P17325 (JUN_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Jun
Synonyms:	Rjg-9

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	334 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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 domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Disease	Proto-oncogene
Ligand	DNA-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	aging Inferred from expression pattern. Source: RGD angiogenesis Inferred from mutant phenotype. Source: RGD cellular response to potassium ion starvation Inferred from mutant phenotype. Source: RGD circadian rhythm Inferred from expression pattern. Source: RGD learning Inferred from mutant phenotype. Source: RGD membrane depolarization Inferred from direct assay. Source: RGD positive regulation of DNA replication Inferred from mutant phenotype. Source: RGD positive regulation of monocyte differentiation Inferred from direct assay. Source: RGD positive regulation of neuron apoptosis Inferred from mutant phenotype. Source: RGD positive regulation of smooth muscle cell proliferation Inferred from direct assay. Source: RGD release of cytochrome c from mitochondria Inferred from mutant phenotype. Source: RGD response to cAMP Inferred from expression pattern. Source: RGD response to cytokine stimulus Inferred from expression pattern. Source: RGD response to drug Inferred from expression pattern. Source: RGD response to hydrogen peroxide Inferred from expression pattern. Source: RGD response to lipopolysaccharide Inferred from expression pattern. Source: RGD response to mechanical stimulus Inferred from expression pattern. Source: RGD response to organic cyclic compound Inferred from expression pattern. Source: RGD response to radiation Inferred from direct assay. Source: RGD
Cellular component	cytosol Inferred from direct assay. Source: RGD
Molecular function	HMG box domain binding Inferred from physical interaction. Source: UniProtKB RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Inferred from mutant phenotype. Source: RGD double-stranded DNA binding Inferred from direct assay. Source: RGD protein heterodimerization activity Inferred from physical interaction. Source: RGD protein homodimerization activity Inferred from direct assay. Source: RGD sequence-specific DNA binding Inferred from direct assay. Source: RGD transcription factor binding Inferred from physical interaction. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 334	334	Transcription factor AP-1		PRO_0000076432
Regions
	Domain	283 – 311	29	Leucine-zipper
	DNA binding	260 – 279	20	Basic motif
Sites
	Site	275	1	Necessary for syngernistic transcriptional activity with SMAD3 By similarity
Amino acid modifications
	Modified residue	58	1	Phosphoserine By similarity
	Modified residue	62	1	Phosphothreonine By similarity
	Modified residue	63	1	Phosphoserine; by MAPK8 and PLK3 By similarity
	Modified residue	73	1	Phosphoserine; by MAPK8 and PLK3 By similarity
	Modified residue	242	1	Phosphothreonine; by GSK3-beta By similarity
	Modified residue	246	1	Phosphoserine; by GSK3-beta By similarity
	Modified residue	252	1	Phosphoserine; by GSK3-beta By similarity
	Modified residue	271	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P17325 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: AFD9DF7D7C791B58	FASTA	334	36,001
	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

References

	« Hide 'large scale' referencesShow '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: 2507134] [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: 2113275] [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: 1310930] [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: 15489334] [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: 9154808] [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: 20852630] [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.
IPI	IPI00215370.
PIR	S12742.
RefSeq	NP_068607.1. NM_021835.3.
UniGene	Rn.225373. Rn.93714.
3D structure databases
ProteinModelPortal	P17325.
SMR	P17325. Positions 260-311.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-653N.
MINT	MINT-220059.
STRING	P17325.
PTM databases
PhosphoSite	P17325.
Proteomic databases
PRIDE	P17325.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000011731; ENSRNOP00000011732; ENSRNOG00000026293.
GeneID	24516.
KEGG	rno:24516.
UCSC	NM_021835. rat.
Organism-specific databases
CTD	3725.
RGD	2943. Jun.
Phylogenomic databases
eggNOG	maNOG17334.
GeneTree	ENSGT00390000009929.
HOVERGEN	HBG001722.
InParanoid	P17325.
OMA	KPHLRNK.
OrthoDB	EOG4RV2RS.
PhylomeDB	P17325.
Gene expression databases
ArrayExpress	P17325.
Genevestigator	P17325.
GermOnline	ENSRNOG00000026293. Rattus norvegicus.
Family and domain databases
InterPro	IPR004827. bZIP. IPR011616. bZIP_1. IPR015558. C_Jun. IPR008917. Euk_TF_DNA-bd. IPR005643. JNK. IPR002112. Leuzip_Jun. [Graphical view]
Gene3D	G3DSA:1.10.880.10. G3DSA:1.10.880.10. 1 hit.
KO	K04448.
PANTHER	PTHR11462:SF8. C_Jun. 1 hit.
Pfam	PF00170. bZIP_1. 1 hit. PF03957. Jun. 1 hit. [Graphical view]
PRINTS	PR00043. LEUZIPPRJUN.
SMART	SM00338. BRLZ. 1 hit. [Graphical view]
SUPFAM	SSF47454. Euk_transcr_DNA. 1 hit.
PROSITE	PS50217. BZIP. 1 hit. PS00036. BZIP_BASIC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	603545.

Entry information

Entry name

JUN_RAT

Accession

Primary (citable) accession number: P17325

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	December 14, 2011
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program