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Transcription factor AP-1 (Activator protein 1) (AP1) (Proto-oncogene c-Jun) (V-jun avian sarcoma virus 17 oncogene homolog)

 JUN_RAT                 Reviewed;         334 AA.
P17325;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
01-AUG-1990, sequence version 1.
25-OCT-2017, entry version 164.
RecName: Full=Transcription factor AP-1;
AltName: Full=Activator protein 1;
Short=AP1;
AltName: Full=Proto-oncogene c-Jun;
AltName: Full=V-jun avian sarcoma virus 17 oncogene homolog;
Name=Jun; Synonyms=Rjg-9;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=2507134;
Sakai M., Okuda A., Hatayama I., Sato K., Nishi S., Muramatsu M.;
"Structure and expression of the rat c-jun messenger RNA: tissue
distribution and increase during chemical hepatocarcinogenesis.";
Cancer Res. 49:5633-5637(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Fischer;
PubMed=2113275; DOI=10.1093/nar/18.11.3400;
Kitabayashi I., Saka F., Gachelin G., Yokoyama K.;
"Nucleotide sequence of rat c-jun protooncogene.";
Nucleic Acids Res. 18:3400-3400(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Fischer;
PubMed=1310930;
Kitabayashi I., Kawakami Z., Chiu R., Ozawa K., Matsuoka T.,
Toyoshima S., Umesono K., Evans R.M., Gachelin G., Yokoyama K.;
"Transcriptional regulation of the c-jun gene by retinoic acid and E1A
during differentiation of F9 cells.";
EMBO J. 11:167-175(1992).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH BATF3.
PubMed=9154808; DOI=10.1128/MCB.17.6.3094;
Aronheim A., Zandi E., Hennemann H., Elledge S.J., Karin M.;
"Isolation of an AP-1 repressor by a novel method for detecting
protein-protein interactions.";
Mol. Cell. Biol. 17:3094-3102(1997).
[6]
INTERACTION WITH RNF187.
PubMed=20852630; DOI=10.1038/ncb2098;
Davies C.C., Chakraborty A., Cipriani F., Haigh K., Haigh J.J.,
Behrens A.;
"Identification of a co-activator that links growth factor signalling
to c-Jun/AP-1 activation.";
Nat. Cell Biol. 12:963-972(2010).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[8]
INTERACTION WITH PRR7, AND UBIQUITINATION.
PubMed=27458189; DOI=10.15252/embj.201593070;
Kravchick D.O., Karpova A., Hrdinka M., Lopez-Rojas J., Iacobas S.,
Carbonell A.U., Iacobas D.A., Kreutz M.R., Jordan B.A.;
"Synaptonuclear messenger PRR7 inhibits c-Jun ubiquitination and
regulates NMDA-mediated excitotoxicity.";
EMBO J. 35:1923-1934(2016).
-!- 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. Involved in activated KRAS-mediated transcriptional
activation of USP28 in colorectal cancer (CRC) cells. Binds to the
USP28 promoter in colorectal cancer (CRC) cells.
{ECO:0000250|UniProtKB:P05412}.
-!- SUBUNIT: 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). Interacts with PRR7
(PubMed:27458189). Found in a complex with PRR7 and FBXW7 (By
similarity). Interacts with PRR7 and FBXW7; the interaction
inhibits ubiquitination-mediated JUN degradation promoting its
phosphorylation and transcriptional activity (By similarity).
{ECO:0000250|UniProtKB:P05412, ECO:0000250|UniProtKB:P05627,
ECO:0000269|PubMed:20852630, ECO:0000269|PubMed:27458189,
ECO:0000269|PubMed:9154808}.
-!- INTERACTION:
P49185:Mapk8; NbExp=2; IntAct=EBI-7709365, EBI-7456505;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P05412}.
-!- PTM: 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). {ECO:0000250|UniProtKB:P05412}.
-!- PTM: Ubiquitinated (PubMed:27458189). Ubiquitination by the
SCF(FBXW7) is leading to its degradation (By similarity).
Ubiquitination takes place following phosphorylation, that
promotes interaction with FBXW7 (By similarity).
{ECO:0000250|UniProtKB:P05412, ECO:0000269|PubMed:27458189}.
-!- PTM: Acetylated at Lys-271 by EP300.
{ECO:0000250|UniProtKB:P05412}.
-!- SIMILARITY: Belongs to the bZIP family. Jun subfamily.
{ECO:0000305}.
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EMBL; X17163; CAA35041.1; -; mRNA.
