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Q07279

- NFE2_MOUSE

UniProt

Q07279 - NFE2_MOUSE

Protein

Transcription factor NF-E2 45 kDa subunit

Gene

Nfe2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Component of the NF-E2 complex essential for regulating erythroid and megakaryocytic maturation and differentiation. Binds to the hypersensitive site 2 (HS2) of the beta-globin control region (LCR). This subunit (NFE2) recognizes the TCAT/C sequence of the AP-1-like core palindrome present in a number of erythroid and megakaryocytic gene promoters. Requires MAFK or other small MAF proteins for binding to the NF-E2 motif. May play a role in all aspects of hemoglobin production from globin and heme synthesis to procurement of iron.1 Publication

    GO - Molecular functioni

    1. protein binding Source: MGI
    2. sequence-specific DNA binding Source: InterPro
    3. sequence-specific DNA binding transcription factor activity Source: InterPro

    GO - Biological processi

    1. cell-cell signaling Source: MGI
    2. labyrinthine layer blood vessel development Source: MGI
    3. negative regulation of bone mineralization Source: MGI
    4. negative regulation of syncytium formation by plasma membrane fusion Source: MGI
    5. positive regulation of peptidyl-lysine acetylation Source: MGI
    6. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_198649. Factors involved in megakaryocyte development and platelet production.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription factor NF-E2 45 kDa subunit
    Alternative name(s):
    Leucine zipper protein NF-E2
    Nuclear factor, erythroid-derived 2 45 kDa subunit
    p45 NF-E2
    Gene namesi
    Name:Nfe2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:97308. Nfe2.

    Subcellular locationi

    NucleusPML body. Cytoplasm By similarity
    Note: The sumoylated form locates to the nuclear bodies PML oncogenic domains (PODs). Translocated to the cytoplasm through interaction with ITCH By similarity.By similarity

    GO - Cellular componenti

    1. actin cytoskeleton Source: Ensembl
    2. cytoplasm Source: UniProtKB-SubCell
    3. nucleoplasm Source: Reactome
    4. nucleus Source: MGI
    5. PML body Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi63 – 653PTY → AAA: Loss of transactivation activity. No induction of histone H3 'K-4' acetylation. 1 Publication
    Mutagenesisi157 – 1571S → A: Loss of MAPK8-mediated phosphorylation and no protein degradation. 2 Publications
    Mutagenesisi170 – 1701S → A: Abolishes phosphorylation by PKA. No effect on ability to bind DNA nor on transactivation activity. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 373373Transcription factor NF-E2 45 kDa subunitPRO_0000320078Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei157 – 1571Phosphoserine; by MAPK81 Publication
    Modified residuei170 – 1701Phosphoserine; by PKA1 Publication
    Cross-linki368 – 368Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

    Post-translational modificationi

    Phosphorylated on serine residues. In undifferentiated erythrocytes, phosphorylated by MAPK8 which then leads to ubiquitination and protein degradation By similarity.By similarity
    Sumoylated. Sumoylation is required for translocation to nuclear bodies PODs, anchoring to the gene loci, and transactivation of the beta-globin gene By similarity.By similarity
    Ubiquitinated mainly by 'Lys63'-linked ubiquitin By similarity. Polyubiquitination with 'Lys63'-linked ubiquitin by ITCH retains NFE2 in the cytoplasm preventing its transactivation activity By similarity. In undifferentiated erythrocyte, ubiquitinated after MAPK8-mediatd phosphorylation leading to protein degradation.By similarity2 Publications

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiQ07279.

    PTM databases

    PhosphoSiteiQ07279.

    Expressioni

    Gene expression databases

    ArrayExpressiQ07279.
    BgeeiQ07279.
    CleanExiMM_NFE2.
    GenevestigatoriQ07279.

    Interactioni

    Subunit structurei

    Homodimer; can bind DNA as a homodimer By similarity. Erythroid transcription activator nuclear factor erythroid-derived 2 (NF-E2), composed of a heterodimer of NFE2 and MAFK, possesses transactivation activity on beta-globin. Also forms high affinity heterodimer with MAFG; the interaction promotes erythropoiesis. Interacts (via the PXY motif 1) with ITCH (via the WW 1 domain); the interaction promotes 'Lys63'-linked ubiquitination of NFE2, translocates it to the cytoplasm and inhibits its transactivation activity. Interacts with KMT2D/MLL2; the interaction promotes transactivation of the beta-globin locus. Interacts with MAPK8 (phosphorylated form); the interaction leads to phosphorylation of NFE2 in undifferentiated cells.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi201742. 68 interactions.
    DIPiDIP-44849N.
    IntActiQ07279. 1 interaction.
    MINTiMINT-1539543.
    STRINGi10090.ENSMUSP00000121817.

    Structurei

    3D structure databases

    ProteinModelPortaliQ07279.
    SMRiQ07279. Positions 214-326.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini266 – 32964bZIPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 206206Transactivation domainBy similarityAdd
    BLAST
    Regioni1 – 8383Required for interaction with MAPK8By similarityAdd
    BLAST
    Regioni268 – 28720Basic motifPROSITE-ProRule annotationAdd
    BLAST
    Regioni291 – 2988Leucine-zipperPROSITE-ProRule annotation

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi61 – 655PXY motif 1
    Motifi79 – 835PXY motif 2

    Domaini

    The PXY motifs are required for binding WW domains. PXY1 is required to promote transactivation of beta-globin and for hyperacetylation of histone H3, but not for binding to the HS2 promoter site.

    Sequence similaritiesi

    Belongs to the bZIP family. CNC subfamily.Curated
    Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG326795.
    GeneTreeiENSGT00550000074399.
    HOGENOMiHOG000234410.
    HOVERGENiHBG002901.
    InParanoidiQ07279.
    KOiK09039.
    OrthoDBiEOG715Q3N.
    PhylomeDBiQ07279.
    TreeFamiTF326681.

    Family and domain databases

    Gene3Di1.10.880.10. 1 hit.
    InterProiIPR004827. bZIP.
    IPR004826. bZIP_Maf.
    IPR008917. TF_DNA-bd.
    [Graphical view]
    PfamiPF03131. bZIP_Maf. 1 hit.
    [Graphical view]
    SMARTiSM00338. BRLZ. 1 hit.
    [Graphical view]
    SUPFAMiSSF47454. SSF47454. 1 hit.
    PROSITEiPS50217. BZIP. 1 hit.
    PS00036. BZIP_BASIC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q07279-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPPCPPQQNR NRLSQLPVGE LGEMELTWQE IMSITELQGL NVPSETSFEP    50
    QAPTPYPGPL PPPTYCPCSI HPDAGFSLPP PSYELPASTP HVPELPYSYG 100
    NVAIPVSKPL TLSGLLNEPL PDHLALLDIG LPVGQPKPQE DPESDSGLSL 150
    NYSDAESLEL EGMEAGRRRS EYVDMYPVEY PYSLMPNSLA HPNYTLPPTE 200
    TPLALESSSG PVRAKPAVRG EAGSRDERRA LAMKIPFPTD KIVNLPVDDF 250
    NELLAQYPLT ESQLALVRDI RRRGKNKVAA QNCRKRKLET IVQLERELER 300
    LSSERERLLR ARGEADRTLE VMRQQLAELY HDIFQHLRDE SGNSYSPEEY 350
    VLQQAADGAI FLVPRGTKME ATD 373
    Length:373
    Mass (Da):41,565
    Last modified:November 1, 1996 - v1
    Checksum:i47E505F78B6EEB65
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti173 – 1731V → A in AAH62171. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L09600 mRNA. Translation: AAA40417.1.
    AK156702 mRNA. Translation: BAE33812.1.
    BC062171 mRNA. Translation: AAH62171.1.
    CCDSiCCDS27900.1.
    PIRiS32537.
    RefSeqiNP_032711.2. NM_008685.2.
    XP_006520633.1. XM_006520570.1.
    XP_006520634.1. XM_006520571.1.
    XP_006520635.1. XM_006520572.1.
    XP_006520636.1. XM_006520573.1.
    XP_006520637.1. XM_006520574.1.
    XP_006520638.1. XM_006520575.1.
    UniGeneiMm.457989.

    Genome annotation databases

    EnsembliENSMUST00000075192; ENSMUSP00000074684; ENSMUSG00000058794.
    ENSMUST00000134554; ENSMUSP00000117474; ENSMUSG00000058794.
    ENSMUST00000149111; ENSMUSP00000122476; ENSMUSG00000058794.
    ENSMUST00000156927; ENSMUSP00000114160; ENSMUSG00000058794.
    GeneIDi18022.
    KEGGimmu:18022.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L09600 mRNA. Translation: AAA40417.1 .
    AK156702 mRNA. Translation: BAE33812.1 .
    BC062171 mRNA. Translation: AAH62171.1 .
    CCDSi CCDS27900.1.
    PIRi S32537.
    RefSeqi NP_032711.2. NM_008685.2.
    XP_006520633.1. XM_006520570.1.
    XP_006520634.1. XM_006520571.1.
    XP_006520635.1. XM_006520572.1.
    XP_006520636.1. XM_006520573.1.
    XP_006520637.1. XM_006520574.1.
    XP_006520638.1. XM_006520575.1.
    UniGenei Mm.457989.

