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P05412 (JUN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 187. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
p39
Gene names
Name:JUN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length331 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Ref.15 Ref.19

Subunit structure

Heterodimer with either FOS or BATF3 or ATF7. The ATF7/JUN heterodimer is essential for ATF7 transactivation activity. Interacts with DSIPI; the interaction inhibits the binding of active AP1 to its target DNA By similarity. Interacts with HIVEP3 and MYBBP1A By similarity. 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. 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. Interacts with methylated RNF187. Binds to HIPK3. Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.20 Ref.26 Ref.31

Subcellular location

Nucleus.

Post-translational modification

Phosphorylated by CaMK4 and PRKDC; phosphorylation enhances the transcriptional activity. Phosphorylated by HIPK3. Phosphorylated by DYRK2 at Ser-243; this primes the protein for subsequent phosphorylation by GSK3B at Thr-239. Phosphorylated at Thr-239, Ser-243 and Ser-249 by GSK3B; phosphorylation reduces its ability to bind DNA. Phosphorylated by PAK2 at Thr-2, Thr-8, Thr-89, Thr-93 and Thr-286 thereby promoting JUN-mediated cell proliferation and transformation. Phosphorylated by PLK3 following hypoxia or UV irradiation, leading to increase DNA-binding activity. Ref.7 Ref.8 Ref.9 Ref.19 Ref.21 Ref.22 Ref.28 Ref.30

Acetylated at Lys-271 by EP300. Ref.16

Sequence similarities

Belongs to the bZIP family. Jun subfamily.

Contains 1 bZIP (basic-leucine zipper) domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DiseaseProto-oncogene
   LigandDNA-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

MyD88-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

MyD88-independent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

SMAD protein import into nucleus

Inferred from direct assay Ref.12. Source: BHF-UCL

SMAD protein signal transduction

Inferred from direct assay Ref.12. Source: BHF-UCL

TRIF-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

aging

Inferred from electronic annotation. Source: Ensembl

angiogenesis

Inferred from electronic annotation. Source: Ensembl

axon regeneration

Inferred from electronic annotation. Source: Ensembl

cellular response to calcium ion

Inferred from electronic annotation. Source: Ensembl

cellular response to potassium ion starvation

Inferred from electronic annotation. Source: Ensembl

circadian rhythm

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

leading edge cell differentiation

Inferred from electronic annotation. Source: Ensembl

learning

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from electronic annotation. Source: Ensembl

membrane depolarization

Inferred from electronic annotation. Source: Ensembl

microglial cell activation

Inferred from electronic annotation. Source: Ensembl

monocyte differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation by host of viral transcription

Inferred from direct assay PubMed 2833704. Source: UniProtKB

negative regulation of DNA binding

Inferred from direct assay PubMed 14645924. Source: UniProtKB

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 2833704. Source: UniProtKB

outflow tract morphogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation by host of viral transcription

Inferred from direct assay PubMed 2833704. Source: UniProtKB

positive regulation of DNA replication

Inferred from electronic annotation. Source: Ensembl

positive regulation of Rho GTPase activity

Inferred from direct assay PubMed 11804590. Source: GOC

positive regulation of endothelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of fibroblast proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of monocyte differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 2833704. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 2833704. Source: UniProtKB

regulation of cell cycle

Inferred from electronic annotation. Source: Ensembl

regulation of sequence-specific DNA binding transcription factor activity

Traceable author statement. Source: Reactome

release of cytochrome c from mitochondria

Inferred from electronic annotation. Source: Ensembl

response to cAMP

Inferred from electronic annotation. Source: Ensembl

response to cytokine

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

response to radiation

Inferred from electronic annotation. Source: Ensembl

stress-activated MAPK cascade

Traceable author statement. Source: Reactome

toll-like receptor 10 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 3 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 5 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 9 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR1:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR6:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

transforming growth factor beta receptor signaling pathway

Inferred from direct assay Ref.12. Source: BHF-UCL

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Ensembl

nuclear chromosome

Traceable author statement PubMed 10918580. Source: ProtInc

nuclear euchromatin

Inferred from direct assay PubMed 19861239. Source: BHF-UCL

nucleoplasm

Traceable author statement. Source: Reactome

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

transcriptional repressor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Traceable author statement Ref.2. Source: ProtInc

R-SMAD binding

Inferred from physical interaction Ref.12. Source: BHF-UCL

RNA polymerase II activating transcription factor binding

Inferred from physical interaction PubMed 19861239. Source: BHF-UCL

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II distal enhancer sequence-specific DNA binding

Inferred from direct assay PubMed 19861239. Source: BHF-UCL

RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 2833704. Source: UniProtKB

RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription

Inferred by curator PubMed 19861239. Source: BHF-UCL

Rho GTPase activator activity

Inferred from direct assay PubMed 11804590. Source: UniProtKB

cAMP response element binding

Inferred from direct assay PubMed 19861239. Source: BHF-UCL

double-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.12. Source: BHF-UCL

transcription coactivator activity

Inferred from direct assay PubMed 2833704. Source: UniProtKB

transcription factor binding

Inferred from physical interaction PubMed 16007074. Source: BHF-UCL

transcription regulatory region DNA binding

Inferred from direct assay PubMed 14645924. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 331331Transcription factor AP-1
PRO_0000076429

Regions

Domain252 – 31564bZIP
Region252 – 27928Basic motif By similarity
Region280 – 30829Leucine-zipper By similarity

Sites

Site2721Necessary for syngernistic transcriptional activity with SMAD3

Amino acid modifications

Modified residue21Phosphothreonine; by PAK2 Ref.28
Modified residue81Phosphothreonine; by PAK2 Ref.28
Modified residue561N6-acetyllysine By similarity
Modified residue581Phosphoserine Ref.23 Ref.29
Modified residue631Phosphoserine; by MAPK8 and PLK3 Ref.21 Ref.22 Ref.23 Ref.25 Ref.27 Ref.29
Modified residue731Phosphoserine; by MAPK8 and PLK3 Ref.21 Ref.22
Modified residue891Phosphothreonine; by PAK2 Ref.28
Modified residue931Phosphothreonine; by PAK2 Ref.28
Modified residue2391Phosphothreonine; by GSK3-beta Ref.7 Ref.23
Modified residue2431Phosphoserine; by DYRK2 and GSK3-beta Ref.7 Ref.23 Ref.25 Ref.30
Modified residue2491Phosphoserine; by GSK3-beta Ref.7 Ref.8
Modified residue2711N6-acetyllysine Ref.16
Modified residue2861Phosphothreonine; by PAK2 Ref.28

Natural variations

Natural variant2971T → M.
Corresponds to variant rs9989 [ dbSNP | Ensembl ].
VAR_012070

Experimental info

Mutagenesis21T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-8; A-89; A-93; and A-286. Ref.28
Mutagenesis81T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-89; A-93; and A-286. Ref.28
Mutagenesis631S → A: Greatly reduced ATF7-mediated transcriptional activity; when associated with A-73. Ref.14
Mutagenesis731S → A: Greatly reduced ATF7-mediated transcriptional activity; when associated with A-63. Ref.14
Mutagenesis891T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-8; A-93; and A-286. Ref.28
Mutagenesis931T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-8; A-89; and A-286. Ref.28
Mutagenesis2431S → A: Abolishes phosphorylation by DYRK2. Abolishes phosphorylation by GSK3B at Thr-239. Ref.30
Mutagenesis2721R → V: Abolishes the syngernistic activity with SMAD3 to activate TGF-beta-mediated transcription. Ref.15
Mutagenesis2861T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-8; A-89; and A-93. Ref.28
Sequence conflict111D → G AA sequence Ref.2
Sequence conflict141L → F AA sequence Ref.2
Sequence conflict801I → V AA sequence Ref.2

Secondary structure

... 331
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05412 [UniParc].

Last modified October 1, 1989. Version 2.
Checksum: 0695E23AC4D33561

FASTA33135,676
        10         20         30         40         50         60 
MTAKMETTFY DDALNASFLP SESGPYGYSN PKILKQSMTL NLADPVGSLK PHLRAKNSDL 

        70         80         90        100        110        120 
LTSPDVGLLK LASPELERLI IQSSNGHITT TPTPTQFLCP KNVTDEQEGF AEGFVRALAE 

       130        140        150        160        170        180 
LHSQNTLPSV TSAAQPVNGA GMVAPAVASV AGGSGSGGFS ASLHSEPPVY ANLSNFNPGA 

       190        200        210        220        230        240 
LSSGGGAPSY GAAGLAFPAQ PQQQQQPPHH LPQQMPVQHP RLQALKEEPQ TVPEMPGETP 

       250        260        270        280        290        300 
PLSPIDMESQ ERIKAERKRM RNRIAASKCR KRKLERIARL EEKVKTLKAQ NSELASTANM 