EMBL; X17215; CAA35084.1; -; Genomic_DNA.
EMBL; BC078738; AAH78738.1; -; mRNA.
PIR; S12742; S12742.
RefSeq; NP_068607.1; NM_021835.3.
UniGene; Rn.93714; -.
ProteinModelPortal; P17325; -.
SMR; P17325; -.
BioGrid; 246671; 6.
CORUM; P17325; -.
DIP; DIP-653N; -.
IntAct; P17325; 3.
MINT; MINT-220059; -.
STRING; 10116.ENSRNOP00000011732; -.
BindingDB; P17325; -.
ChEMBL; CHEMBL3341579; -.
iPTMnet; P17325; -.
PhosphoSitePlus; P17325; -.
PaxDb; P17325; -.
PRIDE; P17325; -.
Ensembl; ENSRNOT00000011731; ENSRNOP00000011732; ENSRNOG00000026293.
GeneID; 24516; -.
KEGG; rno:24516; -.
UCSC; RGD:2943; rat.
CTD; 3725; -.
RGD; 2943; Jun.
eggNOG; KOG0837; Eukaryota.
eggNOG; ENOG410XRWH; LUCA.
GeneTree; ENSGT00390000009929; -.
HOGENOM; HOG000006648; -.
HOVERGEN; HBG001722; -.
InParanoid; P17325; -.
KO; K04448; -.
OMA; KDHVAQL; -.
OrthoDB; EOG091G0N0L; -.
PhylomeDB; P17325; -.
TreeFam; TF323952; -.
Reactome; R-RNO-2559580; Oxidative Stress Induced Senescence.
Reactome; R-RNO-2871796; FCERI mediated MAPK activation.
Reactome; R-RNO-450341; Activation of the AP-1 family of transcription factors.
PRO; PR:P17325; -.
Proteomes; UP000002494; Chromosome 5.
Bgee; ENSRNOG00000026293; -.
Genevisible; P17325; RN.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005719; C:nuclear euchromatin; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0035976; C:transcription factor AP-1 complex; IEA:Ensembl.
GO; GO:0005667; C:transcription factor complex; IBA:GO_Central.
GO; GO:0017053; C:transcriptional repressor complex; IEA:Ensembl.
GO; GO:0033613; F:activating transcription factor binding; IPI:RGD.
GO; GO:0035497; F:cAMP response element binding; IEA:Ensembl.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
GO; GO:0005096; F:GTPase activator activity; IEA:Ensembl.
GO; GO:0071837; F:HMG box domain binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IPI:RGD.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0070412; F:R-SMAD binding; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; IEA:Ensembl.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IEA:Ensembl.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; IEA:Ensembl.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IMP:RGD.
GO; GO:0008134; F:transcription factor binding; IPI:RGD.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISS:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IMP:RGD.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0001525; P:angiogenesis; IMP:RGD.
GO; GO:0031103; P:axon regeneration; IEA:Ensembl.
GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl.
GO; GO:0032870; P:cellular response to hormone stimulus; IBA:GO_Central.
GO; GO:0051365; P:cellular response to potassium ion starvation; IMP:RGD.
GO; GO:0034614; P:cellular response to reactive oxygen species; IEA:Ensembl.
GO; GO:0007623; P:circadian rhythm; IEP:RGD.
GO; GO:0061029; P:eyelid development in camera-type eye; IEA:Ensembl.
GO; GO:0035026; P:leading edge cell differentiation; IEA:Ensembl.
GO; GO:0007612; P:learning; IMP:RGD.
GO; GO:0001889; P:liver development; IEA:Ensembl.
GO; GO:0051899; P:membrane depolarization; IDA:RGD.
GO; GO:0001774; P:microglial cell activation; IEA:Ensembl.
GO; GO:0030224; P:monocyte differentiation; IEA:Ensembl.
GO; GO:0043922; P:negative regulation by host of viral transcription; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0043392; P:negative regulation of DNA binding; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0031953; P:negative regulation of protein autophosphorylation; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:1990441; P:negative regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IEA:Ensembl.
GO; GO:0003151; P:outflow tract morphogenesis; IEA:Ensembl.
GO; GO:0043923; P:positive regulation by host of viral transcription; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:RGD.
GO; GO:0045740; P:positive regulation of DNA replication; IMP:RGD.
GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; IEA:Ensembl.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
GO; GO:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
GO; GO:0045657; P:positive regulation of monocyte differentiation; IDA:RGD.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:RGD.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:RGD.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:RGD.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
GO; GO:0001836; P:release of cytochrome c from mitochondria; IMP:RGD.