    3D structure databases

    ProteinModelPortali Q07279.
    SMRi Q07279. Positions 214-326.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201742. 68 interactions.
    DIPi DIP-44849N.
    IntActi Q07279. 1 interaction.
    MINTi MINT-1539543.
    STRINGi 10090.ENSMUSP00000121817.

    PTM databases

    PhosphoSitei Q07279.

    Proteomic databases

    PRIDEi Q07279.

    Protocols and materials databases

    DNASUi 18022.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000075192 ; ENSMUSP00000074684 ; ENSMUSG00000058794 .
    ENSMUST00000134554 ; ENSMUSP00000117474 ; ENSMUSG00000058794 .
    ENSMUST00000149111 ; ENSMUSP00000122476 ; ENSMUSG00000058794 .
    ENSMUST00000156927 ; ENSMUSP00000114160 ; ENSMUSG00000058794 .
    GeneIDi 18022.
    KEGGi mmu:18022.

    Organism-specific databases

    CTDi 4778.
    MGIi MGI:97308. Nfe2.

    Phylogenomic databases

    eggNOGi NOG326795.
    GeneTreei ENSGT00550000074399.
    HOGENOMi HOG000234410.
    HOVERGENi HBG002901.
    InParanoidi Q07279.
    KOi K09039.
    OrthoDBi EOG715Q3N.
    PhylomeDBi Q07279.
    TreeFami TF326681.

    Enzyme and pathway databases

    Reactomei REACT_198649. Factors involved in megakaryocyte development and platelet production.

    Miscellaneous databases

    NextBioi 293079.
    PROi Q07279.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q07279.
    Bgeei Q07279.
    CleanExi MM_NFE2.
    Genevestigatori Q07279.

    Family and domain databases

    Gene3Di 1.10.880.10. 1 hit.
    InterProi IPR004827. bZIP.
    IPR004826. bZIP_Maf.
    IPR008917. TF_DNA-bd.
    [Graphical view ]
    Pfami PF03131. bZIP_Maf. 1 hit.
    [Graphical view ]
    SMARTi SM00338. BRLZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47454. SSF47454. 1 hit.
    PROSITEi PS50217. BZIP. 1 hit.
    PS00036. BZIP_BASIC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Erythroid transcription factor NF-E2 is a haematopoietic-specific basic-leucine zipper protein."
      Andrews N.C., Erdjument-Bromage H., Davidson M.B., Tempst P., Orkin S.H.
      Nature 362:722-728(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: DBA.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: NOD.
      Tissue: Spleen.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "Multiple regions of p45 NF-E2 are required for beta-globin gene expression in erythroid cells."
      Bean T.L., Ney P.A.
      Nucleic Acids Res. 25:2509-2515(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: TRANSACTIVATION DOMAIN.
    5. "Regulation of the erythroid transcription factor NF-E2 by cyclic adenosine monophosphate-dependent protein kinase."
      Casteel D., Suhasini M., Gudi T., Naima R., Pilz R.B.
      Blood 91:3193-3201(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-170, FUNCTION, MUTAGENESIS OF SER-170.
    6. "A WW domain-binding motif within the activation domain of the hematopoietic transcription factor NF-E2 is essential for establishment of a tissue-specific histone modification pattern."
      Kiekhaefer C.M., Boyer M.E., Johnson K.D., Bresnick E.H.
      J. Biol. Chem. 279:7456-7461(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PXY MOTIF DOMAIN, MUTAGENESIS OF 63-PRO--TYR-65.
    7. "Sumoylation of p45/NF-E2: nuclear positioning and transcriptional activation of the mammalian beta-like globin gene locus."
      Shyu Y.-C., Lee T.-L., Ting C.-Y., Wen S.-C., Hsieh L.-J., Li Y.-C., Hwang J.-L., Lin C.-C., Shen C.-K.J.
      Mol. Cell. Biol. 25:10365-10378(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION.
    8. "Activator-mediated recruitment of the MLL2 methyltransferase complex to the beta-globin locus."
      Demers C., Chaturvedi C.-P., Ranish J.A., Juban G., Lai P., Morle F., Aebersold R., Dilworth F.J., Groudine M., Brand M.
      Mol. Cell 27:573-584(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KMT2D.
    9. "JNK-mediated turnover and stabilization of the transcription factor p45/NF-E2 during differentiation of murine erythroleukemia cells."
      Lee T.L., Shyu Y.C., Hsu P.H., Chang C.W., Wen S.C., Hsiao W.Y., Tsai M.D., Shen C.K.
      Proc. Natl. Acad. Sci. U.S.A. 107:52-57(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-157, INTERACTION WITH MAPK8, UBIQUITINATION, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF SER-157.

    Entry informationi

    Entry nameiNFE2_MOUSE
    AccessioniPrimary (citable) accession number: Q07279
    Secondary accession number(s): Q6P6K5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 114 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3