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Q07279

- NFE2_MOUSE

UniProt

Q07279 - NFE2_MOUSE

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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

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
Complete GO annotation...

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.

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
Complete GO annotation...

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. 1 Publication
Mutagenesisi170 – 1701S → A: Abolishes phosphorylation by PKA. No effect on ability to bind DNA nor on transactivation activity. 1 Publication

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.2 Publications
Sumoylated. Sumoylation is required for translocation to nuclear bodies PODs, anchoring to the gene loci, and transactivation of the beta-globin gene By similarity.1 Publication
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.1 Publication

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.2 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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini266 – 32964bZIPAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 206206Transactivation domain By similarityAdd
BLAST
Regioni1 – 8383Required for interaction with MAPK8 By similarityAdd
BLAST
Regioni268 – 28720Basic motif By similarityAdd
BLAST
Regioni291 – 2988Leucine-zipper By similarity

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.2 Publications

Sequence similaritiesi

Belongs to the bZIP family. CNC subfamily.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti173 – 1731V → A in AAH62171. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 113 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