Transcription factor AP-1

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• cAMP response element binding Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "cJun modulates Ggamma-globin gene expression via an upstream cAMP response element."
    Kodeboyina S., Balamurugan P., Liu L., Pace B.S.
    Blood Cells Mol Dis 44:7-15(2010) [PubMed] [Europe PMC] [Abstract]
• DNA binding Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • Ref.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.
• DNA-binding transcription activator activity, RNA polymerase II-specific Source: BHF-UCLInferred from direct assayⁱ
  • "cJun modulates Ggamma-globin gene expression via an upstream cAMP response element."
    Kodeboyina S., Balamurugan P., Liu L., Pace B.S.
    Blood Cells Mol Dis 44:7-15(2010) [PubMed] [Europe PMC] [Abstract]
• DNA-binding transcription factor activity Source: BHF-UCLInferred from direct assayⁱ
  • Ref.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.
• DNA-binding transcription factor activity, RNA polymerase II-specific Source: UniProtKBInferred from direct assayⁱ
  • "Enhancer binding factors AP-4 and AP-1 act in concert to activate SV40 late transcription in vitro."
    Mermod N., Williams T.J., Tjian R.
    Nature 332:557-561(1988) [PubMed] [Europe PMC] [Abstract]
• DNA-binding transcription repressor activity, RNA polymerase II-specific Source: ARUK-UCLInferred from direct assayⁱ
  • "Enhancer binding factors AP-4 and AP-1 act in concert to activate SV40 late transcription in vitro."
    Mermod N., Williams T.J., Tjian R.
    Nature 332:557-561(1988) [PubMed] [Europe PMC] [Abstract]
• enzyme binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "A high-confidence interaction map identifies SIRT1 as a mediator of acetylation of USP22 and the SAGA coactivator complex."
    Armour S.M., Bennett E.J., Braun C.R., Zhang X.Y., McMahon S.B., Gygi S.P., Harper J.W., Sinclair D.A.
    Mol Cell Biol 33:1487-1502(2013) [PubMed] [Europe PMC] [Abstract]
• GTPase activator activity Source: UniProtKBInferred from direct assayⁱ
  • "ARAP1: a point of convergence for Arf and Rho signaling."
    Miura K., Jacques K.M., Stauffer S., Kubosaki A., Zhu K., Hirsch D.S., Resau J., Zheng Y., Randazzo P.A.
    Mol. Cell 9:109-119(2002) [PubMed] [Europe PMC] [Abstract]
• HMG box domain binding Source: Ensembl
• identical protein binding Source: IntActInferred from physical interactionⁱ
  • "Identification of bZIP interaction partners of viral proteins HBZ, MEQ, BZLF1, and K-bZIP using coiled-coil arrays."
    Reinke A.W., Grigoryan G., Keating A.E.
    Biochemistry 49:1985-1997(2010) [PubMed] [Europe PMC] [Abstract]
  • "Proteomic analyses reveal distinct chromatin-associated and soluble transcription factor complexes."
    Li X., Wang W., Wang J., Malovannaya A., Xi Y., Li W., Guerra R., Hawke D.H., Qin J., Chen J.
    Mol Syst Biol 11:775-775(2015) [PubMed] [Europe PMC] [Abstract]
  • Ref.43

