NFE2L1

Functionⁱ

Endoplasmic reticulum membrane sensor NFE2L1: Endoplasmic reticulum membrane sensor that translocates into the nucleus in response to various stresses to act as a transcription factor (PubMed:20932482, PubMed:24448410). Constitutes a precursor of the transcription factor NRF1 (By similarity). Able to detect various cellular stresses, such as cholesterol excess, oxidative stress or proteasome inhibition (PubMed:20932482). In response to stress, it is released from the endoplasmic reticulum membrane following cleavage by the protease DDI2 and translocates into the nucleus to form the transcription factor NRF1 (By similarity). Acts as a key sensor of cholesterol excess: in excess cholesterol conditions, the endoplasmic reticulum membrane form of the protein directly binds cholesterol via its CRAC motif, preventing cleavage and release of the transcription factor NRF1, thereby allowing expression of genes promoting cholesterol removal, such as CD36 (By similarity). Involved in proteasome homeostasis: in response to proteasome inhibition, it is released from the endoplasmic reticulum membrane, translocates to the nucleus and activates expression of genes encoding proteasome subunits (PubMed:20932482).By similarity2 Publications

Transcription factor NRF1: CNC-type bZIP family transcription factor that translocates to the nucleus and regulates expression of target genes in response to various stresses (PubMed:8932385, PubMed:9421508). Heterodimerizes with small-Maf proteins (MAFF, MAFG or MAFK) and binds DNA motifs including the antioxidant response elements (AREs), which regulate expression of genes involved in oxidative stress response (PubMed:8932385, PubMed:9421508). Activates or represses expression of target genes, depending on the context (PubMed:8932385, PubMed:9421508). Plays a key role in cholesterol homeostasis by acting as a sensor of cholesterol excess: in low cholesterol conditions, translocates into the nucleus and represses expression of genes involved in defense against cholesterol excess, such as CD36 (By similarity). In excess cholesterol conditions, the endoplasmic reticulum membrane form of the protein directly binds cholesterol via its CRAC motif, preventing cleavage and release of the transcription factor NRF1, thereby allowing expression of genes promoting cholesterol removal (By similarity). Critical for redox balance in response to oxidative stress: acts by binding the AREs motifs on promoters and mediating activation of oxidative stress response genes, such as GCLC, GCLM, GSS, MT1 and MT2 (By similarity). Plays an essential role during fetal liver hematopoiesis: probably has a protective function against oxidative stress and is involved in lipid homeostasis in the liver (By similarity). Involved in proteasome homeostasis: in response to proteasome inhibition, mediates the 'bounce-back' of proteasome subunits by translocating into the nucleus and activating expression of genes encoding proteasome subunits (PubMed:20932482). Also involved in regulating glucose flux (By similarity). Together with CEBPB; represses expression of DSPP during odontoblast differentiation (PubMed:15308669). In response to ascorbic acid induction, activates expression of SP7/Osterix in osteoblasts.By similarity4 Publications

Caution

Endoplasmic reticulum membrane sensor NFE2L1: According to a report, processing following retrotranslocation is dependent on the proteasome (PubMed:24998528). However, it was later shown that processing takes place in a proteasome-independent manner (PubMed:27676297, PubMed:27676298).3 Publications

Endoplasmic reticulum membrane sensor NFE2L1: its topology is subject to discussion. According to some groups, it has a single-pass type II membrane protein in normal conditions and is retrotranslocated into a single-pass type III membrane protein in response to stress (PubMed:24448410). According to other reports, it is integrated into the endoplasmic reticulum membrane via multiple membrane-spanning alpha-helices.By similarity1 Publication

Transcription factor NRF1: Was initially thought to activate erythroid-specific, globin gene expression (PubMed:8036168). Knockout experiments in mouse however demonstrated that it is not the case.By similarity1 Publication

