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P05627 (JUN_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor AP-1
Alternative name(s):
AH119
Activator protein 1
Short name=AP1
Proto-oncogene c-Jun
V-jun avian sarcoma virus 17 oncogene homolog
Short name=Jun A
Gene names
Name:Jun
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length334 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.8

Subunit structure

Heterodimer with either FOS or BATF3 or ATF7 By similarity. The ATF7/JUN heterodimer is essential for ATF7 transactivation activity. Interacts with SP1, SPIB and TCF20. Interacts with COPS5; the interaction leads indirectly to its phosphorylation. Component of the SMAD3/SMAD4/JUN/FOS/complex which forms at the AP1 promoter site. The SMAD3/SMAD4 heterodimer acts syngernistically with the JUN/FOS heterodimer to activate transcription in response to TGF-beta By similarity. 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 By similarity. Interacts with DSIPI; the interaction inhibits the binding of active AP1 to its target DNA. Interacts with HIVEP3 and MYBBP1A. Interacts with methylated RNF187. Binds to HIPK3. Ref.5 Ref.6 Ref.7 Ref.10

Subcellular location

Nucleus.

Post-translational modification

Phosphorylated by CaMK4 and PRKDC; phosphorylation enhances the transcriptional activity. Phosphorylated by HIPK3. Phosphorylated by DYRK2 at Ser-246; this primes the protein for subsequent phosphorylation by GSK3B at Thr-242. Phosphorylated at Thr-242, Ser-246 and Ser-252 by GSK3B; phosphorylation reduces its ability to bind DNA. Phosphorylated by PAK2 at Thr-2, Thr-8, Thr-89, Thr-93 and Thr-289 thereby promoting JUN-mediated cell proliferation and transformation. Phosphorylated by PLK3 following hypoxia or UV irradiation, leading to increase DNA-binding activity By similarity. Ref.8

Acetylated at Lys-271 by EP300 By similarity.

Sequence similarities

Belongs to the bZIP family. Jun subfamily.

Contains 1 bZIP (basic-leucine zipper) domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DiseaseProto-oncogene
   LigandDNA-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processSMAD protein import into nucleus

Inferred from electronic annotation. Source: Ensembl

SMAD protein signal transduction

Inferred from electronic annotation. Source: Ensembl

aging

Inferred from electronic annotation. Source: Ensembl

angiogenesis

Inferred from mutant phenotype PubMed 16847049. Source: MGI

axon regeneration

Inferred from mutant phenotype PubMed 15233917. Source: MGI

cellular process

Inferred from mutant phenotype PubMed 11818961. Source: MGI

cellular response to calcium ion

Inferred from direct assay PubMed 19303854. Source: MGI

cellular response to potassium ion starvation

Inferred from electronic annotation. Source: Ensembl

circadian rhythm

Inferred from electronic annotation. Source: Ensembl

leading edge cell differentiation

Inferred from mutant phenotype PubMed 12791271. Source: MGI

learning

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from mutant phenotype PubMed 10352021. Source: MGI

membrane depolarization

Inferred from electronic annotation. Source: Ensembl

microglial cell activation

Inferred from mutant phenotype PubMed 15233917. Source: MGI

monocyte differentiation

Inferred from mutant phenotype PubMed 18326819. Source: MGI

negative regulation by host of viral transcription

Inferred from electronic annotation. Source: Ensembl

negative regulation of DNA binding

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 10352021. Source: MGI

negative regulation of cell proliferation

Inferred from genetic interaction PubMed 16007074. Source: MGI

negative regulation of neuron apoptotic process

Inferred from mutant phenotype PubMed 15233917. Source: MGI

negative regulation of protein autophosphorylation

Inferred from mutant phenotype PubMed 16916642. Source: MGI

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

outflow tract morphogenesis

Inferred from mutant phenotype PubMed 10352021. Source: MGI

positive regulation by host of viral transcription

Inferred from electronic annotation. Source: Ensembl

positive regulation of DNA replication

Inferred from electronic annotation. Source: Ensembl

positive regulation of endothelial cell proliferation

Inferred from mutant phenotype PubMed 16847049. Source: MGI

positive regulation of fibroblast proliferation

Inferred from direct assay PubMed 17182846. Source: MGI

positive regulation of monocyte differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 12798298PubMed 17182846. Source: MGI

