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P05412

- JUN_HUMAN

UniProt

P05412 - JUN_HUMAN

Protein

Transcription factor AP-1

Gene

JUN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 192 (01 Oct 2014)
      Sequence version 2 (01 Oct 1989)
      Previous versions | rss
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    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
    Sitei272 – 2721Necessary for syngernistic transcriptional activity with SMAD3

    GO - Molecular functioni

    1. cAMP response element binding Source: BHF-UCL
    2. DNA binding Source: ProtInc
    3. double-stranded DNA binding Source: Ensembl
    4. enzyme binding Source: UniProt
    5. poly(A) RNA binding Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. Rho GTPase activator activity Source: UniProtKB
    8. RNA polymerase II activating transcription factor binding Source: BHF-UCL
    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: BHF-UCL
    11. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: UniProtKB
    12. RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription Source: BHF-UCL
    13. R-SMAD binding Source: BHF-UCL
    14. sequence-specific DNA binding Source: InterPro
    15. sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    16. transcription coactivator activity Source: UniProtKB
    17. transcription factor binding Source: BHF-UCL
    18. transcription regulatory region DNA binding Source: UniProtKB

    GO - Biological processi

    1. aging Source: Ensembl
    2. angiogenesis Source: Ensembl
    3. axon regeneration Source: Ensembl
    4. cellular response to calcium ion Source: Ensembl
    5. cellular response to potassium ion starvation Source: Ensembl
    6. circadian rhythm Source: Ensembl
    7. Fc-epsilon receptor signaling pathway Source: Reactome
    8. innate immune response Source: Reactome
    9. leading edge cell differentiation Source: Ensembl
    10. learning Source: Ensembl
    11. liver development Source: Ensembl
    12. membrane depolarization Source: Ensembl
    13. microglial cell activation Source: Ensembl
    14. monocyte differentiation Source: Ensembl
    15. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    16. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    17. negative regulation by host of viral transcription Source: UniProtKB
    18. negative regulation of cell proliferation Source: Ensembl
    19. negative regulation of DNA binding Source: UniProtKB
    20. negative regulation of neuron apoptotic process Source: Ensembl
    21. negative regulation of protein autophosphorylation Source: Ensembl
    22. negative regulation of transcription, DNA-templated Source: UniProtKB
    23. outflow tract morphogenesis Source: Ensembl
    24. positive regulation by host of viral transcription Source: UniProtKB
    25. positive regulation of DNA replication Source: Ensembl
    26. positive regulation of endothelial cell proliferation Source: Ensembl
    27. positive regulation of fibroblast proliferation Source: Ensembl
    28. positive regulation of monocyte differentiation Source: Ensembl
    29. positive regulation of neuron apoptotic process Source: Ensembl
    30. positive regulation of Rho GTPase activity Source: GOC
    31. positive regulation of smooth muscle cell proliferation Source: Ensembl
    32. positive regulation of transcription, DNA-templated Source: UniProtKB
    33. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    34. regulation of cell cycle Source: Ensembl
    35. regulation of sequence-specific DNA binding transcription factor activity Source: Reactome
    36. release of cytochrome c from mitochondria Source: Ensembl
    37. response to cAMP Source: Ensembl
    38. response to cytokine Source: Ensembl
    39. response to drug Source: Ensembl
    40. response to hydrogen peroxide Source: Ensembl
    41. response to lipopolysaccharide Source: Ensembl
    42. response to mechanical stimulus Source: Ensembl
    43. response to radiation Source: Ensembl
    44. SMAD protein import into nucleus Source: BHF-UCL
    45. SMAD protein signal transduction Source: BHF-UCL
    46. stress-activated MAPK cascade Source: Reactome
    47. toll-like receptor 10 signaling pathway Source: Reactome
    48. toll-like receptor 2 signaling pathway Source: Reactome
    49. toll-like receptor 3 signaling pathway Source: Reactome
    50. toll-like receptor 4 signaling pathway Source: Reactome
    51. toll-like receptor 5 signaling pathway Source: Reactome
    52. toll-like receptor 9 signaling pathway Source: Reactome
    53. toll-like receptor signaling pathway Source: Reactome
    54. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    55. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    56. transforming growth factor beta receptor signaling pathway Source: BHF-UCL
    57. TRIF-dependent toll-like receptor signaling pathway Source: Reactome

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_118568. Pre-NOTCH Transcription and Translation.
    REACT_163701. FCERI mediated MAPK activation.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_21326. Activation of the AP-1 family of transcription factors.
    SignaLinkiP05412.

