DNA damage-inducible transcript 3 protein

<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

<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 protein binding Source: UniProtKB <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
  • Ref.17

    "ER-stress-induced transcriptional regulation increases protein synthesis leading to cell death."
    Han J., Back S.H., Hur J., Lin Y.H., Gildersleeve R., Shan J., Yuan C.L., Krokowski D., Wang S., Hatzoglou M., Kilberg M.S., Sartor M.A., Kaufman R.J.
    Nat. Cell Biol. 15:481-490(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH ATF4.
• DNA binding Source: MGIInferred from direct assayⁱ
  • Ref.7

    "CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum."
    Marciniak S.J., Yun C.Y., Oyadomari S., Novoa I., Zhang Y., Jungreis R., Nagata K., Harding H.P., Ron D.
    Genes Dev. 18:3066-3077(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• DNA-binding transcription activator activity, RNA polymerase II-specific Source: MGI
• DNA-binding transcription factor activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.17

    "ER-stress-induced transcriptional regulation increases protein synthesis leading to cell death."
    Han J., Back S.H., Hur J., Lin Y.H., Gildersleeve R., Shan J., Yuan C.L., Krokowski D., Wang S., Hatzoglou M., Kilberg M.S., Sartor M.A., Kaufman R.J.
    Nat. Cell Biol. 15:481-490(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH ATF4.
• leucine zipper domain binding Source: MGI
• protein heterodimerization activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.17

    "ER-stress-induced transcriptional regulation increases protein synthesis leading to cell death."
    Han J., Back S.H., Hur J., Lin Y.H., Gildersleeve R., Shan J., Yuan C.L., Krokowski D., Wang S., Hatzoglou M., Kilberg M.S., Sartor M.A., Kaufman R.J.
    Nat. Cell Biol. 15:481-490(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH ATF4.
• protein homodimerization activity Source: Ensembl
• RNA polymerase II cis-regulatory region sequence-specific DNA binding Source: MGI
• transcription factor binding Source: ParkinsonsUK-UCL <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
  • "CHOP enhancement of gene transcription by interactions with Jun/Fos AP-1 complex proteins."
    Ubeda M., Vallejo M., Habener J.F.
    Mol Cell Biol 19:7589-7599(1999) [PubMed] [Europe PMC] [Abstract]
  • Ref.1

    "CHOP, a novel developmentally regulated nuclear protein that dimerizes with transcription factors C/EBP and LAP and functions as a dominant-negative inhibitor of gene transcription."
    Ron D., Habener J.F.
    Genes Dev. 6:439-453(1992) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
• transcription regulator inhibitor activity Source: ARUK-UCLInferred from direct assayⁱ
  • Ref.1

    "CHOP, a novel developmentally regulated nuclear protein that dimerizes with transcription factors C/EBP and LAP and functions as a dominant-negative inhibitor of gene transcription."
    Ron D., Habener J.F.
    Genes Dev. 6:439-453(1992) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
• transcription regulatory region sequence-specific DNA binding Source: ParkinsonsUK-UCLInferred from direct assayⁱ
  • Ref.7

    "CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum."
    Marciniak S.J., Yun C.Y., Oyadomari S., Novoa I., Zhang Y., Jungreis R., Nagata K., Harding H.P., Ron D.
    Genes Dev. 18:3066-3077(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.

GO - Biological processⁱ

• anterior/posterior axis specification Source: BHF-UCLInferred from direct assayⁱ
  • "The C/EBP homologous protein CHOP (GADD153) is an inhibitor of Wnt/TCF signals."
    Horndasch M., Lienkamp S., Springer E., Schmitt A., Pavenstaedt H., Walz G., Gloy J.
    Oncogene 25:3397-3407(2006) [PubMed] [Europe PMC] [Abstract]
• apoptotic process Source: UniProtKB <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
  • Ref.16

    "C/EBP homologous protein-10 (CHOP-10) limits postnatal neovascularization through control of endothelial nitric oxide synthase gene expression."
    Loinard C., Zouggari Y., Rueda P., Ramkhelawon B., Cochain C., Vilar J., Recalde A., Richart A., Charue D., Duriez M., Mori M., Arenzana-Seisdedos F., Levy B.I., Heymes C., Silvestre J.S.
    Circulation 125:1014-1026(2012) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• blood vessel maturation Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.16