GO - Molecular functionⁱ

cholesterol binding
Source: UniProtKB
Inferred from sequence or structural similarityⁱ
- 29149604
distal enhancer DNA-binding transcription activator activity, RNA polymerase II-specific Source: Ensembl
DNA-binding transcription factor activity
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
DNA-binding transcription factor activity, RNA polymerase II-specific Source: NTNU_SB
lipid binding Source: UniProtKB-KW
protein-containing complex binding Source: Ensembl
protein domain specific binding Source: Ensembl
protein heterodimerization activity
Source: UniProtKB
Inferred from physical interactionⁱ
- 8932385
- 9421508
proximal promoter DNA-binding transcription activator activity, RNA polymerase II-specific
Source: UniProtKB
Inferred from sequence or structural similarityⁱ
proximal promoter DNA-binding transcription repressor activity, RNA polymerase II-specific
Source: UniProtKB
Inferred from direct assayⁱ
- 15308669
RNA polymerase II distal enhancer sequence-specific DNA binding Source: Ensembl
RNA polymerase II proximal promoter sequence-specific DNA binding
Source: UniProtKB
Inferred from direct assayⁱ
- 8932385
- 9421508
transcription coregulator activity
Source: ProtInc
Traceable author statementⁱ
- 9826775
transcription regulatory region sequence-specific DNA binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

anatomical structure morphogenesis
Source: ProtInc
Traceable author statementⁱ
- 9501099
cell redox homeostasis
Source: UniProtKB
Inferred from sequence or structural similarityⁱ
- 10601325
- 11342101
cellular response to cholesterol
Source: UniProtKB
Inferred from sequence or structural similarityⁱ
- 29149604
cellular response to oxidative stress
Source: UniProtKB
Inferred from sequence or structural similarityⁱ
- 10601325
- 11342101
cholesterol homeostasis
Source: UniProtKB
Inferred from sequence or structural similarityⁱ
- 29149604
cholesterol metabolic process Source: UniProtKB-KW
erythrocyte differentiation Source: Ensembl
heme biosynthetic process
Source: ProtInc
Traceable author statementⁱ
- 9501099
inflammatory response
Source: ProtInc
Traceable author statementⁱ
- 9826775
lipid homeostasis
Source: UniProtKB
Inferred from sequence or structural similarityⁱ
- 22586274
negative regulation of transcription by RNA polymerase II
Source: UniProtKB
Inferred from direct assayⁱ
- 15308669
negative regulation of transcription from RNA polymerase II promoter in response to stress
Source: UniProtKB
Inferred from sequence or structural similarityⁱ
- 29149604
positive regulation of transcription, DNA-templated
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
positive regulation of transcription from RNA polymerase II promoter in response to stress
Source: UniProtKB
Inferred from sequence or structural similarityⁱ
regulation of odontoblast differentiation
Source: UniProtKB
Inferred from direct assayⁱ
- 15308669
transcription by RNA polymerase II
Source: ProtInc
Traceable author statementⁱ
- 9826775

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Activator, DNA-binding, Repressor
Biological process	Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism, Transcription, Transcription regulation
Ligand	Lipid-binding

Enzyme and pathway databases

SignaLinkⁱ	Q14494
SIGNORⁱ	Q14494

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Endoplasmic reticulum membrane sensor NFE2L1Curated Alternative name(s): Locus control region-factor 11 Publication Short name: LCR-F11 Publication Nuclear factor erythroid 2-related factor 1 Short name: NF-E2-related factor 12 Publications Short name: NFE2-related factor 12 Publications Nuclear factor, erythroid derived 2, like 1 Protein NRF1, p120 form1 Publication Transcription factor 111 Publication Short name: TCF-111 Publication Cleaved into the following chain: Transcription factor NRF1Curated Alternative name(s): Protein NRF1, p110 form1 Publication
Gene namesⁱ	Name:NFE2L1 Synonyms:HBZ17, NRF12 Publications, TCF111 Publication
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 17