    "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.
• protein-containing complex binding Source: Ensembl
• RNA binding Source: UniProtKBInferred from high throughput direct assayⁱ
  • "The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts."
    Baltz A.G., Munschauer M., Schwanhausser B., Vasile A., Murakawa Y., Schueler M., Youngs N., Penfold-Brown D., Drew K., Milek M., Wyler E., Bonneau R., Selbach M., Dieterich C., Landthaler M.
    Mol Cell 46:674-690(2012) [PubMed] [Europe PMC] [Abstract]
• RNA polymerase II cis-regulatory region sequence-specific DNA binding Source: BHF-UCLInferred from direct assayⁱ
  • "cJun modulates Ggamma-globin gene expression via an upstream cAMP response element."
    Kodeboyina S., Balamurugan P., Liu L., Pace B.S.
    Blood Cells Mol Dis 44:7-15(2010) [PubMed] [Europe PMC] [Abstract]
• RNA polymerase II-specific DNA-binding transcription factor binding Source: CAFAInferred from physical interactionⁱ
  • "Presenilin 1 suppresses the function of c-Jun homodimers via interaction with QM/Jif-1."
    Imafuku I., Masaki T., Waragai M., Takeuchi S., Kawabata M., Hirai S., Ohno S., Nee L.E., Lippa C.F., Kanazawa I., Imagawa M., Okazawa H.
    J Cell Biol 147:121-134(1999) [PubMed] [Europe PMC] [Abstract]
• R-SMAD binding Source: BHF-UCLInferred from physical interactionⁱ
  • Ref.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.
• sequence-specific double-stranded DNA binding Source: ARUK-UCLInferred from direct assayⁱ
  • "Impact of cytosine methylation on DNA binding specificities of human transcription factors."
    Yin Y., Morgunova E., Jolma A., Kaasinen E., Sahu B., Khund-Sayeed S., Das P.K., Kivioja T., Dave K., Zhong F., Nitta K.R., Taipale M., Popov A., Ginno P.A., Domcke S., Yan J., Schubeler D., Vinson C., Taipale J.
    Science 356:0-0(2017) [PubMed] [Europe PMC] [Abstract]
• transcription cis-regulatory region binding Source: UniProtKBInferred from direct assayⁱ
  • "A promoter within the E6 ORF of human papillomavirus type 16 contributes to the expression of the E7 oncoprotein from a monocistronic mRNA."
    Glahder J.A., Hansen C.N., Vinther J., Madsen B.S., Norrild B.
    J Gen Virol 84:3429-3441(2003) [PubMed] [Europe PMC] [Abstract]
  • Ref.28

    "The forkhead transcription factor FOXK2 promotes AP-1-mediated transcriptional regulation."
    Ji Z., Donaldson I.J., Liu J., Hayes A., Zeef L.A., Sharrocks A.D.
    Mol. Cell. Biol. 32:385-398(2012) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, DNA-BINDING.
  • Ref.38

    "A KRAS-directed transcriptional silencing pathway that mediates the CpG island methylator phenotype."
    Serra R.W., Fang M., Park S.M., Hutchinson L., Green M.R.
    Elife 3:E02313-E02313(2014) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, DNA-BINDING.
• transcription factor binding Source: BHF-UCLInferred from physical interactionⁱ
  • "Interaction of phosphorylated c-Jun with TCF4 regulates intestinal cancer development."
    Nateri A.S., Spencer-Dene B., Behrens A.
    Nature 437:281-285(2005) [PubMed] [Europe PMC] [Abstract]
• ubiquitin-like protein ligase binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.40

    "Synaptonuclear messenger PRR7 inhibits c-Jun ubiquitination and regulates NMDA-mediated excitotoxicity."
    Kravchick D.O., Karpova A., Hrdinka M., Lopez-Rojas J., Iacobas S., Carbonell A.U., Iacobas D.A., Kreutz M.R., Jordan B.A.
    EMBO J. 35:1923-1934(2016) [PubMed] [Europe PMC] [Abstract]

