Reviewed, UniProtKB/Swiss-Prot P17325 (JUN_RAT)

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.
Sequence processing	The displayed sequence is not processed.
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'.
Subunit structure	Heterodimer with either FOS or BATF3. Interacts with SMAD3/SMAD4 heterodimers. 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 By similarity.
Subcellular location	Nucleus.
Post-translational modification	Phosphorylation enhances the transcriptional activity. Phosphorylated by PRKDC 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	Phosphoprotein
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 positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype. 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 substance Inferred from expression pattern. Source: RGD transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: RGD
Cellular component	cytosol Inferred from direct assay. Source: RGD transcription factor complex Inferred from mutant phenotype. Source: RGD
Molecular function	RNA polymerase II transcription factor activity 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 activator activity Traceable author statement. Source: RGD transcription factor activity Inferred from mutant phenotype. 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
Amino acid modifications
	Modified residue	58	1	Phosphoserine By similarity
	Modified residue	63	1	Phosphoserine; by MAPK8 By similarity
	Modified residue	73	1	Phosphoserine; by MAPK8 By similarity
	Modified residue	242	1	Phosphothreonine By similarity
	Modified residue	246	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P17325-1 [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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X17163 mRNA. Translation: CAA35041.1. X17215 Genomic DNA. Translation: CAA35084.1. BC078738 mRNA. Translation: AAH78738.1.
IPI	IPI00215370.
PIR	S12742.
RefSeq	NP_068607.1.
UniGene	Rn.93714
3D structure databases
HSSP	HSSP built from PDB template 1FOS based on UniProtKB P05412.
SMR	P17325. Positions 256-317.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:653N.
STRING	P17325.
PTM databases
PhosphoSite	P17325.
Proteomic databases
PRIDE	P17325.
Genome annotation databases
Ensembl	ENSRNOT00000011731; ENSRNOP00000011732; ENSRNOG00000026293; Rattus norvegicus. [Genome view]
GeneID	24516.
KEGG	rno:24516.
UCSC	NM_021835. rat.
Organism-specific databases
CTD	24516.
RGD	2943. Jun.
Phylogenomic databases
HOVERGEN	P17325.
OMA	KPHLRNK.
Gene expression databases
ArrayExpress	P17325.
Genevestigator	P17325.
GermOnline	ENSRNOG00000026293. Rattus norvegicus.
Family and domain databases
InterPro	IPR011616. bZIP_1. IPR015558. C_Jun. IPR005643. JNK. IPR002112. Leuzip_Jun. IPR004827. TF_bZIP. [Graphical view]
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]
PROSITE	PS50217. BZIP. 1 hit. PS00036. BZIP_BASIC. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
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:	November 3, 2009
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)