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000082641.15
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:7781 NFE2L1
MIMⁱ	163260 gene
neXtProtⁱ	NX_Q14494

Topology

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Transmembraneⁱ	7 – 24	Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST		18

Keywords - Cellular componentⁱ

Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	101 – 106	NAWLVH → AAAAAA in m1; impaired protein cleavage. 1 Publication	6
Mutagenesisⁱ	101 – 103	NAW → AAA in m2; impaired protein cleavage. 1 Publication	3
Mutagenesisⁱ	103 – 104	WL → AA in m5; impaired protein cleavage. 1 Publication	2
Mutagenesisⁱ	103	W → A in m3; impaired protein cleavage. 1 Publication	1
Mutagenesisⁱ	104 – 106	LVH → AAA in m6; Slightly impaired protein cleavage. 1 Publication	3
Mutagenesisⁱ	104	L → A in m4; Slightly impaired protein cleavage. 1 Publication	1
Mutagenesisⁱ	599	S → A: Impaired interaction with CEBPB. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	4779
Open Targets More...OpenTargetsⁱ	ENSG00000082641
PharmGKBⁱ	PA31587

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB04147 Lauryl Dimethylamine-N-Oxide

DrugBankⁱ

DB04147 Lauryl Dimethylamine-N-Oxide

Polymorphism and mutation databases

BioMutaⁱ	NFE2L1
DMDMⁱ	3183180

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000076447	1 – 772	Endoplasmic reticulum membrane sensor NFE2L1Add BLAST		772
ChainⁱPRO_0000443103	104 – 772	Transcription factor NRF11 PublicationAdd BLAST		669

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Glycosylationⁱ	348	N-linked (GlcNAc...) asparagineSequence analysis	1
Glycosylationⁱ	360	N-linked (GlcNAc...) asparagineSequence analysis	1
Glycosylationⁱ	412	N-linked (GlcNAc...) asparagineSequence analysis	1
Glycosylationⁱ	423	N-linked (GlcNAc...) asparagineSequence analysis	1
Modified residueⁱ	528	Phosphoserine; by CK2By similarity	1
Modified residueⁱ	599	Phosphoserine; by PKA1 Publication	1

Post-translational modificationⁱ

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).4 Publications

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).4 Publications

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).By similarity3 Publications

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).By similarity1 Publication

Transcription factor NRF1: Ubiquitinated by the SCF(BTRC) complex in the nucleus, leading to its degradation by the proteasome.By similarity

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Siteⁱ	103 – 104	Cleavage; by DDI21 Publication		2

Keywords - PTMⁱ

Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	Q14494
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q14494
PaxDbⁱ	Q14494
PeptideAtlas More...PeptideAtlasⁱ	Q14494
PRIDEⁱ	Q14494
ProteomicsDBⁱ	60003 60004 [Q14494-2]

PTM databases

iPTMnetⁱ	Q14494
PhosphoSitePlusⁱ	Q14494

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000082641 Expressed in 244 organ(s), highest expression level in deltoid
CleanExⁱ	HS_NFE2L1 HS_NRF1
ExpressionAtlasⁱ	Q14494 baseline and differential
Genevisibleⁱ	Q14494 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA063384 HPA065424

HPAⁱ

HPA063384
HPA065424

Interactionⁱ

Subunit structureⁱ

Interacts with KEAP1 (PubMed:16687406). Endoplasmic reticulum membrane sensor NFE2L1: Interacts (via CPD region) with FBXW7; leading to its ubiquitination and degradation (By similarity). Endoplasmic reticulum membrane sensor NFE2L1: Interacts with SYVN1/HRD1; leading to its ubiquitination and degradation (By similarity). Endoplasmic reticulum membrane sensor NFE2L1: Interacts (when ubiquitinated) with DDI2; leading to its cleavage (By similarity). Transcription factor NRF1: Interacts (via the bZIP domain) with small MAF protein (MAFF, MAFG or MAFK); required for binding to antioxidant response elements (AREs) on DNA (PubMed:8932385, PubMed:9421508). Transcription factor NRF1: Interacts (via Destruction motif) with BTRC; leading to its ubiquitination and degradation (By similarity). Transcription factor NRF1: Interacts with CEBPB; the heterodimer represses expression of DSPP during odontoblast differentiation (PubMed:15308669).By similarity4 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
CREBZF	Q9NS37	2	EBI-2804436,EBI-632965
MAFG	O15525	2	EBI-2804436,EBI-713514