    Names & Taxonomyi

    Protein namesi
    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
    p39
    Gene namesi
    Name:JUN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:6204. JUN.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. nuclear chromosome Source: ProtInc
    3. nuclear euchromatin Source: BHF-UCL
    4. nucleoplasm Source: Reactome
    5. nucleus Source: InterPro
    6. transcriptional repressor complex Source: Ensembl
    7. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 21T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-8; A-89; A-93; and A-286. 1 Publication
    Mutagenesisi8 – 81T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-89; A-93; and A-286. 1 Publication
    Mutagenesisi63 – 631S → A: Greatly reduced ATF7-mediated transcriptional activity; when associated with A-73. 1 Publication
    Mutagenesisi73 – 731S → A: Greatly reduced ATF7-mediated transcriptional activity; when associated with A-63. 1 Publication
    Mutagenesisi89 – 891T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-8; A-93; and A-286. 1 Publication
    Mutagenesisi93 – 931T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-8; A-89; and A-286. 1 Publication
    Mutagenesisi243 – 2431S → A: Abolishes phosphorylation by DYRK2. Abolishes phosphorylation by GSK3B at Thr-239. 1 Publication
    Mutagenesisi272 – 2721R → V: Abolishes the syngernistic activity with SMAD3 to activate TGF-beta-mediated transcription. 1 Publication
    Mutagenesisi286 – 2861T → A: Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-8; A-89; and A-93. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA30006.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 331331Transcription factor AP-1PRO_0000076429Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21Phosphothreonine; by PAK21 Publication
    Modified residuei8 – 81Phosphothreonine; by PAK21 Publication
    Modified residuei56 – 561N6-acetyllysineBy similarity
    Modified residuei58 – 581Phosphoserine2 Publications
    Modified residuei63 – 631Phosphoserine; by MAPK8 and PLK36 Publications
    Modified residuei73 – 731Phosphoserine; by MAPK8 and PLK32 Publications
    Modified residuei89 – 891Phosphothreonine; by PAK21 Publication
    Modified residuei93 – 931Phosphothreonine; by PAK21 Publication
    Modified residuei239 – 2391Phosphothreonine; by GSK3-beta2 Publications
    Modified residuei243 – 2431Phosphoserine; by DYRK2 and GSK3-beta4 Publications
    Modified residuei249 – 2491Phosphoserine; by GSK3-beta2 Publications
    Modified residuei271 – 2711N6-acetyllysine1 Publication
    Modified residuei286 – 2861Phosphothreonine; by PAK21 Publication

    Post-translational modificationi

    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.12 Publications
    Acetylated at Lys-271 by EP300.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP05412.
    PaxDbiP05412.
    PRIDEiP05412.

    PTM databases

    PhosphoSiteiP05412.

    Expressioni

    Gene expression databases

    BgeeiP05412.
    CleanExiHS_JUN.
    GenevestigatoriP05412.

    Organism-specific databases

    HPAiCAB003801.
    CAB007780.

    Interactioni

    Subunit structurei

    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.By similarity11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    APLP2Q064813EBI-852823,EBI-79306
    APPP050672EBI-852823,EBI-77613
    ATF2P153365EBI-852823,EBI-1170906
    ATF4P188482EBI-852823,EBI-492498
    BBS7Q8IWZ63EBI-852823,EBI-1806001
    CITED1Q999662EBI-852823,EBI-2624951
    CREB3O438894EBI-852823,EBI-625002
    ETS1P149213EBI-852823,EBI-913209
    FOSP0110021EBI-852823,EBI-852851
    HSP90AA1P079002EBI-852823,EBI-296047
    jnk-1Q8WQG93EBI-852823,EBI-321822From a different organism.
    KPNA2P522922EBI-852823,EBI-349938
    MAPK10P537792EBI-852823,EBI-713543
    MAPK8P459834EBI-852823,EBI-286483
    MAPK8P45983-12EBI-852823,EBI-288687
    MAPRE3Q9UPY83EBI-852823,EBI-726739
    MDM2Q009873EBI-852823,EBI-389668
    PRRC2AP486342EBI-852823,EBI-347545
    STRN4Q9NRL33EBI-852823,EBI-717245
    VRK1Q999864EBI-852823,EBI-1769146

    Protein-protein interaction databases

    BioGridi109928. 180 interactions.
    DIPiDIP-5961N.
    IntActiP05412. 64 interactions.
    MINTiMINT-105756.
    STRINGi9606.ENSP00000360266.

    Structurei

    Secondary structure

    1
    331
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi255 – 30652

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A02X-ray2.70J253-308[»]
    1FOSX-ray3.05F/H254-315[»]
    1JNMX-ray2.20A/B254-315[»]
    1JUNNMR-A/B276-314[»]
    1S9KX-ray3.10E257-308[»]
    1T2KX-ray3.00C254-314[»]
    ProteinModelPortaliP05412.
    SMRiP05412. Positions 257-308.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05412.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini252 – 31564bZIPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni252 – 27928Basic motifPROSITE-ProRule annotationAdd
    BLAST
    Regioni280 – 30829Leucine-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.
    InParanoidiP05412.
    KOiK04448.
    OMAiAELHNQN.
    OrthoDBiEOG75MVXV.
    PhylomeDBiP05412.
    TreeFamiTF323952.

    Family and domain databases

    Gene3Di1.10.880.10. 1 hit.
    InterProiIPR004827. bZIP.
    IPR005643. JNK.
    IPR002112. Leuzip_Jun.
    IPR008917. TF_DNA-bd.
    [Graphical view]
    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.

    P05412-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTAKMETTFY DDALNASFLP SESGPYGYSN PKILKQSMTL NLADPVGSLK    50
    PHLRAKNSDL LTSPDVGLLK LASPELERLI IQSSNGHITT TPTPTQFLCP 100
    KNVTDEQEGF AEGFVRALAE LHSQNTLPSV TSAAQPVNGA GMVAPAVASV 150
    AGGSGSGGFS ASLHSEPPVY ANLSNFNPGA LSSGGGAPSY GAAGLAFPAQ 200
    PQQQQQPPHH LPQQMPVQHP RLQALKEEPQ TVPEMPGETP PLSPIDMESQ 250
    ERIKAERKRM RNRIAASKCR KRKLERIARL EEKVKTLKAQ NSELASTANM 300
    LREQVAQLKQ KVMNHVNSGC QLMLTQQLQT F 331
    Length:331
    Mass (Da):35,676
    Last modified:October 1, 1989 - v2
    Checksum:i0695E23AC4D33561
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 111D → G AA sequence (PubMed:2825349)Curated
    Sequence conflicti14 – 141L → F AA sequence (PubMed:2825349)Curated
    Sequence conflicti80 – 801I → V AA sequence (PubMed:2825349)Curated
    Sequence conflicti151 – 1511A → S in CAG46525. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti297 – 2971T → M.
    Corresponds to variant rs9989 [ dbSNP | Ensembl ].
    VAR_012070

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04111 Genomic DNA. Translation: AAA59197.1.
    CR541724 mRNA. Translation: CAG46525.1.
    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.
    CCDSiCCDS610.1.
    PIRiA31264. TVHUJN.
    RefSeqiNP_002219.1. NM_002228.3.
    UniGeneiHs.696684.

    Genome annotation databases

    EnsembliENST00000371222; ENSP00000360266; ENSG00000177606.
    GeneIDi3725.
    KEGGihsa:3725.
    UCSCiuc001cze.3. human.