regulation of cell cycle

Inferred from mutant phenotype PubMed 11818961. Source: MGI

regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 11818961. Source: MGI

release of cytochrome c from mitochondria

Inferred from electronic annotation. Source: Ensembl

response to cAMP

Inferred from electronic annotation. Source: Ensembl

response to cytokine

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from direct assay PubMed 9098922. Source: MGI

response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

response to radiation

Inferred from electronic annotation. Source: Ensembl

transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Ensembl

nuclear euchromatin

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 12050152. Source: MGI

transcription factor complex

Inferred from direct assay PubMed 12798298PubMed 12943993. Source: MGI

transcriptional repressor complex

Inferred from physical interaction PubMed 17182846. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay PubMed 10076871PubMed 12798298PubMed 19477969. Source: MGI

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II distal enhancer sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

Rho GTPase activator activity

Inferred from electronic annotation. Source: Ensembl

cAMP response element binding

Inferred from electronic annotation. Source: Ensembl

double-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 10581243PubMed 11477071PubMed 17255944PubMed 23948297. Source: IntAct

transcription coactivator activity

Inferred from electronic annotation. Source: Ensembl

transcription regulatory region DNA binding

Inferred from direct assay PubMed 19303854. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Cdk6Q642612EBI-764369,EBI-847380
ESR1P033726EBI-764369,EBI-78473From a different organism.
Mapk8Q91Y862EBI-764369,EBI-298784

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 334334Transcription factor AP-1
PRO_0000076430

Regions

Domain255 – 31864bZIP
Region255 – 28228Basic motif By similarity
Region283 – 31129Leucine-zipper By similarity

Sites

Site2751Necessary for syngernistic transcriptional activity with SMAD3 By similarity

Amino acid modifications

Modified residue21Phosphothreonine; by PAK2 By similarity
Modified residue81Phosphothreonine; by PAK2 By similarity
Modified residue561N6-acetyllysine Ref.11
Modified residue581Phosphoserine By similarity
Modified residue631Phosphoserine; alternate Ref.9
Modified residue631Phosphoserine; by MAPK8 and PLK3; alternate By similarity
Modified residue731Phosphoserine; by MAPK8 and PLK3 Probable
Modified residue891Phosphothreonine; by PAK2 By similarity
Modified residue931Phosphothreonine; by PAK2 By similarity
Modified residue2421Phosphothreonine; by GSK3-beta By similarity
Modified residue2461Phosphoserine; by DYRK2 and GSK3-beta By similarity
Modified residue2521Phosphoserine; by GSK3-beta By similarity
Modified residue2741N6-acetyllysine By similarity
Modified residue2891Phosphothreonine; by PAK2 By similarity

Experimental info

Sequence conflict1831S → C in CAA31252. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P05627 [UniParc].

Last modified October 1, 1989. Version 3.
Checksum: 2BE0E4025B8B1CA3

FASTA33435,944
        10         20         30         40         50         60 
MTAKMETTFY DDALNASFLQ SESGAYGYSN PKILKQSMTL NLADPVGSLK PHLRAKNSDL 

        70         80         90        100        110        120 
LTSPDVGLLK LASPELERLI IQSSNGHITT TPTPTQFLCP KNVTDEQEGF AEGFVRALAE 

       130        140        150        160        170        180 
LHSQNTLPSV TSAAQPVSGA GMVAPAVASV AGAGGGGGYS ASLHSEPPVY ANLSNFNPGA 

       190        200        210        220        230        240 
LSSGGGAPSY GAAGLAFPSQ PQQQQQPPQP PHHLPQQIPV QHPRLQALKE EPQTVPEMPG 

       250        260        270        280        290        300 
ETPPLSPIDM ESQERIKAER KRMRNRIAAS KCRKRKLERI ARLEEKVKTL KAQNSELAST 

