Nuclear factor erythroid 2-related factor 2

<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

• DNA binding Source: MGI <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
  • 12220541
  • 14517290
  • 15870285
• DNA-binding transcription factor activity Source: MGIInferred from direct assayⁱ
  • 12220541
  • 14517290
• protein domain specific binding Source: MGI
• protein heterodimerization activity Source: ParkinsonsUK-UCL <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
  • 14978030
• RNA polymerase II activating transcription factor binding Source: MGI
• RNA polymerase II distal enhancer sequence-specific DNA binding Source: NTNU_SBInferred from direct assayⁱ
  • 10037736
• sequence-specific DNA binding Source: MGI
• transcriptional activator activity, RNA polymerase II distal enhancer sequence-specific DNA binding Source: NTNU_SBInferred from direct assayⁱ
  • 10037736
• transcription cofactor binding Source: MGI
• transcription factor 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
  • 17920186
• transcription regulatory region sequence-specific DNA binding Source: MGI

GO - Biological processⁱ

• aflatoxin catabolic process Source: MGI
• aging Source: Ensembl
• cell redox homeostasis Source: ParkinsonsUK-UCL <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
  • 14978030
• cellular response to angiotensin Source: Ensembl
• cellular response to drug Source: MGIInferred from mutant phenotypeⁱ
  • 24486487
• cellular response to fluid shear stress Source: UniProtKB
• cellular response to glucose starvation Source: ParkinsonsUK-UCLInferred from mutant phenotypeⁱ
  • 14978030
• cellular response to hydrogen peroxide Source: MGI
• cellular response to laminar fluid shear stress Source: MGI
• cellular response to oxidative stress Source: BHF-UCLInferred from direct assayⁱ
  • 20978343
• cellular response to tumor necrosis factor Source: MGI
• endoplasmic reticulum unfolded protein response Source: MGIInferred from direct assayⁱ
  • 14517290
• inflammatory response Source: MGIInferred from mutant phenotypeⁱ
  • 24486487
• negative regulation of cardiac muscle cell apoptotic process Source: MGI
• negative regulation of cell death Source: MGI
• negative regulation of endothelial cell apoptotic process Source: MGI
• negative regulation of hematopoietic stem cell differentiation Source: CACAOInferred from mutant phenotypeⁱ
  • 23434824
• negative regulation of hydrogen peroxide-induced cell death Source: MGI
• negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: MGI
• negative regulation of vascular associated smooth muscle cell migration Source: MGI
• PERK-mediated unfolded protein response Source: ParkinsonsUK-UCLInferred from direct assayⁱ
  • 14517290
• positive regulation of angiogenesis Source: MGI
• positive regulation of blood coagulation Source: BHF-UCLInferred from mutant phenotypeⁱ
  • 20978343
• positive regulation of blood vessel endothelial cell migration Source: MGI
• positive regulation of gene expression 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
  • 14978030
• positive regulation of glucose import Source: CACAOInferred from direct assayⁱ
  • 24024172
• positive regulation of glutathione biosynthetic process Source: ParkinsonsUK-UCLInferred from mutant phenotypeⁱ
  • 14978030
• positive regulation of neuron projection development Source: MGI
• positive regulation of reactive oxygen species metabolic process Source: BHF-UCLInferred from mutant phenotypeⁱ
  • 20978343
• positive regulation of transcription, DNA-templated Source: MGIInferred from direct assayⁱ
  • 14517290
  • 15870285
• positive regulation of transcription by RNA polymerase II Source: NTNU_SBInferred from direct assayⁱ
  • 10037736
  • 15574414
• positive regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: MGI
• positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress Source: MGI
• positive regulation of transcription from RNA polymerase II promoter in response to stress Source: MGI
• proteasomal ubiquitin-independent protein catabolic process Source: UniProtKB
• proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
• protein ubiquitination Source: UniProtKB
• regulation of embryonic development Source: MGIInferred from genetic interactionⁱ
  • 15087497
• regulation of removal of superoxide radicals Source: BHF-UCLInferred from mutant phenotypeⁱ
  • 20978343
• regulation of transcription, DNA-templated Source: MGIInferred from direct assayⁱ
  • 12220541
• response to endoplasmic reticulum stress Source: ParkinsonsUK-UCLInferred from mutant phenotypeⁱ
  • 14978030

<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

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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypeⁱ

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_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

<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%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• protein domain specific binding Source: MGI
• protein heterodimerization activity Source: ParkinsonsUK-UCLTraceable author statementⁱ
  • 14978030
• RNA polymerase II activating transcription factor binding Source: MGI
• transcription cofactor binding Source: MGI
• transcription factor binding Source: UniProtKBInferred from physical interactionⁱ
  • 17920186

Protein-protein interaction 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>.<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
MMDLELPPPG LQSQQDMDLI DILWRQDIDL GVSREVFDFS QRQKDYELEK 
        60         70         80         90        100
QKKLEKERQE QLQKEQEKAF FAQFQLDEET GEFLPIQPAQ HIQTDTSGSA 
       110        120        130        140        150
SYSQVAHIPK QDALYFEDCM QLLAETFPFV DDHESLALDI PSHAESSVFT 
       160        170        180        190        200
APHQAQSLNS SLEAAMTDLS SIEQDMEQVW QELFSIPELQ CLNTENKQLA 
       210        220        230        240        250
DTTAVPSPEA TLTEMDSNYH FYSSISSLEK EVGNCGPHFL HGFEDSFSSI 
       260        270        280        290        300
LSTDDASQLT SLDSNPTLNT DFGDEFYSAF IAEPSDGGSM PSSAAISQSL 
       310        320        330        340        350
SELLDGTIEG CDLSLCKAFN PKHAEGTMEF NDSDSGISLN TSPSRASPEH 
       360        370        380        390        400
SVESSIYGDP PPGFSDSEME ELDSAPGSVK QNGPKAQPAH SPGDTVQPLS 
       410        420        430        440        450
PAQGHSAPMR ESQCENTTKK EVPVSPGHQK APFTKDKHSS RLEAHLTRDE 
       460        470        480        490        500
LRAKALHIPF PVEKIINLPV DDFNEMMSKE QFNEAQLALI RDIRRRGKNK 
       510        520        530        540        550
VAAQNCRKRK LENIVELEQD LGHLKDEREK LLREKGENDR NLHLLKRRLS 
       560        570        580        590 
TLYLEVFSML RDEDGKPYSP SEYSLQQTRD GNVFLVPKSK KPDTKKN    

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

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