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Protein

Transcription factor AP-1

Gene

Jun

Organism
Mus musculus (Mouse)
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.2 Publications

Sites

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

GO - Molecular functioni

  1. cAMP response element binding Source: MGI
  2. chromatin binding Source: MGI
  3. DNA binding Source: MGI
  4. double-stranded DNA binding Source: Ensembl
  5. enzyme binding Source: MGI
  6. poly(A) RNA binding Source: MGI
  7. Rho GTPase activator activity Source: MGI
  8. RNA polymerase II activating transcription factor binding Source: MGI
  9. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
  10. RNA polymerase II distal enhancer sequence-specific DNA binding Source: MGI
  11. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: MGI
  12. R-SMAD binding Source: MGI
  13. sequence-specific DNA binding transcription factor activity Source: MGI
  14. transcription coactivator activity Source: MGI
  15. transcription factor binding Source: MGI
  16. transcription regulatory region DNA binding Source: MGI

GO - Biological processi

  1. aging Source: Ensembl
  2. angiogenesis Source: MGI
  3. axon regeneration Source: MGI
  4. cellular process Source: MGI
  5. cellular response to calcium ion Source: MGI
  6. cellular response to potassium ion starvation Source: Ensembl
  7. circadian rhythm Source: Ensembl
  8. leading edge cell differentiation Source: MGI
  9. learning Source: Ensembl
  10. liver development Source: MGI
  11. membrane depolarization Source: Ensembl
  12. microglial cell activation Source: MGI
  13. monocyte differentiation Source: MGI
  14. negative regulation by host of viral transcription Source: MGI
  15. negative regulation of apoptotic process Source: MGI
  16. negative regulation of cell proliferation Source: MGI
  17. negative regulation of DNA binding Source: MGI
  18. negative regulation of neuron apoptotic process Source: MGI
  19. negative regulation of protein autophosphorylation Source: MGI
  20. negative regulation of transcription, DNA-templated Source: MGI
  21. negative regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress Source: MGI
  22. outflow tract morphogenesis Source: MGI
  23. positive regulation by host of viral transcription Source: MGI
  24. positive regulation of DNA replication Source: Ensembl
  25. positive regulation of endothelial cell proliferation Source: MGI
  26. positive regulation of fibroblast proliferation Source: MGI
  27. positive regulation of monocyte differentiation Source: Ensembl
  28. positive regulation of neuron apoptotic process Source: Ensembl
  29. positive regulation of Rho GTPase activity Source: MGI
  30. positive regulation of smooth muscle cell proliferation Source: Ensembl
  31. positive regulation of transcription, DNA-templated Source: MGI
  32. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  33. regulation of cell cycle Source: MGI
  34. regulation of transcription, DNA-templated Source: MGI
  35. release of cytochrome c from mitochondria Source: Ensembl
  36. response to cAMP Source: Ensembl
  37. response to cytokine Source: Ensembl
  38. response to drug Source: MGI
  39. response to hydrogen peroxide Source: Ensembl
  40. response to lipopolysaccharide Source: Ensembl
  41. response to muscle stretch Source: MGI
  42. response to radiation Source: Ensembl
  43. SMAD protein import into nucleus Source: MGI
  44. SMAD protein signal transduction Source: MGI
  45. transforming growth factor beta receptor signaling pathway Source: MGI
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_305463. Oxidative Stress Induced Senescence.
REACT_314186. FCERI mediated MAPK activation.
REACT_320943. Activation of the AP-1 family of transcription factors.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor AP-1
Alternative name(s):
AH119
Activator protein 1
Short name:
AP1
Proto-oncogene c-Jun
V-jun avian sarcoma virus 17 oncogene homolog
Short name:
Jun A
Gene namesi
Name:Jun
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:96646. Jun.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. nuclear euchromatin Source: MGI
  3. nucleoplasm Source: MGI
  4. nucleus Source: MGI
  5. transcriptional repressor complex Source: MGI
  6. transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 334334Transcription factor AP-1PRO_0000076430Add
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-acetyllysine1 Publication
Modified residuei58 – 581PhosphoserineBy similarity
Modified residuei63 – 631Phosphoserine1 Publication
Modified residuei73 – 731Phosphoserine; by MAPK8 and PLK31 Publication
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 PAK2 at Thr-2, Thr-8, Thr-89, Thr-93 and Thr-289 thereby promoting JUN-mediated cell proliferation and transformation. 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

MaxQBiP05627.
PaxDbiP05627.
PRIDEiP05627.

PTM databases

PhosphoSiteiP05627.

Expressioni

Gene expression databases

BgeeiP05627.
CleanExiMM_JUN.
ExpressionAtlasiP05627. baseline and differential.
GenevestigatoriP05627.

Interactioni

Subunit structurei

Heterodimer with either FOS or BATF3 or ATF7 (By similarity). The ATF7/JUN heterodimer is essential for ATF7 transactivation activity. Interacts with SP1, SPIB and TCF20. Interacts with COPS5; the interaction leads indirectly to its phosphorylation. 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 (By similarity). 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). Interacts with DSIPI; the interaction inhibits the binding of active AP1 to its target DNA (PubMed:11397794). Interacts with HIVEP3 and MYBBP1A (PubMed:9447996, PubMed:14707112). Interacts with methylated RNF187 (PubMed:20852630). Binds to HIPK3. Interacts (when phosphorylated) with FBXW7 (By similarity).By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Cdk6Q642612EBI-764369,EBI-847380
ESR1P033726EBI-764369,EBI-78473From a different organism.
Mapk8Q91Y862EBI-764369,EBI-298784

Protein-protein interaction databases

BioGridi200871. 40 interactions.
DIPiDIP-1068N.
IntActiP05627. 5 interactions.
MINTiMINT-209953.

