Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Transcription factor AP-1

Gene

Jun

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. Binds to the USP28 promoter in colorectal cancer (CRC) cells.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei275 – 2751Necessary for synergistic transcriptional activity with SMAD3By similarity

GO - Molecular functioni

  • activating transcription factor binding Source: RGD
  • cAMP response element binding Source: Ensembl
  • chromatin binding Source: Ensembl
  • double-stranded DNA binding Source: RGD
  • GTPase activator activity Source: Ensembl
  • HMG box domain binding Source: UniProtKB
  • poly(A) RNA binding Source: Ensembl
  • protein heterodimerization activity Source: RGD
  • protein homodimerization activity Source: RGD
  • RNA polymerase II distal enhancer sequence-specific DNA binding Source: Ensembl
  • sequence-specific DNA binding Source: RGD
  • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: RGD
  • transcription coactivator activity Source: Ensembl
  • transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding Source: Ensembl
  • transcription factor activity, sequence-specific DNA binding Source: RGD
  • transcription factor binding Source: RGD
  • transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

  • aging Source: RGD
  • angiogenesis Source: RGD
  • axon regeneration Source: Ensembl
  • cellular response to calcium ion Source: Ensembl
  • cellular response to potassium ion starvation Source: RGD
  • circadian rhythm Source: RGD
  • eyelid development in camera-type eye Source: Ensembl
  • leading edge cell differentiation Source: Ensembl
  • learning Source: RGD
  • liver development Source: Ensembl
  • membrane depolarization Source: RGD
  • microglial cell activation Source: Ensembl
  • monocyte differentiation Source: Ensembl
  • negative regulation by host of viral transcription Source: Ensembl
  • negative regulation of cell proliferation Source: Ensembl
  • negative regulation of DNA binding Source: Ensembl
  • negative regulation of neuron apoptotic process Source: Ensembl
  • negative regulation of protein autophosphorylation Source: Ensembl
  • negative regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress Source: Ensembl
  • outflow tract morphogenesis Source: Ensembl
  • positive regulation by host of viral transcription Source: Ensembl
  • positive regulation of apoptotic process Source: RGD
  • positive regulation of cell proliferation Source: RGD
  • positive regulation of DNA replication Source: RGD
  • positive regulation of DNA-templated transcription, initiation Source: Ensembl
  • 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: RGD
  • positive regulation of neuron apoptotic process Source: RGD
  • positive regulation of pri-miRNA transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of smooth muscle cell proliferation Source: RGD
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: RGD
  • Ras protein signal transduction Source: UniProtKB
  • regulation of cell cycle Source: Ensembl
  • release of cytochrome c from mitochondria Source: RGD
  • response to cAMP Source: RGD
  • response to cytokine Source: RGD
  • response to drug Source: RGD
  • response to hydrogen peroxide Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to mechanical stimulus Source: RGD
  • response to muscle stretch Source: Ensembl
  • response to organic cyclic compound Source: RGD
  • response to organic substance Source: RGD
  • response to radiation Source: RGD
  • SMAD protein import into nucleus Source: Ensembl
  • SMAD protein signal transduction Source: Ensembl
  • transcription, DNA-templated Source: UniProtKB
  • transcription from RNA polymerase II promoter Source: RGD
  • transforming growth factor beta receptor signaling pathway Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-RNO-2559580. Oxidative Stress Induced Senescence.
R-RNO-2871796. FCERI mediated MAPK activation.
R-RNO-450341. Activation of the AP-1 family of transcription factors.

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
Gene namesi
Name:Jun
Synonyms:Rjg-9
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi2943. Jun.

Subcellular locationi

  • Nucleus By similarity

GO - Cellular componenti

  • cytosol Source: RGD
  • nuclear euchromatin Source: Ensembl
  • nucleoplasm Source: Ensembl
  • nucleus Source: RGD
  • transcriptional repressor complex Source: Ensembl
  • transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

Chemistry

ChEMBLiCHEMBL3341579.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 334334Transcription factor AP-1PRO_0000076432Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21Phosphothreonine; by PAK2By similarity
Modified residuei8 – 81Phosphothreonine; by PAK2By similarity
Modified residuei56 – 561N6-acetyllysineBy similarity
Modified residuei58 – 581PhosphoserineBy similarity
Modified residuei63 – 631Phosphoserine; by MAPK8 and PLK3By similarity
Modified residuei73 – 731Phosphoserine; by MAPK8 and PLK3By similarity
Modified residuei89 – 891Phosphothreonine; by PAK2By similarity
Modified residuei91 – 911PhosphothreonineBy similarity
Modified residuei93 – 931Phosphothreonine; by PAK2By similarity
Modified residuei242 – 2421Phosphothreonine; by GSK3-betaBy similarity
Modified residuei246 – 2461Phosphoserine; by DYRK2 and GSK3-betaBy similarity
Modified residuei252 – 2521Phosphoserine; by GSK3-betaBy similarity
Modified residuei274 – 2741N6-acetyllysineBy similarity
Modified residuei289 – 2891Phosphothreonine; by PAK2By similarity

Post-translational modificationi

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).By similarity
Ubiquitinated by the SCF(FBXW7), leading to its degradation. Ubiquitination takes place following phosphorylation, that promotes interaction with FBXW7.By similarity
Acetylated at Lys-271 by EP300.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP17325.
PRIDEiP17325.

PTM databases

iPTMnetiP17325.
PhosphoSiteiP17325.

Expressioni

Gene expression databases

GenevisibleiP17325. RN.

Interactioni

Subunit structurei

Heterodimer with either FOS or BATF3 or ATF7 (PubMed:9154808). 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 synergistically 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 methylated RNF187 (PubMed:20852630). Interacts (when phosphorylated) with FBXW7 (By similarity).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Mapk8P491852EBI-7709365,EBI-7456505

GO - Molecular functioni

  • activating transcription factor binding Source: RGD
  • HMG box domain binding Source: UniProtKB
  • protein heterodimerization activity Source: RGD
  • protein homodimerization activity Source: RGD
  • transcription factor binding Source: RGD

Protein-protein interaction databases

BioGridi246671. 5 interactions.
DIPiDIP-653N.
IntActiP17325. 3 interactions.
MINTiMINT-220059.
STRINGi10116.ENSRNOP00000011732.

Structurei

3D structure databases

ProteinModelPortaliP17325.
SMRiP17325. Positions 260-311.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini255 – 31864bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni255 – 28228Basic motifPROSITE-ProRule annotationAdd
BLAST
Regioni283 – 31129Leucine-zipperPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the bZIP family. Jun subfamily.Curated
Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0837. Eukaryota.
ENOG410XRWH. LUCA.
GeneTreeiENSGT00390000009929.
HOGENOMiHOG000006648.
HOVERGENiHBG001722.
InParanoidiP17325.
KOiK04448.
OMAiAELHNQN.
OrthoDBiEOG75MVXV.
PhylomeDBiP17325.
TreeFamiTF323952.