    "C/EBP homologous protein-10 (CHOP-10) limits postnatal neovascularization through control of endothelial nitric oxide synthase gene expression."
    Loinard C., Zouggari Y., Rueda P., Ramkhelawon B., Cochain C., Vilar J., Recalde A., Richart A., Charue D., Duriez M., Mori M., Arenzana-Seisdedos F., Levy B.I., Heymes C., Silvestre J.S.
    Circulation 125:1014-1026(2012) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• cell cycle arrest Source: MGI
• cell redox homeostasis Source: MGI
• endoplasmic reticulum unfolded protein response Source: UniProtKBInferred from direct assayⁱ
  • Ref.17

    "ER-stress-induced transcriptional regulation increases protein synthesis leading to cell death."
    Han J., Back S.H., Hur J., Lin Y.H., Gildersleeve R., Shan J., Yuan C.L., Krokowski D., Wang S., Hatzoglou M., Kilberg M.S., Sartor M.A., Kaufman R.J.
    Nat. Cell Biol. 15:481-490(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH ATF4.
• ER overload response Source: MGIInferred from mutant phenotypeⁱ
  • "Targeted disruption of the Chop gene delays endoplasmic reticulum stress-mediated diabetes."
    Oyadomari S., Koizumi A., Takeda K., Gotoh T., Akira S., Araki E., Mori M.
    J Clin Invest 109:525-532(2002) [PubMed] [Europe PMC] [Abstract]
• establishment of protein localization to mitochondrion Source: ParkinsonsUK-UCLInferred from direct assayⁱ
  • "hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria."
    Gotoh T., Terada K., Oyadomari S., Mori M.
    Cell Death Differ. 11:390-402(2004) [PubMed] [Europe PMC] [Abstract]
• intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: UniProtKBInferred from direct assayⁱ
  • Ref.17

    "ER-stress-induced transcriptional regulation increases protein synthesis leading to cell death."
    Han J., Back S.H., Hur J., Lin Y.H., Gildersleeve R., Shan J., Yuan C.L., Krokowski D., Wang S., Hatzoglou M., Kilberg M.S., Sartor M.A., Kaufman R.J.
    Nat. Cell Biol. 15:481-490(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH ATF4.
• intrinsic apoptotic signaling pathway in response to nitrosative stress Source: ParkinsonsUK-UCLInferred from direct assayⁱ
  • "hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria."
    Gotoh T., Terada K., Oyadomari S., Mori M.
    Cell Death Differ. 11:390-402(2004) [PubMed] [Europe PMC] [Abstract]
• negative regulation of canonical Wnt signaling pathway Source: BHF-UCLInferred from direct assayⁱ
  • "The C/EBP homologous protein CHOP (GADD153) is an inhibitor of Wnt/TCF signals."
    Horndasch M., Lienkamp S., Springer E., Schmitt A., Pavenstaedt H., Walz G., Gloy J.
    Oncogene 25:3397-3407(2006) [PubMed] [Europe PMC] [Abstract]
• negative regulation of cold-induced thermogenesis Source: YuBioLabInferred from mutant phenotypeⁱ
  • "Activation of Toll-like receptor 4 (TLR4) attenuates adaptive thermogenesis via endoplasmic reticulum stress."
    Okla M., Wang W., Kang I., Pashaj A., Carr T., Chung S.
    J Biol Chem 290:26476-26490(2015) [PubMed] [Europe PMC] [Abstract]
• negative regulation of CREB transcription factor activity Source: MGI
• negative regulation of determination of dorsal identity Source: BHF-UCLInferred from direct assayⁱ
  • "The C/EBP homologous protein CHOP (GADD153) is an inhibitor of Wnt/TCF signals."
    Horndasch M., Lienkamp S., Springer E., Schmitt A., Pavenstaedt H., Walz G., Gloy J.
    Oncogene 25:3397-3407(2006) [PubMed] [Europe PMC] [Abstract]
• negative regulation of DNA binding Source: ParkinsonsUK-UCL <p>Inferred from Genetic Interaction</p> <p>Used to describe "traditional" genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ
  • Ref.1

    "CHOP, a novel developmentally regulated nuclear protein that dimerizes with transcription factors C/EBP and LAP and functions as a dominant-negative inhibitor of gene transcription."
    Ron D., Habener J.F.
    Genes Dev. 6:439-453(1992) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
• negative regulation of DNA-binding transcription factor activity Source: MGI
• negative regulation of fat cell differentiation Source: MGIInferred from genetic interactionⁱ
  • "RNase L controls terminal adipocyte differentiation, lipids storage and insulin sensitivity via CHOP10 mRNA regulation."
    Fabre O., Salehzada T., Lambert K., Boo Seok Y., Zhou A., Mercier J., Bisbal C.
    Cell Death Differ 19:1470-1481(2012) [PubMed] [Europe PMC] [Abstract]
• negative regulation of interferon-gamma production Source: MGI
• negative regulation of interleukin-17 production Source: MGI
• negative regulation of interleukin-4 production Source: MGI
• negative regulation of myoblast differentiation Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.15