Structurei

3D structure databases

ProteinModelPortaliP05627.
SMRiP05627. 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

eggNOGiNOG283376.
HOGENOMiHOG000006648.
HOVERGENiHBG001722.
InParanoidiP05627.
KOiK04448.
OMAiAELHNQN.
OrthoDBiEOG75MVXV.
PhylomeDBiP05627.
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.

P05627-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAKMETTFY DDALNASFLQ SESGAYGYSN PKILKQSMTL NLADPVGSLK
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 GAAGLAFPSQ
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):35,944
Last modified:October 1, 1989 - v3
Checksum:i2BE0E4025B8B1CA3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti183 – 1831S → C in CAA31252 (PubMed:3136397).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12761 mRNA. Translation: CAA31252.1.
X12740 mRNA. Translation: CAA31236.1.
J04115 mRNA. Translation: AAA37419.1.
BC002081 mRNA. Translation: AAH02081.1.
BC021888 mRNA. Translation: AAH21888.1.
CCDSiCCDS18364.1.
PIRiA31345. TVMSJA.
RefSeqiNP_034721.1. NM_010591.2.
UniGeneiMm.275071.

Genome annotation databases

EnsembliENSMUST00000107094; ENSMUSP00000102711; ENSMUSG00000052684.
GeneIDi16476.
KEGGimmu:16476.
UCSCiuc008tsq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12761 mRNA. Translation: CAA31252.1.
X12740 mRNA. Translation: CAA31236.1.
J04115 mRNA. Translation: AAA37419.1.
BC002081 mRNA. Translation: AAH02081.1.
BC021888 mRNA. Translation: AAH21888.1.
CCDSiCCDS18364.1.
PIRiA31345. TVMSJA.
RefSeqiNP_034721.1. NM_010591.2.
UniGeneiMm.275071.

3D structure databases

ProteinModelPortaliP05627.
SMRiP05627. Positions 260-311.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200871. 40 interactions.
DIPiDIP-1068N.
IntActiP05627. 5 interactions.
MINTiMINT-209953.

Chemistry

ChEMBLiCHEMBL5369.

PTM databases

PhosphoSiteiP05627.

Proteomic databases

MaxQBiP05627.
PaxDbiP05627.
PRIDEiP05627.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000107094; ENSMUSP00000102711; ENSMUSG00000052684.
GeneIDi16476.
KEGGimmu:16476.
UCSCiuc008tsq.2. mouse.

Organism-specific databases

CTDi3725.
MGIiMGI:96646. Jun.

Phylogenomic databases

eggNOGiNOG283376.
HOGENOMiHOG000006648.
HOVERGENiHBG001722.
InParanoidiP05627.
KOiK04448.
OMAiAELHNQN.
OrthoDBiEOG75MVXV.
PhylomeDBiP05627.
TreeFamiTF323952.

Enzyme and pathway databases

ReactomeiREACT_305463. Oxidative Stress Induced Senescence.
REACT_314186. FCERI mediated MAPK activation.
REACT_320943. Activation of the AP-1 family of transcription factors.

Miscellaneous databases

NextBioi289763.
PROiP05627.
SOURCEiSearch...

Gene expression databases

BgeeiP05627.
CleanExiMM_JUN.
ExpressionAtlasiP05627. baseline and differential.
GenevestigatoriP05627.

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. "Transcriptional activation of c-jun during the G0/G1 transition in mouse fibroblasts."
    Ryseck R.-P., Hirai S., Yaniv M., Bravo R.
    Nature 334:535-537(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Induction of proto-oncogene JUN/AP-1 by serum and TPA."
    Lamph W.W., Wamsley P., Sassone-Corsi P., Verma I.M.
    Nature 334:629-631(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Induction of protooncogene c-jun by serum growth factors."
    Ryder K., Nathans D.
    Proc. Natl. Acad. Sci. U.S.A. 85:8464-8467(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary tumor.
  5. "Molecular cloning reveals that the p160 Myb-binding protein is a novel, predominantly nucleolar protein which may play a role in transactivation by Myb."
    Tavner F.J., Simpson R., Tashiro S., Favier D., Jenkins N.A., Gilbert D.J., Copeland N.G., Macmillan E.M., Lutwyche J., Keough R.A., Ishii S., Gonda T.J.
    Mol. Cell. Biol. 18:989-1002(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MYBBP1A.
  6. "Inhibition of AP-1 by the glucocorticoid-inducible protein GILZ."
    Mittelstadt P.R., Ashwell J.D.
    J. Biol. Chem. 276:29603-29610(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DSIPI.
  7. "Schnurri-3 (KRC) interacts with c-Jun to regulate the IL-2 gene in T cells."
    Oukka M., Wein M.N., Glimcher L.H.
    J. Exp. Med. 199:15-24(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIVEP3, FUNCTION.
  8. "Cyclic AMP stimulates SF-1-dependent CYP11A1 expression through homeodomain-interacting protein kinase 3-mediated Jun N-terminal kinase and c-Jun phosphorylation."
    Lan H.-C., Li H.-J., Lin G., Lai P.-Y., Chung B.-C.
    Mol. Cell. Biol. 27:2027-2036(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION BY HIPK3.
  9. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNF187.
  11. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-56, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiJUN_MOUSE
AccessioniPrimary (citable) accession number: P05627
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 1, 1989
Last modified: April 1, 2015
This is version 154 of the entry and version 3 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.