Carbohydrate-responsive element-binding 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

• carbohydrate response element binding Source: BHF-UCL <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementⁱ
  • "Coordinate regulation/localization of the carbohydrate responsive binding protein (ChREBP) by two nuclear export signal sites: discovery of a new leucine-rich nuclear export signal site."
    Fukasawa M., Ge Q., Wynn R.M., Ishii S., Uyeda K.
    Biochem Biophys Res Commun 391:1166-1169(2010) [PubMed] [Europe PMC] [Abstract]
• DNA 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.1

    "Mechanism for fatty acid 'sparing' effect on glucose-induced transcription: regulation of carbohydrate-responsive element-binding protein by AMP-activated protein kinase."
    Kawaguchi T., Osatomi K., Yamashita H., Kabashima T., Uyeda K.
    J. Biol. Chem. 277:3829-3835(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT SER-568, MUTAGENESIS OF SER-568.
• DNA-binding transcription factor activity Source: RGDInferred from direct assayⁱ
  • Ref.1

    "Mechanism for fatty acid 'sparing' effect on glucose-induced transcription: regulation of carbohydrate-responsive element-binding protein by AMP-activated protein kinase."
    Kawaguchi T., Osatomi K., Yamashita H., Kabashima T., Uyeda K.
    J. Biol. Chem. 277:3829-3835(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT SER-568, MUTAGENESIS OF SER-568.
• DNA-binding transcription factor activity, RNA polymerase II-specific 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]
• DNA-binding transcription repressor activity, RNA polymerase II-specific Source: RGD
• protein heterodimerization activity Source: RGD
• protein kinase 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
  • Ref.1

    "Mechanism for fatty acid 'sparing' effect on glucose-induced transcription: regulation of carbohydrate-responsive element-binding protein by AMP-activated protein kinase."
    Kawaguchi T., Osatomi K., Yamashita H., Kabashima T., Uyeda K.
    J. Biol. Chem. 277:3829-3835(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT SER-568, MUTAGENESIS OF SER-568.
• RNA polymerase II cis-regulatory region sequence-specific DNA binding Source: RGD
• RNA polymerase II-specific DNA-binding transcription factor binding Source: RGD
• sequence-specific DNA binding Source: RGDInferred from direct assayⁱ
  • Ref.1

    "Mechanism for fatty acid 'sparing' effect on glucose-induced transcription: regulation of carbohydrate-responsive element-binding protein by AMP-activated protein kinase."
    Kawaguchi T., Osatomi K., Yamashita H., Kabashima T., Uyeda K.
    J. Biol. Chem. 277:3829-3835(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT SER-568, MUTAGENESIS OF SER-568.

GO - Biological processⁱ

• cellular response to glucose stimulus Source: BHF-UCLInferred from direct assayⁱ
  • "Coordinate regulation/localization of the carbohydrate responsive binding protein (ChREBP) by two nuclear export signal sites: discovery of a new leucine-rich nuclear export signal site."
    Fukasawa M., Ge Q., Wynn R.M., Ishii S., Uyeda K.
    Biochem Biophys Res Commun 391:1166-1169(2010) [PubMed] [Europe PMC] [Abstract]
• energy homeostasis 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.1

    "Mechanism for fatty acid 'sparing' effect on glucose-induced transcription: regulation of carbohydrate-responsive element-binding protein by AMP-activated protein kinase."
    Kawaguchi T., Osatomi K., Yamashita H., Kabashima T., Uyeda K.
    J. Biol. Chem. 277:3829-3835(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT SER-568, MUTAGENESIS OF SER-568.
• fatty acid homeostasis Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.1

    "Mechanism for fatty acid 'sparing' effect on glucose-induced transcription: regulation of carbohydrate-responsive element-binding protein by AMP-activated protein kinase."
    Kawaguchi T., Osatomi K., Yamashita H., Kabashima T., Uyeda K.
    J. Biol. Chem. 277:3829-3835(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT SER-568, MUTAGENESIS OF SER-568.
• glucose homeostasis Source: RGD
• glucose mediated signaling pathway Source: RGD
• negative regulation of oxidative phosphorylation Source: RGD
• negative regulation of peptidyl-serine phosphorylation Source: RGD
• negative regulation of transcription, DNA-templated Source: RGD
• negative regulation of transcription by RNA polymerase II Source: RGD
• positive regulation of cell population proliferation Source: RGD
• positive regulation of fatty acid biosynthetic process Source: RGD
• positive regulation of glycolytic process Source: RGD
• positive regulation of lipid biosynthetic process Source: RGD
• positive regulation of transcription, DNA-templated Source: RGD
• positive regulation of transcription by RNA polymerase II Source: RGD
• regulation of glycolytic process Source: RGDInferred from direct assayⁱ
  • Ref.1