GO - Molecular functionⁱ

protein domain specific binding Source: Ensembl
protein heterodimerization activity
Source: UniProtKB
Inferred from physical interactionⁱ
- 8932385
- 9421508

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	110851, 22 interactors
ELMⁱ	Q14494
IntActⁱ	Q14494, 21 interactors
STRINGⁱ	9606.ENSP00000354855

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q14494
SMRⁱ	Q14494
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	654 – 717	bZIPPROSITE-ProRule annotationAdd BLAST		64

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	191 – 199	Cholesterol recognition/amino acid consensus (CRAC) regionBy similarity	9
Regionⁱ	379 – 383	CPDBy similarity	5
Regionⁱ	656 – 675	Basic motifPROSITE-ProRule annotationAdd BLAST	20
Regionⁱ	682 – 696	Leucine-zipperPROSITE-ProRule annotationAdd BLAST	15

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	476 – 480	Destruction motifBy similarity		5

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	125 – 288	Asp/Glu-rich (acidic)Add BLAST		164
Compositional biasⁱ	496 – 517	Poly-SerAdd BLAST		22

Domainⁱ

The cholesterol recognition/amino acid consensus (CRAC) region directly binds cholesterol, as well as campesterol and 27-hydroxycholesterol. Has much lower affinity for epicholesterol.By similarity

Sequence similaritiesⁱ

Belongs to the bZIP family. CNC subfamily.Curated

Keywords - Domainⁱ

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	KOG3863 Eukaryota ENOG410ZGMS LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00930000150911
HOGENOMⁱ	HOG000234410
HOVERGENⁱ	HBG052609
InParanoidⁱ	Q14494
KEGG Orthology (KO) More...KOⁱ	K09040
OMAⁱ	HKHSGPS
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G02EB
PhylomeDBⁱ	Q14494
TreeFamⁱ	TF326681

Family and domain databases

InterProⁱ	View protein in InterPro IPR004827 bZIP IPR004826 bZIP_Maf IPR029847 Nrf1_NFE2L1 IPR008917 TF_DNA-bd_sf
PANTHERⁱ	PTHR24411:SF31 PTHR24411:SF31, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF03131 bZIP_Maf, 1 hit
SMARTⁱ	View protein in SMART SM00338 BRLZ, 1 hit
SUPFAMⁱ	SSF47454 SSF47454, 1 hit
PROSITEⁱ	View protein in PROSITE PS50217 BZIP, 1 hit PS00036 BZIP_BASIC, 1 hit

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 2 described isoforms and 15 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: Q14494-1) [UniParc]FASTA Add to basket

Also known as: TCF111 Publication

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLSLKKYLTE GLLQFTILLS LIGVRVDVDT YLTSQLPPLR EIILGPSSAY 
        60         70         80         90        100
TQTQFHNLRN TLDGYGIHPK SIDLDNYFTA RRLLSQVRAL DRFQVPTTEV 
       110        120        130        140        150
NAWLVHRDPE GSVSGSQPNS GLALESSSGL QDVTGPDNGV RESETEQGFG 
       160        170        180        190        200
EDLEDLGAVA PPVSGDLTKE DIDLIDILWR QDIDLGAGRE VFDYSHRQKE 
       210        220        230        240        250
QDVEKELRDG GEQDTWAGEG AEALARNLLV DGETGESFPA QVPSGEDQTA 
       260        270        280        290        300
LSLEECLRLL EATCPFGENA EFPADISSIT EAVPSESEPP ALQNNLLSPL 
       310        320        330        340        350
LTGTESPFDL EQQWQDLMSI MEMQAMEVNT SASEILYSAP PGDPLSTNYS 
       360        370        380        390        400
LAPNTPINQN VSLHQASLGG CSQDFLLFSP EVESLPVASS STLLPLAPSN 
       410        420        430        440        450
STSLNSTFGS TNLTGLFFPP QLNGTANDTA GPELPDPLGG LLDEAMLDEI 
       460        470        480        490        500
SLMDLAIEEG FNPVQASQLE EEFDSDSGLS LDSSHSPSSL SSSEGSSSSS 
       510        520        530        540        550
SSSSSSSSSA SSSASSSFSE EGAVGYSSDS ETLDLEEAEG AVGYQPEYSK 
       560        570        580        590        600
FCRMSYQDPA QLSCLPYLEH VGHNHTYNMA PSALDSADLP PPSALKKGSK 
       610        620        630        640        650
EKQADFLDKQ MSRDEHRARA MKIPFTNDKI INLPVEEFNE LLSKYQLSEA 
       660        670        680        690        700
QLSLIRDIRR RGKNKMAAQN CRKRKLDTIL NLERDVEDLQ RDKARLLREK 
       710        720        730        740        750
VEFLRSLRQM KQKVQSLYQE VFGRLRDENG RPYSPSQYAL QYAGDGSVLL 
       760        770 
IPRTMADQQA RRQERKPKDR RK

Length:772

Mass (Da):84,704

Last modified:November 1, 1996 - v1

Checksum:ⁱC868807C6046BEF5

GO

Isoform 2 (identifier: Q14494-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
242-271: Missing.

« Hide

        10         20         30         40         50
MLSLKKYLTE GLLQFTILLS LIGVRVDVDT YLTSQLPPLR EIILGPSSAY 
        60         70         80         90        100
TQTQFHNLRN TLDGYGIHPK SIDLDNYFTA RRLLSQVRAL DRFQVPTTEV 
       110        120        130        140        150
NAWLVHRDPE GSVSGSQPNS GLALESSSGL QDVTGPDNGV RESETEQGFG 
       160        170        180        190        200
EDLEDLGAVA PPVSGDLTKE DIDLIDILWR QDIDLGAGRE VFDYSHRQKE 
       210        220        230        240        250
QDVEKELRDG GEQDTWAGEG AEALARNLLV DGETGESFPA QFPADISSIT 
       260        270        280        290        300
EAVPSESEPP ALQNNLLSPL LTGTESPFDL EQQWQDLMSI MEMQAMEVNT 
       310        320        330        340        350
SASEILYSAP PGDPLSTNYS LAPNTPINQN VSLHQASLGG CSQDFLLFSP 
       360        370        380        390        400
EVESLPVASS STLLPLAPSN STSLNSTFGS TNLTGLFFPP QLNGTANDTA 
       410        420        430        440        450
GPELPDPLGG LLDEAMLDEI SLMDLAIEEG FNPVQASQLE EEFDSDSGLS 
       460        470        480        490        500
LDSSHSPSSL SSSEGSSSSS SSSSSSSSSA SSSASSSFSE EGAVGYSSDS 
       510        520        530        540        550
ETLDLEEAEG AVGYQPEYSK FCRMSYQDPA QLSCLPYLEH VGHNHTYNMA 
       560        570        580        590        600
PSALDSADLP PPSALKKGSK EKQADFLDKQ MSRDEHRARA MKIPFTNDKI 
       610        620        630        640        650
INLPVEEFNE LLSKYQLSEA QLSLIRDIRR RGKNKMAAQN CRKRKLDTIL 
       660        670        680        690        700
NLERDVEDLQ RDKARLLREK VEFLRSLRQM KQKVQSLYQE VFGRLRDENG 
       710        720        730        740 
RPYSPSQYAL QYAGDGSVLL IPRTMADQQA RRQERKPKDR RK

Show »

Length:742

Mass (Da):81,499

Checksum:ⁱB99AAEF1C5F598E6

GO

Computationally mapped potential isoform sequencesⁱ

There are 15 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name	Protein names	Gene names	Length	Annotation

	J9JIE5	J9JIE5_HUMAN	Endoplasmic reticulum membrane sens... Endoplasmic reticulum membrane sensor NFE2L1	NFE2L1	761	Annotation score:
	B4DYE1	B4DYE1_HUMAN	Endoplasmic reticulum membrane sens... Endoplasmic reticulum membrane sensor NFE2L1 (cDNA FLJ53241, highly similar to Nuclear factor erythroid 2-related factor 1)	NFE2L1	584	Annotation score:
	F5H1B7	F5H1B7_HUMAN	Endoplasmic reticulum membrane sens... Endoplasmic reticulum membrane sensor NFE2L1	NFE2L1	616	Annotation score:
	J3QKY3	J3QKY3_HUMAN	Endoplasmic reticulum membrane sens... Endoplasmic reticulum membrane sensor NFE2L1	NFE2L1	573	Annotation score:
	J3QQQ1	J3QQQ1_HUMAN	Endoplasmic reticulum membrane sens... Endoplasmic reticulum membrane sensor NFE2L1	NFE2L1	161	Annotation score:
	J3KRF3	J3KRF3_HUMAN	Endoplasmic reticulum membrane sens... Endoplasmic reticulum membrane sensor NFE2L1	NFE2L1	133	Annotation score:
	J3QQY8	J3QQY8_HUMAN	Endoplasmic reticulum membrane sens... Endoplasmic reticulum membrane sensor NFE2L1	NFE2L1	99	Annotation score:
	J3QRG7	J3QRG7_HUMAN	Endoplasmic reticulum membrane sens... Endoplasmic reticulum membrane sensor NFE2L1	NFE2L1	111	Annotation score:
	J3QLQ1	J3QLQ1_HUMAN	Endoplasmic reticulum membrane sens... Endoplasmic reticulum membrane sensor NFE2L1	NFE2L1	82	Annotation score:
	J3KSR3	J3KSR3_HUMAN	Endoplasmic reticulum membrane sens... Endoplasmic reticulum membrane sensor NFE2L1	NFE2L1	62	Annotation score:
There are more potential isoformsShow all

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_048440	63	D → H. Corresponds to variant dbSNP:rs2229367Ensembl.		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_000579	242 – 271	Missing in isoform 2. 2 PublicationsAdd BLAST		30

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	L24123 mRNA No translation available. X77366 mRNA Translation: CAA54555.1 CH471109 Genomic DNA Translation: EAW94762.1 CH471109 Genomic DNA Translation: EAW94763.1 CH471109 Genomic DNA Translation: EAW94764.1 CH471109 Genomic DNA Translation: EAW94765.1 CH471109 Genomic DNA Translation: EAW94766.1 CH471109 Genomic DNA Translation: EAW94767.1 BC010623 mRNA Translation: AAH10623.1 U08853 mRNA Translation: AAA20466.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS11524.1 [Q14494-1] CCDS82150.1 [Q14494-2]
PIRⁱ	A49672 A55004
NCBI Reference Sequences More...RefSeqⁱ	NP_001317191.1, NM_001330262.1 [Q14494-2] NP_003195.1, NM_003204.2 [Q14494-1] XP_005257467.1, XM_005257410.3 [Q14494-1] XP_005257469.1, XM_005257412.3 [Q14494-2]
UniGeneⁱ	Hs.514284

