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P05627

- JUN_MOUSE

UniProt

P05627 - JUN_MOUSE

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Protein

Transcription factor AP-1

Gene

Jun

Organism
Mus musculus (Mouse)
Status
Reviewed - 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 syngernistic transcriptional activity with SMAD3By similarity

GO - Molecular functioni

  1. cAMP response element binding Source: Ensembl
  2. DNA binding Source: MGI
  3. double-stranded DNA binding Source: Ensembl
  4. poly(A) RNA binding Source: Ensembl
  5. Rho GTPase activator activity Source: Ensembl
  6. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
  7. RNA polymerase II distal enhancer sequence-specific DNA binding Source: Ensembl
  8. transcription coactivator activity Source: Ensembl
  9. 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: Ensembl
  15. negative regulation of apoptotic process Source: MGI
  16. negative regulation of cell proliferation Source: MGI
  17. negative regulation of DNA binding Source: Ensembl
  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: Ensembl
  21. outflow tract morphogenesis Source: MGI
  22. positive regulation by host of viral transcription Source: Ensembl
  23. positive regulation of DNA replication Source: Ensembl
  24. positive regulation of endothelial cell proliferation Source: MGI
  25. positive regulation of fibroblast proliferation Source: MGI
  26. positive regulation of monocyte differentiation Source: Ensembl
  27. positive regulation of neuron apoptotic process Source: Ensembl
  28. positive regulation of smooth muscle cell proliferation Source: Ensembl
  29. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  30. regulation of cell cycle Source: MGI
  31. regulation of transcription, DNA-templated Source: MGI
  32. release of cytochrome c from mitochondria Source: Ensembl
  33. response to cAMP Source: Ensembl
  34. response to cytokine Source: Ensembl
  35. response to drug Source: MGI
  36. response to hydrogen peroxide Source: Ensembl
  37. response to lipopolysaccharide Source: Ensembl
  38. response to mechanical stimulus Source: Ensembl
  39. response to radiation Source: Ensembl
  40. SMAD protein import into nucleus Source: Ensembl
  41. SMAD protein signal transduction Source: Ensembl
  42. transforming growth factor beta receptor signaling pathway Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_188530. FCERI mediated MAPK activation.
REACT_188970. Oxidative Stress Induced Senescence.
REACT_204811. 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: Chromosome 4

Organism-specific databases

MGIiMGI:96646. Jun.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. nuclear euchromatin Source: Ensembl
  3. nucleus Source: MGI
  4. transcriptional repressor complex Source: MGI
  5. 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 – 631Phosphoserine; alternate1 Publication
Modified residuei63 – 631Phosphoserine; by MAPK8 and PLK3; alternateBy similarity
Modified residuei73 – 731Phosphoserine; by MAPK8 and PLK31 Publication
Modified residuei89 – 891Phosphothreonine; by PAK2By 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
Acetylated at Lys-271 by EP300.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

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 syngernistically 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. Interacts with HIVEP3 and MYBBP1A. Interacts with methylated RNF187. Binds to HIPK3.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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS18364.1.
PIRi A31345. TVMSJA.
RefSeqi NP_034721.1. NM_010591.2.
UniGenei Mm.275071.

3D structure databases

ProteinModelPortali P05627.
SMRi P05627. Positions 260-311.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200871. 40 interactions.
DIPi DIP-1068N.
IntActi P05627. 5 interactions.
MINTi MINT-209953.

Chemistry

ChEMBLi CHEMBL5369.

PTM databases

PhosphoSitei P05627.

Proteomic databases

MaxQBi P05627.
PaxDbi P05627.
PRIDEi P05627.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000107094 ; ENSMUSP00000102711 ; ENSMUSG00000052684 .
GeneIDi 16476.
KEGGi mmu:16476.
UCSCi uc008tsq.2. mouse.

Organism-specific databases

CTDi 3725.
MGIi MGI:96646. Jun.

Phylogenomic databases

eggNOGi NOG283376.
HOGENOMi HOG000006648.
HOVERGENi HBG001722.
InParanoidi P05627.
KOi K04448.
OMAi AELHNQN.
OrthoDBi EOG75MVXV.
PhylomeDBi P05627.
TreeFami TF323952.

Enzyme and pathway databases

Reactomei REACT_188530. FCERI mediated MAPK activation.
REACT_188970. Oxidative Stress Induced Senescence.
REACT_204811. Activation of the AP-1 family of transcription factors.

Miscellaneous databases

NextBioi 289763.
PROi P05627.
SOURCEi Search...

Gene expression databases

Bgeei P05627.
CleanExi MM_JUN.
ExpressionAtlasi P05627. baseline and differential.
Genevestigatori P05627.

Family and domain databases

Gene3Di 1.10.880.10. 1 hit.
InterProi IPR004827. bZIP.
IPR015558. C_Jun/v-Jun.
IPR005643. JNK.
IPR002112. Leuzip_Jun.
IPR008917. TF_DNA-bd.
[Graphical view ]
PANTHERi PTHR11462:SF8. PTHR11462:SF8. 1 hit.
Pfami PF00170. bZIP_1. 1 hit.
PF03957. Jun. 1 hit.
[Graphical view ]
PRINTSi PR00043. LEUZIPPRJUN.
SMARTi SM00338. BRLZ. 1 hit.
[Graphical view ]
SUPFAMi SSF47454. SSF47454. 1 hit.
PROSITEi PS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1988) [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(1988) [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(1988) [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(2004) [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(1998) [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(2001) [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(2004) [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(2007) [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(2009) [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(2010) [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(2013) [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: October 29, 2014
This is version 150 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