    "Mechanism for fatty acid 'sparing' effect on glucose-induced transcription: regulation of carbohydrate-responsive element-binding protein by AMP-activated protein kinase."
    Kawaguchi T., Osatomi K., Yamashita H., Kabashima T., Uyeda K.
    J. Biol. Chem. 277:3829-3835(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT SER-568, MUTAGENESIS OF SER-568.
• regulation of transcription by RNA polymerase II Source: RGDInferred from direct assayⁱ
  • Ref.1

    "Mechanism for fatty acid 'sparing' effect on glucose-induced transcription: regulation of carbohydrate-responsive element-binding protein by AMP-activated protein kinase."
    Kawaguchi T., Osatomi K., Yamashita H., Kabashima T., Uyeda K.
    J. Biol. Chem. 277:3829-3835(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT SER-568, MUTAGENESIS OF SER-568.
• response to glucose Source: RGDInferred from direct assayⁱ
  • "A glucose-responsive transcription factor that regulates carbohydrate metabolism in the liver."
    Yamashita H., Takenoshita M., Sakurai M., Bruick R.K., Henzel W.J., Shillinglaw W., Arnot D., Uyeda K.
    Proc Natl Acad Sci U S A 98:9116-9121(2001) [PubMed] [Europe PMC] [Abstract]

<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

<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 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

GO - Molecular functionⁱ

• protein heterodimerization activity Source: RGD
• protein kinase binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.1

    "Mechanism for fatty acid 'sparing' effect on glucose-induced transcription: regulation of carbohydrate-responsive element-binding protein by AMP-activated protein kinase."
    Kawaguchi T., Osatomi K., Yamashita H., Kabashima T., Uyeda K.
    J. Biol. Chem. 277:3829-3835(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT SER-568, MUTAGENESIS OF SER-568.
• RNA polymerase II-specific DNA-binding transcription factor binding Source: RGD

<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

<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

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>Sequence (1+)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 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MARALADLSV NLQVPRVVPS PDSDSDTDLE DPSPRRSAGG LHRSQVIHSG 
        60         70         80         90        100
HFMVSSPHSD SLTRRRDQEG PVGLADFGPR SIDPTLTRLF ECLSLAYSGK 
       110        120        130        140        150
LVSPKWKNFK GLKLLCRDKI RLNNAIWRAW YIQYVQRRKS PVCGFVTPLQ 
       160        170        180        190        200
GSEADEHRKP EAVVLEGNYW KRRIEVVMRE YHKWRIYYKK RLRKSSREGD 
       210        220        230        240        250
FLAPKQVEGG WPPPERWCEQ LFSSVVPVLL GGSEEEPGGR QLLDLDCFLS 
       260        270        280        290        300
DISDTLFTMT QPSPSSLQLP SEDAYVGNAD MIQPDLTPLQ PSLDDFMEIS 
       310        320        330        340        350
DFFTNYRPPQ TPTSSNFPEP PSFGPMADSL FSGGILGPEM PSPASASSSS 
       360        370        380        390        400
GMTPLSGNTR LQARNSCSGP LDPSTFPSSE FLLPEDPKTK MPPAPVPTPL 
       410        420        430        440        450
LPYPGPVKVH GLEPCTPSPF PTMAPPPALL SEEPLFSARF PFTTVPPAPG 
       460        470        480        490        500
VSTLPAPTTF VPTPQPGPGP GPVPFPVDHL PHGYLEPVFG PHFTVPQGVQ 
       510        520        530        540        550
PRCKPCSPPP GGRKASPPTL TSATASPTAT ATARDNNPCL TQLLRAAKPE 
       560        570        580        590        600
QVLEPSTVPS TLLRPPESPD AVPEIPRVRA FYPPIPAPTP PRPPPGPATL 
       610        620        630        640        650
APPRSLVVPK AERLSPPASS GSERRPSGDL NSIQPPGALS VHLSPPQTVL 
       660        670        680        690        700
SRGRVDNNKM ENRRITHISA EQKRRFNIKL GFDTLHGLVS TLSAQPSLKV 
       710        720        730        740        750
SKATTLQKTA EYILMLQQER AAMQEEAQQL RDEIEELNAA INLCQQQLPA 
       760        770        780        790        800
TGVPITHQRF DQMRDMFDDY VRTRTLHNWK FWVFSILIRP LFESFNGMVS 
       810        820        830        840        850
TASLHSLRQT SLAWLDQYCS LPALRPTVLN SLRQLSTSTS ILTDPSLVPE 
       860 
QATRAVTEGP LGRPL                                       

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

• 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

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous 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. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references