Nfe2
entrez
18022
canonical
uniprot
Q07279
canonical
ensembl
ENSMUSG00000058794
resolver
ensp
ENSMUSP00000074684
resolver
ensp
ENSMUSP00000114160
resolver
ensp
ENSMUSP00000117474
resolver
ensp
ENSMUSP00000122476
resolver
ensp
ENSMUSP00000335367
resolver
ensp
ENSMUSP00000365008
resolver
ensp
ENSMUSP00000365009
resolver
enst
ENSMUST00000075192
resolver
enst
ENSMUST00000134554
resolver
enst
ENSMUST00000149111
resolver
enst
ENSMUST00000156927
resolver
genesymbol
Nfe2
resolver
uniprot
A0A0R4J0Y5
resolver
uniprot
Q6P6K5
resolver
uniprot_entry
A0A0R4J0Y5_MOUSE
resolver
uniprot_entry
NFE2_MOUSE
resolver
uniprot_sec
Q6P6K5
resolver
amino_acid_sequence
MPPCPPQQNRNRLSQLPVGELGEMELTWQEIMSITELQGLNVPSETSFEPQAPTPYPGPLPPPTYCPCSIHPDAGFSLPPPSYELPASTPHVPELPYSYGNVAIPVSKPLTLSGLLNEPLPDHLALLDIGLPVGQPKPQEDPESDSGLSLNYSDAESLELEGMEAGRRRSEYVDMYPVEYPYSLMPNSLAHPNYTLPPTETPLALESSSGPVRAKPAVRGEAGSRDERRALAMKIPFPTDKIVNLPVDDFNELLAQYPLTESQLALVRDIRRRGKNKVAAQNCRKRKLETIVQLERELERLSSERERLLRARGEADRTLEVMRQQLAELYHDIFQHLRDESGNSYSPEEYVLQQAADGAIFLVPRGTKMEATD
uniprot
proteins
function
FUNCTION: 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. {ECO:0000269|PubMed:9558374}.
uniprot
proteins
mass_dalton
41565
uniprot
proteins
mutagenesis
MUTAGEN 63..65; /note="PTY->AAA: Loss of transactivation activity. No induction of histone H3 'K-4' acetylation."; /evidence="ECO:0000269|PubMed:14597626"; MUTAGEN 157; /note="S->A: Loss of MAPK8-mediated phosphorylation and no protein degradation."; /evidence="ECO:0000269|PubMed:19966288"; MUTAGEN 170; /note="S->A: Abolishes phosphorylation by PKA. No effect on ability to bind DNA nor on transactivation activity."; /evidence="ECO:0000269|PubMed:9558374
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on serine residues. In undifferentiated erythrocytes, phosphorylated by MAPK8 which then leads to ubiquitination and protein degradation (By similarity). {ECO:0000250}.; PTM: Sumoylated. Sumoylation is required for translocation to nuclear bodies PODs, anchoring to the gene loci, and transactivation of the beta-globin gene (By similarity). {ECO:0000250}.; PTM: 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. {ECO:0000250, ECO:0000269|PubMed:19966288, ECO:0000269|PubMed:9558374}.
uniprot
proteins
protein_family
BZIP family
uniprot
proteins
protein_family
CNC subfamily
uniprot
proteins
pubmed
14597626
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16287851
uniprot
proteins
pubmed
17707229
uniprot
proteins
pubmed
19966288
uniprot
proteins
pubmed
8469283
uniprot
proteins
pubmed
9171106
uniprot
proteins
pubmed
9558374
uniprot
proteins
sequence_length
373
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, PML body. Cytoplasm {ECO:0000250}. Note=The sumoylated form locates to the nuclear bodies PML oncogenic domains (PODs). Translocated to the cytoplasm through interaction with ITCH (By similarity). {ECO:0000250}.
uniprot
proteins