       310        320        330 
ANMLREQVAQ LKQKVMNHVN SGCQLMLTQQ LQTF 

« Hide

References

« Hide 'large scale' references
[1]"Transcriptional activation of c-jun during the G0/G1 transition in mouse fibroblasts."
Ryseck R.-P., Hirai S., Yaniv M., Bravo R.
Nature 334:535-537(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Induction of proto-oncogene JUN/AP-1 by serum and TPA."
Lamph W.W., Wamsley P., Sassone-Corsi P., Verma I.M.
Nature 334:629-631(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Induction of protooncogene c-jun by serum growth factors."
Ryder K., Nathans D.
Proc. Natl. Acad. Sci. U.S.A. 85:8464-8467(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary tumor.
[5]"Molecular cloning reveals that the p160 Myb-binding protein is a novel, predominantly nucleolar protein which may play a role in transactivation by Myb."
Tavner F.J., Simpson R., Tashiro S., Favier D., Jenkins N.A., Gilbert D.J., Copeland N.G., Macmillan E.M., Lutwyche J., Keough R.A., Ishii S., Gonda T.J.
Mol. Cell. Biol. 18:989-1002(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MYBBP1A.
[6]"Inhibition of AP-1 by the glucocorticoid-inducible protein GILZ."
Mittelstadt P.R., Ashwell J.D.
J. Biol. Chem. 276:29603-29610(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DSIPI.
[7]"Schnurri-3 (KRC) interacts with c-Jun to regulate the IL-2 gene in T cells."
Oukka M., Wein M.N., Glimcher L.H.
J. Exp. Med. 199:15-24(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIVEP3, FUNCTION.
[8]"Cyclic AMP stimulates SF-1-dependent CYP11A1 expression through homeodomain-interacting protein kinase 3-mediated Jun N-terminal kinase and c-Jun phosphorylation."
Lan H.-C., Li H.-J., Lin G., Lai P.-Y., Chung B.-C.
Mol. Cell. Biol. 27:2027-2036(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION BY HIPK3.
[9]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Identification of a co-activator that links growth factor signalling to c-Jun/AP-1 activation."
Davies C.C., Chakraborty A., Cipriani F., Haigh K., Haigh J.J., Behrens A.
Nat. Cell Biol. 12:963-972(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNF187.
[11]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-56, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X12761 mRNA. Translation: CAA31252.1.
X12740 mRNA. Translation: CAA31236.1.
J04115 mRNA. Translation: AAA37419.1.
BC002081 mRNA. Translation: AAH02081.1.
BC021888 mRNA. Translation: AAH21888.1.
CCDSCCDS18364.1.
PIRTVMSJA. A31345.
RefSeqNP_034721.1. NM_010591.2.
UniGeneMm.275071.

3D structure databases

ProteinModelPortalP05627.
SMRP05627. Positions 260-311.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200871. 40 interactions.
DIPDIP-1068N.
IntActP05627. 5 interactions.
MINTMINT-209953.

Chemistry

ChEMBLCHEMBL5369.

PTM databases

PhosphoSiteP05627.

Proteomic databases

PaxDbP05627.
PRIDEP05627.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000058555; ENSMUSP00000054270; ENSMUSG00000052684.
ENSMUST00000107094; ENSMUSP00000102711; ENSMUSG00000052684.
GeneID16476.
KEGGmmu:16476.
UCSCuc008tsq.2. mouse.

Organism-specific databases

CTD3725.
MGIMGI:96646. Jun.

Phylogenomic databases

eggNOGNOG283376.
HOGENOMHOG000006648.
HOVERGENHBG001722.
InParanoidP05627.
KOK04448.
OMAAELHNQN.
OrthoDBEOG75MVXV.
PhylomeDBP05627.
TreeFamTF323952.

Gene expression databases

ArrayExpressP05627.
BgeeP05627.
CleanExMM_JUN.
GenevestigatorP05627.

Family and domain databases

Gene3D1.10.880.10. 1 hit.
InterProIPR004827. bZIP.
IPR005643. JNK.
IPR002112. Leuzip_Jun.
IPR008917. TF_DNA-bd.
[Graphical view]
PfamPF00170. bZIP_1. 1 hit.
PF03957. Jun. 1 hit.
[Graphical view]
PRINTSPR00043. LEUZIPPRJUN.
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
SUPFAMSSF47454. SSF47454. 1 hit.
PROSITEPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio289763.
PROP05627.
SOURCESearch...

Entry information

Entry nameJUN_MOUSE
AccessionPrimary (citable) accession number: P05627
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 1, 1989
Last modified: July 9, 2014
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot