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P17325 (JUN_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Gene names
Name:Jun
Synonyms:Rjg-9
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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 By similarity.

Subunit structure

Heterodimer with either FOS or BATF3 or ATF7 By similarity. The ATF7/JUN heterodimer is essential for ATF7 transactivation activity. Interacts with MYBBP1A, SP1, SPIB and TCF20. Interacts with COPS5; indirectly leading to its phosphorylation. Interacts with DSIPI; this interaction inhibits the binding of active AP1 to its target DNA. Interacts with HIVEP3. 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. 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. Binds to HIPK3 By similarity. Interacts with RNF187. Ref.5 Ref.6

Subcellular location

Nucleus By similarity.

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 PLK3 following hypoxia or UV irradiation, leading to increase DNA-binding activity By similarity.

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: Compara

SMAD protein signal transduction

Inferred from electronic annotation. Source: Compara

aging

Inferred from expression pattern PubMed 11389931. Source: RGD

angiogenesis

Inferred from mutant phenotype PubMed 15126605. Source: RGD

axon regeneration

Inferred from electronic annotation. Source: Compara

cellular response to calcium ion

Inferred from electronic annotation. Source: Compara

cellular response to potassium ion starvation

Inferred from mutant phenotype PubMed 17428807. Source: RGD

circadian rhythm

Inferred from expression pattern PubMed 10987819. Source: RGD

leading edge cell differentiation

Inferred from electronic annotation. Source: Compara

learning

Inferred from mutant phenotype PubMed 7948848. Source: RGD

liver development

Inferred from electronic annotation. Source: Compara

membrane depolarization

Inferred from direct assay PubMed 11571252. Source: RGD

microglial cell activation

Inferred from electronic annotation. Source: Compara

monocyte differentiation

Inferred from electronic annotation. Source: Compara

negative regulation by host of viral transcription

Inferred from electronic annotation. Source: Compara

negative regulation of DNA binding

Inferred from electronic annotation. Source: Compara

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Compara

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Compara

negative regulation of protein autophosphorylation

Inferred from electronic annotation. Source: Compara

negative regulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: Compara

outflow tract morphogenesis

Inferred from electronic annotation. Source: Compara

positive regulation by host of viral transcription

Inferred from electronic annotation. Source: Compara

positive regulation of DNA replication

Inferred from mutant phenotype PubMed 9487126. Source: RGD

positive regulation of endothelial cell proliferation

Inferred from electronic annotation. Source: Compara

positive regulation of fibroblast proliferation

Inferred from electronic annotation. Source: Compara

positive regulation of monocyte differentiation

Inferred from direct assay PubMed 7947389. Source: RGD

positive regulation of neuron apoptotic process

Inferred from mutant phenotype PubMed 12514131PubMed 15664113. Source: RGD

positive regulation of smooth muscle cell proliferation

Inferred from direct assay PubMed 11571252. Source: RGD

regulation of cell cycle

Inferred from electronic annotation. Source: Compara

release of cytochrome c from mitochondria

Inferred from mutant phenotype PubMed 11301023. Source: RGD

response to cAMP

Inferred from expression pattern PubMed 18280640. Source: RGD

response to cytokine stimulus

Inferred from expression pattern PubMed 18280640. Source: RGD

response to drug

Inferred from expression pattern PubMed 12093589. Source: RGD

response to hydrogen peroxide

Inferred from expression pattern PubMed 11053775. Source: RGD

response to lipopolysaccharide

Inferred from expression pattern PubMed 11389931. Source: RGD

response to mechanical stimulus

Inferred from expression pattern PubMed 15126239. Source: RGD

response to radiation

Inferred from direct assay PubMed 18439036. Source: RGD

transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Compara

   Cellular_componentcytosol

Inferred from direct assay PubMed 14512277. Source: RGD

nuclear euchromatin

Inferred from electronic annotation. Source: Compara

nucleus

Inferred from direct assay PubMed 10830307PubMed 10837920PubMed 12753154PubMed 14512277. Source: RGD

transcription factor complex

Inferred from electronic annotation. Source: Compara

transcriptional repressor complex

Inferred from electronic annotation. Source: Compara

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

Inferred from mutant phenotype PubMed 17428807. Source: RGD

RNA polymerase II distal enhancer sequence-specific DNA binding

Inferred from electronic annotation. Source: Compara

Rho GTPase activator activity

Inferred from electronic annotation. Source: Compara

cAMP response element binding

Inferred from electronic annotation. Source: Compara

double-stranded DNA binding

Inferred from direct assay PubMed 10830307PubMed 10837920PubMed 14512277. Source: RGD

protein heterodimerization activity

Traceable author statement PubMed 14512277. Source: RGD

protein homodimerization activity

Inferred from direct assay PubMed 9369238. Source: RGD

sequence-specific DNA binding

Inferred from direct assay PubMed 10830307PubMed 10837920PubMed 12753154PubMed 17428807. Source: RGD

transcription coactivator activity

Inferred from electronic annotation. Source: Compara

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 334334Transcription factor AP-1
PRO_0000076432