    Polymorphism databases

    DMDMi135298.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04111 Genomic DNA. Translation: AAA59197.1 .
    CR541724 mRNA. Translation: CAG46525.1 .
    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 .
    CCDSi CCDS610.1.
    PIRi A31264. TVHUJN.
    RefSeqi NP_002219.1. NM_002228.3.
    UniGenei Hs.696684.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A02 X-ray 2.70 J 253-308 [» ]
    1FOS X-ray 3.05 F/H 254-315 [» ]
    1JNM X-ray 2.20 A/B 254-315 [» ]
    1JUN NMR - A/B 276-314 [» ]
    1S9K X-ray 3.10 E 257-308 [» ]
    1T2K X-ray 3.00 C 254-314 [» ]
    ProteinModelPortali P05412.
    SMRi P05412. Positions 257-308.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109928. 180 interactions.
    DIPi DIP-5961N.
    IntActi P05412. 64 interactions.
    MINTi MINT-105756.
    STRINGi 9606.ENSP00000360266.

    Chemistry

    BindingDBi P05412.
    ChEMBLi CHEMBL4977.
    DrugBanki DB01169. Arsenic trioxide.
    DB01029. Irbesartan.
    DB00852. Pseudoephedrine.
    DB00570. Vinblastine.

    PTM databases

    PhosphoSitei P05412.

    Polymorphism databases

    DMDMi 135298.

    Proteomic databases

    MaxQBi P05412.
    PaxDbi P05412.
    PRIDEi P05412.

    Protocols and materials databases

    DNASUi 3725.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371222 ; ENSP00000360266 ; ENSG00000177606 .
    GeneIDi 3725.
    KEGGi hsa:3725.
    UCSCi uc001cze.3. human.

    Organism-specific databases

    CTDi 3725.
    GeneCardsi GC01M059246.
    H-InvDB HIX0000635.
    HGNCi HGNC:6204. JUN.
    HPAi CAB003801.
    CAB007780.
    MIMi 165160. gene.
    neXtProti NX_P05412.
    PharmGKBi PA30006.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG283376.
    HOGENOMi HOG000006648.
    HOVERGENi HBG001722.
    InParanoidi P05412.
    KOi K04448.
    OMAi AELHNQN.
    OrthoDBi EOG75MVXV.
    PhylomeDBi P05412.
    TreeFami TF323952.

    Enzyme and pathway databases

    Reactomei REACT_118568. Pre-NOTCH Transcription and Translation.
    REACT_163701. FCERI mediated MAPK activation.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_21326. Activation of the AP-1 family of transcription factors.
    SignaLinki P05412.

    Miscellaneous databases

    ChiTaRSi Jun. human.
    EvolutionaryTracei P05412.
    GeneWikii C-jun.
    GenomeRNAii 3725.
    NextBioi 14583.
    PROi P05412.
    SOURCEi Search...

    Gene expression databases

    Bgeei P05412.
    CleanExi HS_JUN.
    Genevestigatori P05412.

    Family and domain databases

    Gene3Di 1.10.880.10. 1 hit.
    InterProi IPR004827. bZIP.
    IPR005643. JNK.
    IPR002112. Leuzip_Jun.
    IPR008917. TF_DNA-bd.
    [Graphical view ]
    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

    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 open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "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].
    5. NIEHS SNPs program
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "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.
      , 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].
    7. "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.
    8. "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.
    9. "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.
    10. "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.
    11. "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.
    12. "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.
    13. "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.
    14. "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.
    15. Cited for: INTERACTION WITH ATF7, MUTAGENESIS OF SER-63 AND SER-73.
    16. "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.
    17. "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.
    18. "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.
    19. "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.
    20. "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.
    21. "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.
    22. "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.
    23. "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.
    24. 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.
    25. "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].
    26. "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.
    27. "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.
    28. "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.
    29. "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.
    30. "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].
    31. "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.
    32. "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.
    33. "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.
    34. "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.

    Entry informationi

    Entry nameiJUN_HUMAN
    AccessioniPrimary (citable) accession number: P05412
    Secondary accession number(s): Q6FHM7, Q96G93
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 192 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3