       310        320        330 
LREQVAQLKQ KVMNHVNSGC QLMLTQQLQT F 

« Hide

References

« Hide 'large scale' references
[1]"Structure and chromosomal localization of the functional intronless human JUN protooncogene."
Hattori K., Angel P., le Beau M.M., Karin M.
Proc. Natl. Acad. Sci. U.S.A. 85:9148-9152(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Human proto-oncogene c-jun encodes a DNA binding protein with structural and functional properties of transcription factor AP-1."
Bohmann D., Bos T.J., Admon A., Nishimura T., Vogt P.K., Tjian R.
Science 238:1386-1392(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]NIEHS SNPs program
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: B-cell, Ovary, Testis and Uterus.
[7]"Activation of protein kinase C decreases phosphorylation of c-Jun at sites that negatively regulate its DNA-binding activity."
Boyle W.J., Smeal T., Defize L.H., Angel P., Woodgett J.R., Karin M., Hunter T.
Cell 64:573-584(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-239; SER-243 AND SER-249 BY GSK3B.
[8]"c-Jun is phosphorylated by the DNA-dependent protein kinase in vitro; definition of the minimal kinase recognition motif."
Bannister A.J., Gottlieb T.M., Kouzarides T., Jackson S.P.
Nucleic Acids Res. 21:1289-1295(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-249.
[9]"Regulation of mitogen-activated protein kinases by a calcium/calmodulin-dependent protein kinase cascade."
Enslen H., Tokumitsu H., Stork P.J., Davis R.J., Soderling T.R.
Proc. Natl. Acad. Sci. U.S.A. 93:10803-10808(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY CAMK4.
[10]"Cross-talk between different enhancer elements during mitogenic induction of the human stromelysin-1 gene."
Kirstein M., Sanz L., Moscat J., Diaz-Meco M.T., Saus J.
J. Biol. Chem. 271:18231-18236(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TCF20.
[11]"A new group of conserved coactivators that increase the specificity of AP-1 transcription factors."
Claret F.-X., Hibi M., Dhut S., Toda T., Karin M.
Nature 383:453-457(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH COPS5.
[12]"Smad3 and Smad4 cooperate with c-Jun/c-Fos to mediate TGF-beta-induced transcription."
Zhang Y., Feng X.H., Derynck R.
Nature 394:909-913(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A COMPONENT OF THE SMAD3/SMAD4/JUN/FOS COMPLEX, INTERACTION WITH SMAD3.
[13]"SPI-B activates transcription via a unique proline, serine, and threonine domain and exhibits DNA binding affinity differences from PU.1."
Rao S., Matsumura A., Yoon J., Simon M.C.
J. Biol. Chem. 274:11115-11124(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPIB.
[14]"Role of the ATFa/JNK2 complex in Jun activation."
De Graeve F., Bahr A., Sabapathy K.T., Hauss C., Wagner E.F., Kedinger C., Chatton B.
Oncogene 18:3491-3500(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATF7, MUTAGENESIS OF SER-63 AND SER-73.
[15]"Structural and functional characterization of the transforming growth factor-beta -induced Smad3/c-Jun transcriptional cooperativity."
Qing J., Zhang Y., Derynck R.
J. Biol. Chem. 275:38802-38812(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SMAD3 IN THE SMAD3/SMAD4/JUN/FOS COMPLEX, DNA-BINDING, FUNCTION, MUTAGENESIS OF ARG-272.
[16]"A specific lysine in c-Jun is required for transcriptional repression by E1A and is acetylated by p300."
Vries R.G., Prudenziati M., Zwartjes C., Verlaan M., Kalkhoven E., Zantema A.
EMBO J. 20:6095-6103(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-271 BY EP300.
[17]"Correlation of transcriptional repression by p21(SNFT) with changes in DNA.NF-AT complex interactions."
Bower K.E., Zeller R.W., Wachsman W., Martinez T., McGuire K.L.
J. Biol. Chem. 277:34967-34977(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BATF3.
[18]"Transcriptional repression of MMP-1 by p21SNFT and reduced in vitro invasiveness of hepatocarcinoma cells."
Bower K.E., Fritz J.M., McGuire K.L.
Oncogene 23:8805-8814(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BATF3.
[19]"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.
[20]"Sp1 deacetylation induced by phorbol ester recruits p300 to activate 12(S)-lipoxygenase gene transcription."
Hung J.J., Wang Y.T., Chang W.C.
Mol. Cell. Biol. 26:1770-1785(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SP1.
[21]"Stress-induced c-Jun activation mediated by Polo-like kinase 3 in corneal epithelial cells."
Wang L., Dai W., Lu L.
J. Biol. Chem. 282:32121-32127(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-63 AND SER-73.
[22]"Activation of Polo-like kinase 3 by hypoxic stresses."
Wang L., Gao J., Dai W., Lu L.
J. Biol. Chem. 283:25928-25935(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-63 AND SER-73.
[23]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-63; THR-239 AND SER-243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63 AND SER-243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[26]"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.
[27]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[28]"P21-activated protein kinase (PAK2)-mediated c-Jun phosphorylation at 5 threonine sites promotes cell transformation."
Li T., Zhang J., Zhu F., Wen W., Zykova T., Li X., Liu K., Peng C., Ma W., Shi G., Dong Z., Bode A.M., Dong Z.
Carcinogenesis 32:659-666(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-2; THR-8; THR-89; THR-93 AND THR-286, MUTAGENESIS OF THR-2; THR-8; THR-89; THR-93 AND THR-286.
[29]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND SER-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"DYRK2 priming phosphorylation of c-Jun and c-Myc modulates cell cycle progression in human cancer cells."
Taira N., Mimoto R., Kurata M., Yamaguchi T., Kitagawa M., Miki Y., Yoshida K.
J. Clin. Invest. 122:859-872(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-243, MUTAGENESIS OF SER-243.
[31]"Arginine methylation of the c-Jun coactivator RACO-1 is required for c-Jun/AP-1 activation."
Davies C.C., Chakraborty A., Diefenbacher M.E., Skehel M., Behrens A.
EMBO J. 32:1556-1567(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNF187.
[32]"Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA."
Glover J.N., Harrison S.C.
Nature 373:257-261(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 257-313 OF COMPLEX WITH FOS.
[33]"High resolution NMR solution structure of the leucine zipper domain of the c-Jun homodimer."
Junius F.K., O'Donoghue S.I., Nilges M., Weiss A.S., King G.F.
J. Biol. Chem. 271:13663-13667(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 276-314.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04111 Genomic DNA. Translation: AAA59197.1.
BT019759 mRNA. Translation: AAV38564.1.
AY217548 Genomic DNA. Translation: AAO22993.1.
AL136985 Genomic DNA. Translation: CAC10201.1.
BC002646 mRNA. No translation available.
BC006175 mRNA. Translation: AAH06175.1.
BC009874 mRNA. Translation: AAH09874.2.
BC068522 mRNA. Translation: AAH68522.1.
PIRTVHUJN. A31264.
RefSeqNP_002219.1. NM_002228.3.
UniGeneHs.696684.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A02X-ray2.70J254-308[»]
1FOSX-ray3.05F/H254-315[»]
1JNMX-ray2.20A/B254-315[»]
1JUNNMR-A/B276-314[»]
1S9KX-ray3.10E257-308[»]
1T2KX-ray3.00C254-314[»]
ProteinModelPortalP05412.
SMRP05412. Positions 257-308.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109928. 179 interactions.
DIPDIP-5961N.
IntActP05412. 62 interactions.
MINTMINT-105756.
STRING9606.ENSP00000360266.