    Cited for: IDENTIFICATION IN COMPLEX WITH PRR7 AND FBXW7, INTERACTION WITH PRR7 AND FBXW7, UBIQUITINATION.
• ubiquitin protein ligase binding Source: UniProtKBInferred from physical interactionⁱ
  • "Human De-etiolated-1 regulates c-Jun by assembling a CUL4A ubiquitin ligase."
    Wertz I.E., O'Rourke K.M., Zhang Z., Dornan D., Arnott D., Deshaies R.J., Dixit V.M.
    Science 303:1371-1374(2004) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• aging Source: Ensembl
• angiogenesis Source: Ensembl
• cellular response to cadmium ion Source: CAFA <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Cadmium induces matrix metalloproteinase-9 expression via ROS-dependent EGFR, NF-кB, and AP-1 pathways in human endothelial cells."
    Lian S., Xia Y., Khoi P.N., Ung T.T., Yoon H.J., Kim N.H., Kim K.K., Jung Y.D.
    Toxicology 338:104-116(2015) [PubMed] [Europe PMC] [Abstract]
• cellular response to potassium ion starvation Source: Ensembl
• cellular response to reactive oxygen species Source: CAFAInferred from mutant phenotypeⁱ
  • "Cadmium induces matrix metalloproteinase-9 expression via ROS-dependent EGFR, NF-кB, and AP-1 pathways in human endothelial cells."
    Lian S., Xia Y., Khoi P.N., Ung T.T., Yoon H.J., Kim N.H., Kim K.K., Jung Y.D.
    Toxicology 338:104-116(2015) [PubMed] [Europe PMC] [Abstract]
• circadian rhythm Source: Ensembl
• learning Source: Ensembl
• membrane depolarization Source: Ensembl
• negative regulation by host of viral transcription Source: UniProtKBInferred from direct assayⁱ
  • "Enhancer binding factors AP-4 and AP-1 act in concert to activate SV40 late transcription in vitro."
    Mermod N., Williams T.J., Tjian R.
    Nature 332:557-561(1988) [PubMed] [Europe PMC] [Abstract]
• negative regulation of DNA binding Source: UniProtKBInferred from direct assayⁱ
  • "A promoter within the E6 ORF of human papillomavirus type 16 contributes to the expression of the E7 oncoprotein from a monocistronic mRNA."
    Glahder J.A., Hansen C.N., Vinther J., Madsen B.S., Norrild B.
    J Gen Virol 84:3429-3441(2003) [PubMed] [Europe PMC] [Abstract]
• negative regulation of transcription, DNA-templated Source: UniProtKBInferred from direct assayⁱ
  • "Enhancer binding factors AP-4 and AP-1 act in concert to activate SV40 late transcription in vitro."
    Mermod N., Williams T.J., Tjian R.
    Nature 332:557-561(1988) [PubMed] [Europe PMC] [Abstract]
• negative regulation of transcription by RNA polymerase II Source: ARUK-UCLInferred from direct assayⁱ
  • "Enhancer binding factors AP-4 and AP-1 act in concert to activate SV40 late transcription in vitro."
    Mermod N., Williams T.J., Tjian R.
    Nature 332:557-561(1988) [PubMed] [Europe PMC] [Abstract]
• negative regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress Source: ParkinsonsUK-UCLInferred from mutant phenotypeⁱ
  • "Parkin is transcriptionally regulated by ATF4: evidence for an interconnection between mitochondrial stress and ER stress."
    Bouman L., Schlierf A., Lutz A.K., Shan J., Deinlein A., Kast J., Galehdar Z., Palmisano V., Patenge N., Berg D., Gasser T., Augustin R., Trumbach D., Irrcher I., Park D.S., Wurst W., Kilberg M.S., Tatzelt J., Winklhofer K.F.
    Cell Death Differ 18:769-782(2011) [PubMed] [Europe PMC] [Abstract]
• positive regulation by host of viral transcription Source: UniProtKBInferred from direct assayⁱ
  • "Enhancer binding factors AP-4 and AP-1 act in concert to activate SV40 late transcription in vitro."
    Mermod N., Williams T.J., Tjian R.
    Nature 332:557-561(1988) [PubMed] [Europe PMC] [Abstract]
• positive regulation of apoptotic process Source: CAFAInferred from mutant phenotypeⁱ
  • "Presenilin 1 suppresses the function of c-Jun homodimers via interaction with QM/Jif-1."
    Imafuku I., Masaki T., Waragai M., Takeuchi S., Kawabata M., Hirai S., Ohno S., Nee L.E., Lippa C.F., Kanazawa I., Imagawa M., Okazawa H.
    J Cell Biol 147:121-134(1999) [PubMed] [Europe PMC] [Abstract]
• positive regulation of DNA replication Source: Ensembl
• positive regulation of DNA-templated transcription, initiation Source: CACAOInferred from direct assayⁱ
  • "Transcriptional regulation of the interleukin-11 gene by oncogenic Ras."
    Shin S.Y., Choi C., Lee H.G., Lim Y., Lee Y.H.
    Carcinogenesis 33:2467-2476(2012) [PubMed] [Europe PMC] [Abstract]
• positive regulation of monocyte differentiation Source: Ensembl
• positive regulation of neuron apoptotic process Source: Ensembl
• positive regulation of pri-miRNA transcription by RNA polymerase II Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "miR-221&222 regulate TRAIL resistance and enhance tumorigenicity through PTEN and TIMP3 downregulation."
    Garofalo M., Di Leva G., Romano G., Nuovo G., Suh S.S., Ngankeu A., Taccioli C., Pichiorri F., Alder H., Secchiero P., Gasparini P., Gonelli A., Costinean S., Acunzo M., Condorelli G., Croce C.M.
    Cancer Cell 16:498-509(2009) [PubMed] [Europe PMC] [Abstract]
  • "MiR-92a mediates AZD6244 induced apoptosis and G1-phase arrest of lymphoma cells by targeting Bim."
    Lv X.B., Zhang X., Deng L., Jiang L., Meng W., Lu Z., Wang X.
    Cell Biol Int 38:435-443(2014) [PubMed] [Europe PMC] [Abstract]
• positive regulation of transcription, DNA-templated Source: UniProtKBInferred from direct assayⁱ
  • Ref.28

    "The forkhead transcription factor FOXK2 promotes AP-1-mediated transcriptional regulation."
    Ji Z., Donaldson I.J., Liu J., Hayes A., Zeef L.A., Sharrocks A.D.
    Mol. Cell. Biol. 32:385-398(2012) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, DNA-BINDING.
  • "Enhancer binding factors AP-4 and AP-1 act in concert to activate SV40 late transcription in vitro."
    Mermod N., Williams T.J., Tjian R.
    Nature 332:557-561(1988) [PubMed] [Europe PMC] [Abstract]
• positive regulation of transcription by RNA polymerase II Source: UniProtKBInferred from direct assayⁱ
  • "Enhancer binding factors AP-4 and AP-1 act in concert to activate SV40 late transcription in vitro."
    Mermod N., Williams T.J., Tjian R.
    Nature 332:557-561(1988) [PubMed] [Europe PMC] [Abstract]
• positive regulation of vascular associated smooth muscle cell proliferation Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "miR-4632 mediates PDGF-BB-induced proliferation and antiapoptosis of human pulmonary artery smooth muscle cells via targeting cJUN."
    Qian Z., Li Y., Chen J., Li X., Gou D.
    Am J Physiol Cell Physiol 313:C380-C391(2017) [PubMed] [Europe PMC] [Abstract]
• Ras protein signal transduction Source: UniProtKBInferred from direct assayⁱ
  • Ref.38

    "A KRAS-directed transcriptional silencing pathway that mediates the CpG island methylator phenotype."
    Serra R.W., Fang M., Park S.M., Hutchinson L., Green M.R.
    Elife 3:E02313-E02313(2014) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, DNA-BINDING.
• regulation of cell cycle Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• regulation of cell population proliferation Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• regulation of transcription by RNA polymerase II Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• release of cytochrome c from mitochondria Source: Ensembl
• response to cAMP Source: Ensembl
• response to cytokine Source: Ensembl
• response to drug Source: Ensembl
• response to hydrogen peroxide Source: Ensembl
• response to lipopolysaccharide Source: Ensembl
• response to mechanical stimulus Source: Ensembl
• response to radiation Source: Ensembl
• SMAD protein signal transduction Source: BHF-UCLInferred from direct assayⁱ
  • Ref.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.
• transcription by RNA polymerase II Source: Ensembl
• transforming growth factor beta receptor signaling pathway Source: BHF-UCLInferred from direct assayⁱ
  • Ref.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.

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

• UniProt annotation
• GO - Cellular component

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

Keywords - Diseaseⁱ

Organism-specific databases

Miscellaneous databases

Chemistry databases

Genetic variation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• enzyme binding Source: UniProtKBInferred from physical interactionⁱ
  • "A high-confidence interaction map identifies SIRT1 as a mediator of acetylation of USP22 and the SAGA coactivator complex."
    Armour S.M., Bennett E.J., Braun C.R., Zhang X.Y., McMahon S.B., Gygi S.P., Harper J.W., Sinclair D.A.
    Mol Cell Biol 33:1487-1502(2013) [PubMed] [Europe PMC] [Abstract]
• HMG box domain binding Source: Ensembl
• identical protein binding Source: IntActInferred from physical interactionⁱ
  • "Identification of bZIP interaction partners of viral proteins HBZ, MEQ, BZLF1, and K-bZIP using coiled-coil arrays."
    Reinke A.W., Grigoryan G., Keating A.E.
    Biochemistry 49:1985-1997(2010) [PubMed] [Europe PMC] [Abstract]
  • "Proteomic analyses reveal distinct chromatin-associated and soluble transcription factor complexes."
    Li X., Wang W., Wang J., Malovannaya A., Xi Y., Li W., Guerra R., Hawke D.H., Qin J., Chen J.
    Mol Syst Biol 11:775-775(2015) [PubMed] [Europe PMC] [Abstract]
  • Ref.43

    "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.
• RNA polymerase II-specific DNA-binding transcription factor binding Source: CAFAInferred from physical interactionⁱ
  • "Presenilin 1 suppresses the function of c-Jun homodimers via interaction with QM/Jif-1."
    Imafuku I., Masaki T., Waragai M., Takeuchi S., Kawabata M., Hirai S., Ohno S., Nee L.E., Lippa C.F., Kanazawa I., Imagawa M., Okazawa H.
    J Cell Biol 147:121-134(1999) [PubMed] [Europe PMC] [Abstract]
• R-SMAD binding Source: BHF-UCLInferred from physical interactionⁱ
  • Ref.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.
• transcription factor binding Source: BHF-UCLInferred from physical interactionⁱ
  • "Interaction of phosphorylated c-Jun with TCF4 regulates intestinal cancer development."
    Nateri A.S., Spencer-Dene B., Behrens A.
    Nature 437:281-285(2005) [PubMed] [Europe PMC] [Abstract]
• ubiquitin-like protein ligase binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.40

    "Synaptonuclear messenger PRR7 inhibits c-Jun ubiquitination and regulates NMDA-mediated excitotoxicity."
    Kravchick D.O., Karpova A., Hrdinka M., Lopez-Rojas J., Iacobas S., Carbonell A.U., Iacobas D.A., Kreutz M.R., Jordan B.A.
    EMBO J. 35:1923-1934(2016) [PubMed] [Europe PMC] [Abstract]

    Cited for: IDENTIFICATION IN COMPLEX WITH PRR7 AND FBXW7, INTERACTION WITH PRR7 AND FBXW7, UBIQUITINATION.
• ubiquitin protein ligase binding Source: UniProtKBInferred from physical interactionⁱ
  • "Human De-etiolated-1 regulates c-Jun by assembling a CUL4A ubiquitin ligase."
    Wertz I.E., O'Rourke K.M., Zhang Z., Dornan D., Arnott D., Deshaies R.J., Dixit V.M.
    Science 303:1371-1374(2004) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

Chemistry databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Region

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

        10         20         30         40         50
MTAKMETTFY DDALNASFLP SESGPYGYSN PKILKQSMTL NLADPVGSLK 
        60         70         80         90        100
PHLRAKNSDL LTSPDVGLLK LASPELERLI IQSSNGHITT TPTPTQFLCP 
       110        120        130        140        150
KNVTDEQEGF AEGFVRALAE LHSQNTLPSV TSAAQPVNGA GMVAPAVASV 
       160        170        180        190        200
AGGSGSGGFS ASLHSEPPVY ANLSNFNPGA LSSGGGAPSY GAAGLAFPAQ 
       210        220        230        240        250
PQQQQQPPHH LPQQMPVQHP RLQALKEEPQ TVPEMPGETP PLSPIDMESQ 
       260        270        280        290        300
ERIKAERKRM RNRIAASKCR KRKLERIARL EEKVKTLKAQ NSELASTANM 
       310        320        330 
LREQVAQLKQ KVMNHVNSGC QLMLTQQLQT F                     

Experimental Info

Natural variant

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Genetic variation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. Human chromosome 1
   Human chromosome 1: entries, gene names and cross-references to MIM
2. Human entries with genetic variants
   List of human entries with genetic variants
3. Human variants curated from literature reports
   Index of human variants curated from literature reports
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