    "Stress-induced C/EBP homology protein (CHOP) represses MyoD transcription to delay myoblast differentiation."
    Alter J., Bengal E.
    PLoS ONE 6:E29498-E29498(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION, INTERACTION WITH HDAC1.
• negative regulation of NF-kappaB transcription factor activity Source: MGI
• negative regulation of protein kinase B signaling Source: MGI
• negative regulation of RNA polymerase II regulatory region sequence-specific DNA binding Source: MGI
• negative regulation of transcription, DNA-templated Source: UniProtKBInferred from direct assayⁱ
  • Ref.15

    "Stress-induced C/EBP homology protein (CHOP) represses MyoD transcription to delay myoblast differentiation."
    Alter J., Bengal E.
    PLoS ONE 6:E29498-E29498(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION, INTERACTION WITH HDAC1.
• negative regulation of transcription by RNA polymerase II Source: BHF-UCLInferred from direct assayⁱ
  • "The C/EBP homologous protein CHOP (GADD153) is an inhibitor of Wnt/TCF signals."
    Horndasch M., Lienkamp S., Springer E., Schmitt A., Pavenstaedt H., Walz G., Gloy J.
    Oncogene 25:3397-3407(2006) [PubMed] [Europe PMC] [Abstract]
• positive regulation of apoptotic process Source: MGI
• positive regulation of autophagy in response to ER overload Source: MGI
• positive regulation of DNA-binding transcription factor activity Source: ParkinsonsUK-UCLInferred from direct assayⁱ
  • "CHOP enhancement of gene transcription by interactions with Jun/Fos AP-1 complex proteins."
    Ubeda M., Vallejo M., Habener J.F.
    Mol Cell Biol 19:7589-7599(1999) [PubMed] [Europe PMC] [Abstract]
• positive regulation of interleukin-8 production Source: MGI
• positive regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
• positive regulation of neuron apoptotic process Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.13

    "Neuronal apoptosis induced by endoplasmic reticulum stress is regulated by ATF4-CHOP-mediated induction of the Bcl-2 homology 3-only member PUMA."
    Galehdar Z., Swan P., Fuerth B., Callaghan S.M., Park D.S., Cregan S.P.
    J. Neurosci. 30:16938-16948(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INDUCTION.
• positive regulation of neuron death Source: ParkinsonsUK-UCLInferred from mutant phenotypeⁱ
  • "CHOP/GADD153 is a mediator of apoptotic death in substantia nigra dopamine neurons in an in vivo neurotoxin model of parkinsonism."
    Silva R.M., Ries V., Oo T.F., Yarygina O., Jackson-Lewis V., Ryu E.J., Lu P.D., Marciniak S.J., Ron D., Przedborski S., Kholodilov N., Greene L.A., Burke R.E.
    J Neurochem 95:974-986(2005) [PubMed] [Europe PMC] [Abstract]
• positive regulation of transcription, DNA-templated Source: UniProtKBInferred from direct assayⁱ
  • Ref.13

    "Neuronal apoptosis induced by endoplasmic reticulum stress is regulated by ATF4-CHOP-mediated induction of the Bcl-2 homology 3-only member PUMA."
    Galehdar Z., Swan P., Fuerth B., Callaghan S.M., Park D.S., Cregan S.P.
    J. Neurosci. 30:16938-16948(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INDUCTION.
• positive regulation of transcription by RNA polymerase II Source: ParkinsonsUK-UCLInferred from genetic interactionⁱ
  • "CHOP enhancement of gene transcription by interactions with Jun/Fos AP-1 complex proteins."
    Ubeda M., Vallejo M., Habener J.F.
    Mol Cell Biol 19:7589-7599(1999) [PubMed] [Europe PMC] [Abstract]
• positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress Source: ParkinsonsUK-UCLInferred from mutant phenotypeⁱ
  • Ref.7

    "CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum."
    Marciniak S.J., Yun C.Y., Oyadomari S., Novoa I., Zhang Y., Jungreis R., Nagata K., Harding H.P., Ron D.
    Genes Dev. 18:3066-3077(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• proteasome-mediated ubiquitin-dependent protein catabolic process Source: MGI
• regulation of autophagy Source: UniProtKB
• regulation of transcription, DNA-templated Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.8

    "TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death."
    Ohoka N., Yoshii S., Hattori T., Onozaki K., Hayashi H.
    EMBO J. 24:1243-1255(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
  • Ref.10