Chemistry

BindingDBP05412.
ChEMBLCHEMBL2111421.
DrugBankDB01169. Arsenic trioxide.
DB01029. Irbesartan.
DB00570. Vinblastine.

PTM databases

PhosphoSiteP05412.

Polymorphism databases

DMDM135298.

Proteomic databases

PaxDbP05412.
PRIDEP05412.

Protocols and materials databases

DNASU3725.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371222; ENSP00000360266; ENSG00000177606.
GeneID3725.
KEGGhsa:3725.
UCSCuc001cze.3. human.

Organism-specific databases

CTD3725.
GeneCardsGC01M059246.
H-InvDBHIX0000635.
HGNCHGNC:6204. JUN.
HPACAB003801.
CAB007780.
MIM165160. gene.
neXtProtNX_P05412.
PharmGKBPA30006.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG283376.
HOGENOMHOG000006648.
HOVERGENHBG001722.
InParanoidP05412.
KOK04448.
OMAKPHLRNK.
OrthoDBEOG75MVXV.
PhylomeDBP05412.
TreeFamTF323952.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.
SignaLinkP05412.

Gene expression databases

BgeeP05412.
CleanExHS_JUN.
GenevestigatorP05412.

Family and domain databases

Gene3D1.10.880.10. 1 hit.
InterProIPR004827. bZIP.
IPR015558. C_Jun.
IPR005643. JNK.
IPR002112. Leuzip_Jun.
IPR008917. TF_DNA-bd.
[Graphical view]
PANTHERPTHR11462:SF8. PTHR11462:SF8. 1 hit.
PfamPF00170. bZIP_1. 1 hit.
PF03957. Jun. 1 hit.
[Graphical view]
PRINTSPR00043. LEUZIPPRJUN.
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
SUPFAMSSF47454. SSF47454. 1 hit.
PROSITEPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSJun. human.
EvolutionaryTraceP05412.
GeneWikiC-jun.
GenomeRNAi3725.
NextBio14583.
PROP05412.
SOURCESearch...

Entry information

Entry nameJUN_HUMAN
AccessionPrimary (citable) accession number: P05412
Secondary accession number(s): Q96G93
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 1, 1989
Last modified: April 16, 2014
This is version 187 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM