN	NMR	-	A/B	276-314	[»]
	1S9K	X-ray	3.10	E	257-308	[»]
	1T2K	X-ray	3.00	C	254-314	[»]
	5FV8	X-ray	1.99	D/E	277-308	[»]
	5T01	X-ray	1.89	A/B	254-315	[»]
ProteinModelPortalⁱ	P05412
SMRⁱ	P05412
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	109928, 252 interactors
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
CORUMⁱ	P05412
DIPⁱ	DIP-5961N
ELMⁱ	P05412
IntActⁱ	P05412, 1378 interactors
MINTⁱ	P05412
STRINGⁱ	9606.ENSP00000360266

Chemistry databases

BindingDBⁱ	P05412
ChEMBLⁱ	CHEMBL4977
DrugBankⁱ	DB01169 Arsenic trioxide DB01029 Irbesartan DB05785 LGD-1550 DB00852 Pseudoephedrine DB00570 Vinblastine

PTM databases

iPTMnetⁱ	P05412
PhosphoSitePlusⁱ	P05412

Polymorphism and mutation databases

BioMutaⁱ	JUN
DMDMⁱ	135298

Proteomic databases

EPDⁱ	P05412
jPOSTⁱ	P05412
MaxQBⁱ	P05412
PaxDbⁱ	P05412
PeptideAtlasⁱ	P05412
PRIDEⁱ	P05412
ProteomicsDBⁱ	51836

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	3725
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000371222; ENSP00000360266; ENSG00000177606
GeneIDⁱ	3725
KEGGⁱ	hsa:3725
UCSCⁱ	uc001cze.4 human

Organism-specific databases

CTDⁱ	3725
DisGeNETⁱ	3725
EuPathDBⁱ	HostDB:ENSG00000177606.6
GeneCardsⁱ	JUN
H-InvDBⁱ	HIX0000635
HGNCⁱ	HGNC:6204 JUN
HPAⁱ	CAB003801 CAB007780 HPA059474
MIMⁱ	165160 gene
neXtProtⁱ	NX_P05412
OpenTargetsⁱ	ENSG00000177606
PharmGKBⁱ	PA30006
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0837 Eukaryota ENOG410XRWH LUCA
GeneTreeⁱ	ENSGT00940000162061
HOGENOMⁱ	HOG000006648
HOVERGENⁱ	HBG001722
InParanoidⁱ	P05412
KOⁱ	K04448
OMAⁱ	PVYEDLN
OrthoDBⁱ	1090460at2759
PhylomeDBⁱ	P05412
TreeFamⁱ	TF323952

Enzyme and pathway databases

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
SignaLinkⁱ	P05412
SIGNORⁱ	P05412

Miscellaneous databases

ChiTaRSⁱ	JUN human
EvolutionaryTraceⁱ	P05412
GeneWikiⁱ	C-jun
GenomeRNAiⁱ	3725
Protein Ontology More...PROⁱ	PR:P05412
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000177606 Expressed in 238 organ(s), highest expression level in amniotic fluid
CleanExⁱ	HS_JUN
Genevisibleⁱ	P05412 HS

Family and domain databases

InterProⁱ	View protein in InterPro IPR004827 bZIP IPR015558 C_Jun/v-Jun IPR005643 JNK IPR002112 Leuzip_Jun IPR008917 TF_DNA-bd_sf
PANTHERⁱ	PTHR11462:SF8 PTHR11462:SF8, 1 hit
Pfamⁱ	View protein in Pfam PF00170 bZIP_1, 1 hit PF03957 Jun, 1 hit
PRINTSⁱ	PR00043 LEUZIPPRJUN
SMARTⁱ	View protein in SMART SM00338 BRLZ, 1 hit
SUPFAMⁱ	SSF47454 SSF47454, 1 hit
PROSITEⁱ	View protein in PROSITE PS50217 BZIP, 1 hit PS00036 BZIP_BASIC, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	JUN_HUMAN
Accessionⁱ	P05412Primary (citable) accession number: P05412 Secondary accession number(s): Q6FHM7, Q96G93
Entry historyⁱ	Integrated 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.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

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UniProtKB - P05412 (JUN_HUMAN)

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Transcription factor AP-1

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

Sites

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GO - Biological processi

Enzyme and pathway databases

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

Organism-specific databases

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

Nucleus

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Keywords - Cellular componenti

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

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Keywords - Diseasei

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

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

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

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

Gene expression databases

Organism-specific databases

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

GO - Molecular functioni

Protein-protein interaction databases

Chemistry 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

Miscellaneous 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

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<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

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Experimental Info

Natural variant

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

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<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

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation 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

Keywords - Technical termi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