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 similarity
Modified residue81Phosphothreonine By similarity
Modified residue581Phosphoserine By similarity
Modified residue631Phosphoserine; by MAPK8 and PLK3 By similarity
Modified residue731Phosphoserine; by MAPK8 and PLK3 By similarity
Modified residue891Phosphothreonine By similarity
Modified residue931Phosphothreonine 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 similarity

Sequences

Sequence LengthMass (Da)Tools
P17325 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: AFD9DF7D7C791B58

FASTA33436,001
        10         20         30         40         50         60 
MTAKMETTFY DDALNASFLQ SESGAYGYSN PKILKQSMTL NLADPVGNLK 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 GATGLAFPSQ 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]"Structure and expression of the rat c-jun messenger RNA: tissue distribution and increase during chemical hepatocarcinogenesis."
Sakai M., Okuda A., Hatayama I., Sato K., Nishi S., Muramatsu M.
Cancer Res. 49:5633-5637(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Nucleotide sequence of rat c-jun protooncogene."
Kitabayashi I., Saka F., Gachelin G., Yokoyama K.
Nucleic Acids Res. 18:3400-3400(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Fischer.
[3]"Transcriptional regulation of the c-jun gene by retinoic acid and E1A during differentiation of F9 cells."
Kitabayashi I., Kawakami Z., Chiu R., Ozawa K., Matsuoka T., Toyoshima S., Umesono K., Evans R.M., Gachelin G., Yokoyama K.
EMBO J. 11:167-175(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Fischer.
[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: Lung.
[5]"Isolation of an AP-1 repressor by a novel method for detecting protein-protein interactions."
Aronheim A., Zandi E., Hennemann H., Elledge S.J., Karin M.
Mol. Cell. Biol. 17:3094-3102(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BATF3.
[6]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X17163 mRNA. Translation: CAA35041.1.
X17215 Genomic DNA. Translation: CAA35084.1.
BC078738 mRNA. Translation: AAH78738.1.
IPIIPI00215370.
PIRS12742.
RefSeqNP_068607.1. NM_021835.3.
UniGeneRn.93714.

3D structure databases

ProteinModelPortalP17325.
SMRP17325. Positions 260-311.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-653N.
MINTMINT-220059.
STRING10116.ENSRNOP00000011732.

PTM databases

PhosphoSiteP17325.

Proteomic databases

PRIDEP17325.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000011731; ENSRNOP00000011732; ENSRNOG00000026293.
GeneID24516.
KEGGrno:24516.
UCSCRGD:2943. rat.

Organism-specific databases

CTD3725.
RGD2943. Jun.

Phylogenomic databases

eggNOGNOG283376.
GeneTreeENSGT00390000009929.
HOGENOMHOG000006648.
HOVERGENHBG001722.
InParanoidP17325.
KOK04448.
OMAMPVQHPR.
OrthoDBEOG4RV2RS.

Gene expression databases

GenevestigatorP17325.
GermOnlineENSRNOG00000026293. Rattus norvegicus.

Family and domain databases

Gene3D1.10.880.10. 1 hit.
InterProIPR004827. bZIP.
IPR015558. C_Jun.
IPR008917. Euk_TF_DNA-bd.
IPR005643. JNK.
IPR002112. Leuzip_Jun.
[Graphical view]
PANTHERPTHR11462:SF8. PTHR11462:SF8. 1 hit.
PfamPF00170. bZIP_1. 1 hit.
PF03957. Jun. 1 hit.
[Graphical view]
PRINTSPR00043. LEUZIPPRJUN.
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
SUPFAMSSF47454. Euk_transcr_DNA. 1 hit.
PROSITEPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio603545.

Entry information

Entry nameJUN_RAT
AccessionPrimary (citable) accession number: P17325
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: April 3, 2013
This is version 123 of the entry and version 1 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