Mouse Anti-NFE2L1 Recombinant Antibody (A1334) (CBMAB-AP5059LY)

Nuclear Factor, Erythroid 2 Like 1

This gene encodes a protein that is involved in globin gene expression in erythrocytes. Confusion has occurred in bibliographic databases due to the shared symbol of NRF1 for this gene, NFE2L1, and for "nuclear respiratory factor 1" which has an official symbol of NRF1. [provided by RefSeq, Jul 2008]

Nuclear Factor, Erythroid 2 Like 1; Nuclear Factor, Erythroid Derived 2, Like 1; Locus Control Region-Factor 1; Transcription Factor LCR-F1; Transcription Factor HBZ17; NF-E2-Related Factor 1; NFE2-Related Factor 1; TCF-11; TCF11;

CSB-MA037029

Anatomical structure morphogenesis Source: ProtInc
Cell redox homeostasis Source: UniProtKB
Cellular response to cholesterol Source: UniProtKB
Cellular response to oxidative stress Source: UniProtKB
Cholesterol homeostasis Source: UniProtKB
Cholesterol metabolic process Source: UniProtKB-KW
Heme biosynthetic process Source: ProtInc
Integrated stress response signaling Source: ComplexPortal
Lipid homeostasis Source: UniProtKB
Negative regulation of transcription by RNA polymerase II Source: UniProtKB
Negative regulation of transcription from RNA polymerase II promoter in response to stress Source: UniProtKB
Positive regulation of transcription from RNA polymerase II promoter in response to stress Source: UniProtKB
Regulation of odontoblast differentiation Source: UniProtKB
Regulation of transcription by RNA polymerase II Source: GO_Central

Endoplasmic reticulum membrane sensor NFE2L1:
Endoplasmic reticulum
Endoplasmic reticulum membrane
Note: In normal conditions, probably has a single-pass type II membrane protein topology, with the DNA-binding domain facing the endoplasmic reticulum lumen (PubMed:24448410). Following cellular stress, it is rapidly and efficiently retrotranslocated to the cytosolic side of the membrane, a process dependent on p97/VCP, to have a single-pass type III membrane protein topology with the major part of the protein facing the cytosol (PubMed:24448410). Retrotranslocated proteins are normally rapidly degraded by the proteasome and active species do not accumulate (PubMed:24448410). However, retrotranslocated protein NFE2L1 escapes degradation and is cleaved at Leu-104 by DDI2, releasing the protein from the endoplasmic reticulum membrane and forming the transcription factor NRF1 that translocates into the nucleus (PubMed:24448410).
Transcription factor NRF1:
Nucleus
Note: Translocates into the nucleus following cleavage of Endoplasmic reticulum membrane sensor NFE2L1 by aspartyl protease DDI2.

Helical: 7-24

Endoplasmic reticulum membrane sensor NFE2L1:
Cleaved at Leu-104 by the aspartyl protease DDI2 following retrotranslocation, releasing the protein from the endoplasmic reticulum membrane and forming the transcription factor NRF1 that translocates into the nucleus (PubMed:24448410, PubMed:27676297, PubMed:27676298, PubMed:27528193). Ubiquitination is prerequisite for cleavage by aspartyl protease DDI2 (PubMed:27676298).
Endoplasmic reticulum membrane sensor NFE2L1:
N-glycosylated in normal conditions, when it has a single-pass type II membrane protein topology, with the DNA-binding domain facing the endoplasmic reticulum lumen (PubMed:20932482, PubMed:24998528, PubMed:24448410, PubMed:27528193). Deglycosylated during retrotranslocation to the cytosolic side of the membrane, to have a single-pass type III membrane protein topology with the major part of the protein facing the cytosol (PubMed:20932482, PubMed:24998528, PubMed:24448410).
Endoplasmic reticulum membrane sensor NFE2L1:
Ubiquitinated by the SCF(FBXW7) complex and SYVN1/HRD1, leading to its degradation by the proteasome (PubMed:20932482). Ubiquitinated during retrotranslocation to the cytosolic side of the membrane: ubiquitination does not lead to degradation and is required for processing by the aspartyl protease DDI2 and subsequent release from the endoplasmic reticulum membrane (PubMed:24998528, PubMed:27676298).
Transcription factor NRF1:
Phosphorylation by CK2 at Ser-528 inhibits transcription factor activity, possibly by affecting DNA-binding activity (By similarity). Phosphorylation at Ser-599 is required for interaction with CEBPB (PubMed:15308669).
Transcription factor NRF1:
Ubiquitinated by the SCF(BTRC) complex in the nucleus, leading to its degradation by the proteasome.