Genome annotation databases

Ensemblⁱ	ENST00000357480; ENSP00000350072; ENSG00000082641 [Q14494-2] ENST00000362042; ENSP00000354855; ENSG00000082641 [Q14494-1] ENST00000585291; ENSP00000461960; ENSG00000082641 [Q14494-2]
GeneIDⁱ	4779
KEGGⁱ	hsa:4779
UCSC genome browser More...UCSCⁱ	uc002imz.5 human [Q14494-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q14494	FLJ00380 protein (Fragment)		HUMAN		791	UniRef100_Q14494
NFE2L1 isoform 4		PONAB		772
Uncharacterized protein		PANPA		772
NFE2L1 isoform 11 (Fragment)		PANTR		47
Endoplasmic reticulum membrane sensor NFE2L1 (Fragment)		HUMAN		47
+6
Q14494-2	NFE2L1 isoform 2		PONAB		742	UniRef100_A0A2J8W9B4
Uncharacterized protein		PANPA		742

Protein	Similar proteins		Species	Score	Length	Source
Q14494	Endoplasmic reticulum membrane sensor NFE2L1		PONAB		772	UniRef90_Q14494
FLJ00380 protein (Fragment)		HUMAN		791
Uncharacterized protein		PANPA		772
NFE2L1 isoform 11 (Fragment)		PANTR		47
Uncharacterized protein		FELCA		863
+104
Q14494-2	Endoplasmic reticulum membrane sensor NFE2L1		MOUSE		741	UniRef90_Q61985
Uncharacterized protein		FELCA		833
Uncharacterized protein		NOMLE		757
Putative bzip transcription factor nrf1 (Fragment)		DESRO		755
nuclear factor erythroid 2-related factor 1 isoform X3		NEOSC		748
+96

Protein	Similar proteins		Species	Score	Length	Source
Q14494	Endoplasmic reticulum membrane sensor NFE2L1		PONAB		772	UniRef50_Q14494
Endoplasmic reticulum membrane sensor NFE2L1		CHICK		772
FLJ00380 protein (Fragment)		HUMAN		791
Uncharacterized protein		PANPA		772
NFE2L1 isoform 11 (Fragment)		PANTR		47
+252
Q14494-2	Endoplasmic reticulum membrane sensor NFE2L1		MOUSE		741	UniRef50_Q61985
Uncharacterized protein		FELCA		833
Uncharacterized protein		NOMLE		757
Putative bzip transcription factor nrf1 (Fragment)		DESRO		755
nuclear factor erythroid 2-related factor 1 isoform X2		LEPWE		748
+171

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	L24123 mRNA No translation available. X77366 mRNA Translation: CAA54555.1 CH471109 Genomic DNA Translation: EAW94762.1 CH471109 Genomic DNA Translation: EAW94763.1 CH471109 Genomic DNA Translation: EAW94764.1 CH471109 Genomic DNA Translation: EAW94765.1 CH471109 Genomic DNA Translation: EAW94766.1 CH471109 Genomic DNA Translation: EAW94767.1 BC010623 mRNA Translation: AAH10623.1 U08853 mRNA Translation: AAA20466.1
CCDSⁱ	CCDS11524.1 [Q14494-1] CCDS82150.1 [Q14494-2]
PIRⁱ	A49672 A55004
RefSeqⁱ	NP_001317191.1, NM_001330262.1 [Q14494-2] NP_003195.1, NM_003204.2 [Q14494-1] XP_005257467.1, XM_005257410.3 [Q14494-1] XP_005257469.1, XM_005257412.3 [Q14494-2]
UniGeneⁱ	Hs.514284

3D structure databases

ProteinModelPortalⁱ	Q14494
SMRⁱ	Q14494
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	110851, 22 interactors
ELMⁱ	Q14494
IntActⁱ	Q14494, 21 interactors
STRINGⁱ	9606.ENSP00000354855