GO; GO:0051591; P:response to cAMP; IEP:RGD.
GO; GO:0034097; P:response to cytokine; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
GO; GO:0035994; P:response to muscle stretch; IEA:Ensembl.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0009314; P:response to radiation; IDA:RGD.
GO; GO:0007184; P:SMAD protein import into nucleus; IEA:Ensembl.
GO; GO:0060395; P:SMAD protein signal transduction; IEA:Ensembl.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; IMP:RGD.
GO; GO:0006351; P:transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
Gene3D; 1.10.880.10; -; 1.
InterPro; IPR004827; bZIP.
InterPro; IPR015558; C_Jun/v-Jun.
InterPro; IPR005643; JNK.
InterPro; IPR002112; Leuzip_Jun.
InterPro; IPR008917; TF_DNA-bd.
PANTHER; PTHR11462:SF8; PTHR11462:SF8; 1.
Pfam; PF00170; bZIP_1; 1.
Pfam; PF03957; Jun; 1.
PRINTS; PR00043; LEUZIPPRJUN.
SMART; SM00338; BRLZ; 1.
SUPFAM; SSF47454; SSF47454; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
1: Evidence at protein level;
Acetylation; Activator; Complete proteome; DNA-binding;
Isopeptide bond; Nucleus; Phosphoprotein; Proto-oncogene;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 334 Transcription factor AP-1.
/FTId=PRO_0000076432.
DOMAIN 255 318 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 255 282 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 283 311 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
SITE 275 275 Necessary for synergistic transcriptional
activity with SMAD3. {ECO:0000250}.
MOD_RES 2 2 Phosphothreonine; by PAK2.
{ECO:0000250|UniProtKB:P05412}.
MOD_RES 8 8 Phosphothreonine; by PAK2.
{ECO:0000250|UniProtKB:P05412}.
MOD_RES 56 56 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P05627}.
MOD_RES 58 58 Phosphoserine.
{ECO:0000250|UniProtKB:P05412}.
MOD_RES 63 63 Phosphoserine; by MAPK8 and PLK3.
{ECO:0000250|UniProtKB:P05412}.
MOD_RES 73 73 Phosphoserine; by MAPK8 and PLK3.
{ECO:0000250|UniProtKB:P05412}.
MOD_RES 89 89 Phosphothreonine; by PAK2.
{ECO:0000250|UniProtKB:P05412}.
MOD_RES 91 91 Phosphothreonine.
{ECO:0000250|UniProtKB:P05412}.
MOD_RES 93 93 Phosphothreonine; by PAK2.
{ECO:0000250|UniProtKB:P05412}.
MOD_RES 242 242 Phosphothreonine; by GSK3-beta.
{ECO:0000250|UniProtKB:P05412}.
MOD_RES 246 246 Phosphoserine; by DYRK2 and GSK3-beta.
{ECO:0000250|UniProtKB:P05412}.
MOD_RES 252 252 Phosphoserine; by GSK3-beta.
{ECO:0000250|UniProtKB:P05412}.
MOD_RES 274 274 N6-acetyllysine.
{ECO:0000250|UniProtKB:P05412}.
MOD_RES 289 289 Phosphothreonine; by PAK2.
{ECO:0000250|UniProtKB:P05412}.
CROSSLNK 35 35 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05412}.
CROSSLNK 50 50 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05412}.
CROSSLNK 56 56 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P05412}.
CROSSLNK 70 70 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05412}.
CROSSLNK 229 229 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05412}.
SEQUENCE 334 AA; 36001 MW; AFD9DF7D7C791B58 CRC64;
MTAKMETTFY DDALNASFLQ SESGAYGYSN PKILKQSMTL NLADPVGNLK PHLRAKNSDL
LTSPDVGLLK LASPELERLI IQSSNGHITT TPTPTQFLCP KNVTDEQEGF AEGFVRALAE
LHSQNTLPSV TSAAQPVSGA GMVAPAVASV AGAGGGGGYS ASLHSEPPVY ANLSNFNPGA
LSSGGGAPSY GATGLAFPSQ PQQQQQPPQP PHHLPQQIPV QHPRLQALKE EPQTVPEMPG
ETPPLSPIDM ESQERIKAER KRMRNRIAAS KCRKRKLERI ARLEEKVKTL KAQNSELAST
ANMLREQVAQ LKQKVMNHVN SGCQLMLTQQ LQTF


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