    "Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis."
    Li G., Mongillo M., Chin K.T., Harding H., Ron D., Marks A.R., Tabas I.
    J. Cell Biol. 186:783-792(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INDUCTION.
• regulation of transcription by RNA polymerase II Source: MGI
• release of sequestered calcium ion into cytosol Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.10

    "Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis."
    Li G., Mongillo M., Chin K.T., Harding H., Ron D., Marks A.R., Tabas I.
    J. Cell Biol. 186:783-792(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INDUCTION.
• response to endoplasmic reticulum stress Source: UniProtKBInferred from direct assayⁱ
  • Ref.10

    "Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis."
    Li G., Mongillo M., Chin K.T., Harding H., Ron D., Marks A.R., Tabas I.
    J. Cell Biol. 186:783-792(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INDUCTION.
  • Ref.13

    "Neuronal apoptosis induced by endoplasmic reticulum stress is regulated by ATF4-CHOP-mediated induction of the Bcl-2 homology 3-only member PUMA."
    Galehdar Z., Swan P., Fuerth B., Callaghan S.M., Park D.S., Cregan S.P.
    J. Neurosci. 30:16938-16948(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INDUCTION.
• response to starvation Source: UniProtKBInferred from direct assayⁱ
  • Ref.15

    "Stress-induced C/EBP homology protein (CHOP) represses MyoD transcription to delay myoblast differentiation."
    Alter J., Bengal E.
    PLoS ONE 6:E29498-E29498(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION, INTERACTION WITH HDAC1.
• response to unfolded protein Source: MGI
• sensory perception of sound Source: MGIInferred from genetic interactionⁱ
  • "Deletion of Tmtc4 activates the unfolded protein response and causes postnatal hearing loss."
    Li J., Akil O., Rouse S.L., McLaughlin C.W., Matthews I.R., Lustig L.R., Chan D.K., Sherr E.H.
    J Clin Invest 128:5150-5162(2018) [PubMed] [Europe PMC] [Abstract]
• Wnt signaling pathway Source: UniProtKB-KW

<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

<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

Chemistry 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%5Fprocessing%5Fsection">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 reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductionⁱ

Gene expression 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%5Fsection">'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%5Fsection">'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%5Fsection">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

• cAMP response element binding protein binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.17

    "ER-stress-induced transcriptional regulation increases protein synthesis leading to cell death."
    Han J., Back S.H., Hur J., Lin Y.H., Gildersleeve R., Shan J., Yuan C.L., Krokowski D., Wang S., Hatzoglou M., Kilberg M.S., Sartor M.A., Kaufman R.J.
    Nat. Cell Biol. 15:481-490(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH ATF4.
• leucine zipper domain binding Source: MGI
• protein heterodimerization activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.17

    "ER-stress-induced transcriptional regulation increases protein synthesis leading to cell death."
    Han J., Back S.H., Hur J., Lin Y.H., Gildersleeve R., Shan J., Yuan C.L., Krokowski D., Wang S., Hatzoglou M., Kilberg M.S., Sartor M.A., Kaufman R.J.
    Nat. Cell Biol. 15:481-490(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH ATF4.
• protein homodimerization activity Source: Ensembl
• transcription factor binding Source: ParkinsonsUK-UCLInferred from physical interactionⁱ
  • "CHOP enhancement of gene transcription by interactions with Jun/Fos AP-1 complex proteins."
    Ubeda M., Vallejo M., Habener J.F.
    Mol Cell Biol 19:7589-7599(1999) [PubMed] [Europe PMC] [Abstract]
  • Ref.1

    "CHOP, a novel developmentally regulated nuclear protein that dimerizes with transcription factors C/EBP and LAP and functions as a dominant-negative inhibitor of gene transcription."
    Ron D., Habener J.F.
    Genes Dev. 6:439-453(1992) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.

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

3D structure 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

Compositional bias

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domainⁱ

<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%5Flength">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>Sequences (2+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

        10         20         30         40         50
MAAESLPFTL ETVSSWELEA WYEDLQEVLS SDEIGGTYIS SPGNEEEESK 
        60         70         80         90        100
TFTTLDPASL AWLTEEPGPT EVTRTSQSPR SPDSSQSSMA QEEEEEEQGR 
       110        120        130        140        150
TRKRKQSGQC PARPGKQRMK EKEQENERKV AQLAEENERL KQEIERLTRE 
       160 
VETTRRALID RMVSLHQA                                    

Experimental Info

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<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

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic 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. MGD cross-references
   Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
2. SIMILARITY comments
   Index of protein domains and families