Chemistry databases

DrugBankⁱ	DB04147 Lauryl Dimethylamine-N-Oxide

DrugBankⁱ

DB04147 Lauryl Dimethylamine-N-Oxide

PTM databases

iPTMnetⁱ	Q14494
PhosphoSitePlusⁱ	Q14494

Polymorphism and mutation databases

BioMutaⁱ	NFE2L1
DMDMⁱ	3183180

Proteomic databases

EPDⁱ	Q14494
MaxQBⁱ	Q14494
PaxDbⁱ	Q14494
PeptideAtlasⁱ	Q14494
PRIDEⁱ	Q14494
ProteomicsDBⁱ	60003 60004 [Q14494-2]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	4779
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000357480; ENSP00000350072; ENSG00000082641 [Q14494-2] ENST00000362042; ENSP00000354855; ENSG00000082641 [Q14494-1] ENST00000585291; ENSP00000461960; ENSG00000082641 [Q14494-2]
GeneIDⁱ	4779
KEGGⁱ	hsa:4779
UCSCⁱ	uc002imz.5 human [Q14494-1]

Organism-specific databases

CTDⁱ	4779
DisGeNETⁱ	4779
EuPathDBⁱ	HostDB:ENSG00000082641.15
GeneCardsⁱ	NFE2L1
HGNCⁱ	HGNC:7781 NFE2L1
HPAⁱ	HPA063384 HPA065424
MIMⁱ	163260 gene
neXtProtⁱ	NX_Q14494
OpenTargetsⁱ	ENSG00000082641
PharmGKBⁱ	PA31587
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG3863 Eukaryota ENOG410ZGMS LUCA
GeneTreeⁱ	ENSGT00930000150911
HOGENOMⁱ	HOG000234410
HOVERGENⁱ	HBG052609
InParanoidⁱ	Q14494
KOⁱ	K09040
OMAⁱ	HKHSGPS
OrthoDBⁱ	EOG091G02EB
PhylomeDBⁱ	Q14494
TreeFamⁱ	TF326681

Enzyme and pathway databases

SignaLinkⁱ	Q14494
SIGNORⁱ	Q14494

Miscellaneous databases

ChiTaRSⁱ	NFE2L1 human
GeneWikiⁱ	NFE2L1
GenomeRNAiⁱ	4779
Protein Ontology More...PROⁱ	PR:Q14494
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000082641 Expressed in 244 organ(s), highest expression level in deltoid
CleanExⁱ	HS_NFE2L1 HS_NRF1
ExpressionAtlasⁱ	Q14494 baseline and differential
Genevisibleⁱ	Q14494 HS

Family and domain databases

InterProⁱ	View protein in InterPro IPR004827 bZIP IPR004826 bZIP_Maf IPR029847 Nrf1_NFE2L1 IPR008917 TF_DNA-bd_sf
PANTHERⁱ	PTHR24411:SF31 PTHR24411:SF31, 1 hit
Pfamⁱ	View protein in Pfam PF03131 bZIP_Maf, 1 hit
SMARTⁱ	View protein in SMART SM00338 BRLZ, 1 hit
SUPFAMⁱ	SSF47454 SSF47454, 1 hit
PROSITEⁱ	View protein in PROSITE PS50217 BZIP, 1 hit PS00036 BZIP_BASIC, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	NF2L1_HUMAN
Accessionⁱ	Q14494Primary (citable) accession number: Q14494 Secondary accession number(s): D3DTU3 , D3DTU5, Q12877, Q96FN6
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
	Last sequence update:	November 1, 1996
	Last modified:	November 7, 2018
	This is version 178 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
Human chromosome 17
Human chromosome 17: entries, gene names and cross-references to MIM

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UniProtKB - Q14494 (NF2L1_HUMAN)

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Endoplasmic reticulum membrane sensor NFE2L1

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<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

Caution

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GO - Biological processi

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<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

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<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

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Keywords - PTMi

Proteomic databases

PTM 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

Organism-specific 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

GO - Molecular functioni

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<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

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<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

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Sequence databases

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Keywords - Coding sequence diversityi

<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

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Chemistry databases

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Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

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Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