Transcription factor NF-E2 45 kDa subunit

<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

• cis-regulatory region sequence-specific DNA binding Source: RGDInferred from sequence orthologyⁱ
  • "Repression of human gamma-globin gene expression by a short isoform of the NF-E4 protein is associated with loss of NF-E2 and RNA polymerase II recruitment to the promoter."
    Zhao Q., Zhou W., Rank G., Sutton R., Wang X., Cumming H., Cerruti L., Cunningham J.M., Jane S.M.
    Blood 107:2138-2145(2006) [PubMed] [Europe PMC] [Abstract]
• DNA binding Source: RGDInferred from sequence orthologyⁱ
  • "A novel erythroid differentiation related gene EDRF1 upregulating globin gene expression in HEL cells."
    Wang D., Li Y., Shen B.
    Chin. Med. J. 115:1701-1705(2002) [PubMed] [Europe PMC] [Abstract]
• DNA-binding transcription factor activity 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%2Dgo%2Devidence%2Dcodes#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. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• protein N-terminus binding Source: RGDInferred from sequence orthologyⁱ
  • "NAPP2, a peroxisomal membrane protein, is also a transcriptional corepressor."
    Gavva N.R., Wen S.C., Daftari P., Moniwa M., Yang W.M., Yang-Feng L.P., Seto E., Davie J.R., Shen C.K.
    Genomics 79:423-431(2002) [PubMed] [Europe PMC] [Abstract]
• transcription regulatory region sequence-specific DNA binding 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. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• WW domain binding Source: RGDInferred from sequence orthologyⁱ
  • "Interaction of WW domains with hematopoietic transcription factor p45/NF-E2 and RNA polymerase II."
    Gavva N.R., Gavva R., Ermekova K., Sudol M., Shen C.J.
    J. Biol. Chem. 272:24105-24108(1997) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• cell-cell signaling Source: RGDInferred from sequence orthologyⁱ
  • "Megakaryocyte-osteoblast interaction revealed in mice deficient in transcription factors GATA-1 and NF-E2."
    Kacena M.A., Shivdasani R.A., Wilson K., Xi Y., Troiano N., Nazarian A., Gundberg C.M., Bouxsein M.L., Lorenzo J.A., Horowitz M.C.
    J. Bone Miner. Res. 19:652-660(2004) [PubMed] [Europe PMC] [Abstract]
• labyrinthine layer blood vessel development Source: RGDInferred from sequence orthologyⁱ
  • "p45NF-E2 represses Gcm1 in trophoblast cells to regulate syncytium formation, placental vascularization and embryonic growth."
    Kashif M., Hellwig A., Kolleker A., Shahzad K., Wang H., Lang S., Wolter J., Thati M., Vinnikov I., Bierhaus A., Nawroth P.P., Isermann B.
    Development 138:2235-2247(2011) [PubMed] [Europe PMC] [Abstract]
• negative regulation of bone mineralization Source: RGDInferred from sequence orthologyⁱ
  • "Megakaryocyte-osteoblast interaction revealed in mice deficient in transcription factors GATA-1 and NF-E2."
    Kacena M.A., Shivdasani R.A., Wilson K., Xi Y., Troiano N., Nazarian A., Gundberg C.M., Bouxsein M.L., Lorenzo J.A., Horowitz M.C.
    J. Bone Miner. Res. 19:652-660(2004) [PubMed] [Europe PMC] [Abstract]
• negative regulation of cell population proliferation Source: RGDInferred from sequence orthologyⁱ
  • "p45(NFE2) is a negative regulator of erythroid proliferation which contributes to the progression of Friend virus-induced erythroleukemias."
    Li Y.J., Higgins R.R., Pak B.J., Shivdasani R.A., Ney P.A., Archer M., Ben-David Y.
    Mol. Cell. Biol. 21:73-80(2001) [PubMed] [Europe PMC] [Abstract]
• negative regulation of syncytium formation by plasma membrane fusion Source: RGDInferred from sequence orthologyⁱ
  • "p45NF-E2 represses Gcm1 in trophoblast cells to regulate syncytium formation, placental vascularization and embryonic growth."
    Kashif M., Hellwig A., Kolleker A., Shahzad K., Wang H., Lang S., Wolter J., Thati M., Vinnikov I., Bierhaus A., Nawroth P.P., Isermann B.
    Development 138:2235-2247(2011) [PubMed] [Europe PMC] [Abstract]
• positive regulation of peptidyl-lysine acetylation Source: RGDInferred from sequence orthologyⁱ
  • "p45NF-E2 represses Gcm1 in trophoblast cells to regulate syncytium formation, placental vascularization and embryonic growth."
    Kashif M., Hellwig A., Kolleker A., Shahzad K., Wang H., Lang S., Wolter J., Thati M., Vinnikov I., Bierhaus A., Nawroth P.P., Isermann B.
    Development 138:2235-2247(2011) [PubMed] [Europe PMC] [Abstract]
• positive regulation of transcription, DNA-templated 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. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• regulation of gene expression Source: RGDInferred from sequence orthologyⁱ
  • "p45(NFE2) is a negative regulator of erythroid proliferation which contributes to the progression of Friend virus-induced erythroleukemias."
    Li Y.J., Higgins R.R., Pak B.J., Shivdasani R.A., Ney P.A., Archer M., Ben-David Y.
    Mol. Cell. Biol. 21:73-80(2001) [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. Bioinformatics 12:449-462(2011) [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

Keywords - Cellular componentⁱ

<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

<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

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

GO - Molecular functionⁱ

• protein N-terminus binding Source: RGDInferred from sequence orthologyⁱ
  • "NAPP2, a peroxisomal membrane protein, is also a transcriptional corepressor."
    Gavva N.R., Wen S.C., Daftari P., Moniwa M., Yang W.M., Yang-Feng L.P., Seto E., Davie J.R., Shen C.K.
    Genomics 79:423-431(2002) [PubMed] [Europe PMC] [Abstract]
• WW domain binding Source: RGDInferred from sequence orthologyⁱ
  • "Interaction of WW domains with hematopoietic transcription factor p45/NF-E2 and RNA polymerase II."
    Gavva N.R., Gavva R., Ermekova K., Sudol M., Shen C.J.
    J. Biol. Chem. 272:24105-24108(1997) [PubMed] [Europe PMC] [Abstract]

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

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

Motif

<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>Sequenceⁱ

<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.

        10         20         30         40         50
MPPCPPQPNR NRLPQLPTGE LGEMELTWQE IMSITELQGL NVPSEPSFEP 
        60         70         80         90        100
QAPTPYPGPL PPPTYCPCSI HPDAGFTLPP PPYELPASTP HAPDLPYSYG 
       110        120        130        140        150
NIAIPVSKPL TLSGLLNEPL PDPLALLDIG LPVGQPKPQE DPESDSGLSL 
       160        170        180        190        200
NYSDAESLEL EGTEAGRRRS EYVDMYPVEY PYSLMPNSLA HPNYTLPPTE 
       210        220        230        240        250
TPLVLESSSG PVRAKPAVRG EAGSRDERRA LAMKIPFPTD KIVNLPVDDF 
       260        270        280        290        300
NELLAQYPLT ESQLALVRDI RRRGKNKVAA QNCRKRKLET IVQLERELER 
       310        320        330        340        350
LGSERERLLR ARGEADRTLE VMRQQLTELY HDIFQHLRDE SGNSYSPEEY 
       360        370 
VLQQAADGAI FLVPRGTKME ATD                              

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

Proteomic 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. SIMILARITY comments
   Index of protein domains and families