Family and domain databases

Gene3Di1.10.880.10. 1 hit.
InterProiIPR004827. bZIP.
IPR015558. C_Jun/v-Jun.
IPR005643. JNK.
IPR002112. Leuzip_Jun.
IPR008917. TF_DNA-bd.
[Graphical view]
PANTHERiPTHR11462:SF8. PTHR11462:SF8. 1 hit.
PfamiPF00170. bZIP_1. 1 hit.
PF03957. Jun. 1 hit.
[Graphical view]
PRINTSiPR00043. LEUZIPPRJUN.
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
SUPFAMiSSF47454. SSF47454. 1 hit.
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P17325-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAKMETTFY DDALNASFLQ SESGAYGYSN PKILKQSMTL NLADPVGNLK
60 70 80 90 100
PHLRAKNSDL LTSPDVGLLK LASPELERLI IQSSNGHITT TPTPTQFLCP
110 120 130 140 150
KNVTDEQEGF AEGFVRALAE LHSQNTLPSV TSAAQPVSGA GMVAPAVASV
160 170 180 190 200
AGAGGGGGYS ASLHSEPPVY ANLSNFNPGA LSSGGGAPSY GATGLAFPSQ
210 220 230 240 250
PQQQQQPPQP PHHLPQQIPV QHPRLQALKE EPQTVPEMPG ETPPLSPIDM
260 270 280 290 300
ESQERIKAER KRMRNRIAAS KCRKRKLERI ARLEEKVKTL KAQNSELAST
310 320 330
ANMLREQVAQ LKQKVMNHVN SGCQLMLTQQ LQTF
Length:334
Mass (Da):36,001
Last modified:August 1, 1990 - v1
Checksum:iAFD9DF7D7C791B58
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17163 mRNA. Translation: CAA35041.1.
X17215 Genomic DNA. Translation: CAA35084.1.
BC078738 mRNA. Translation: AAH78738.1.
PIRiS12742.
RefSeqiNP_068607.1. NM_021835.3.
UniGeneiRn.93714.

Genome annotation databases

EnsembliENSRNOT00000011731; ENSRNOP00000011732; ENSRNOG00000026293.
GeneIDi24516.
KEGGirno:24516.
UCSCiRGD:2943. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17163 mRNA. Translation: CAA35041.1.
X17215 Genomic DNA. Translation: CAA35084.1.
BC078738 mRNA. Translation: AAH78738.1.
PIRiS12742.
RefSeqiNP_068607.1. NM_021835.3.
UniGeneiRn.93714.

3D structure databases

ProteinModelPortaliP17325.
SMRiP17325. Positions 260-311.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246671. 5 interactions.
DIPiDIP-653N.
IntActiP17325. 3 interactions.
MINTiMINT-220059.
STRINGi10116.ENSRNOP00000011732.

Chemistry

ChEMBLiCHEMBL3341579.

PTM databases

iPTMnetiP17325.
PhosphoSiteiP17325.

Proteomic databases

PaxDbiP17325.
PRIDEiP17325.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000011731; ENSRNOP00000011732; ENSRNOG00000026293.
GeneIDi24516.
KEGGirno:24516.
UCSCiRGD:2943. rat.

Organism-specific databases

CTDi3725.
RGDi2943. Jun.

Phylogenomic databases

eggNOGiKOG0837. Eukaryota.
ENOG410XRWH. LUCA.
GeneTreeiENSGT00390000009929.
HOGENOMiHOG000006648.
HOVERGENiHBG001722.
InParanoidiP17325.
KOiK04448.
OMAiAELHNQN.
OrthoDBiEOG75MVXV.
PhylomeDBiP17325.
TreeFamiTF323952.

Enzyme and pathway databases

ReactomeiR-RNO-2559580. Oxidative Stress Induced Senescence.
R-RNO-2871796. FCERI mediated MAPK activation.
R-RNO-450341. Activation of the AP-1 family of transcription factors.

Miscellaneous databases

PROiP17325.

Gene expression databases

GenevisibleiP17325. RN.

Family and domain databases

Gene3Di1.10.880.10. 1 hit.
InterProiIPR004827. bZIP.
IPR015558. C_Jun/v-Jun.
IPR005643. JNK.
IPR002112. Leuzip_Jun.
IPR008917. TF_DNA-bd.
[Graphical view]
PANTHERiPTHR11462:SF8. PTHR11462:SF8. 1 hit.
PfamiPF00170. bZIP_1. 1 hit.
PF03957. Jun. 1 hit.
[Graphical view]
PRINTSiPR00043. LEUZIPPRJUN.
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
SUPFAMiSSF47454. SSF47454. 1 hit.
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.
  7. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiJUN_RAT
AccessioniPrimary (citable) accession number: P17325
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: June 8, 2016
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.