UniProtKB - Q61985 (NF2L1_MOUSE)
Endoplasmic reticulum membrane sensor NFE2L1
Nfe2l1
Functioni
Endoplasmic reticulum membrane sensor that translocates into the nucleus in response to various stresses to act as a transcription factor (PubMed:20385086, PubMed:21536885, PubMed:23816881, PubMed:29149604).
Constitutes a precursor of the transcription factor NRF1. Able to detect various cellular stresses, such as cholesterol excess, oxidative stress or proteasome inhibition (PubMed:20385086, PubMed:21536885, PubMed:23816881, PubMed:29149604).
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 (PubMed:29149604).
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 (PubMed:29149604).
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:20385086, PubMed:21536885, PubMed:23816881).
4 PublicationsCNC-type bZIP family transcription factor that translocates to the nucleus and regulates expression of target genes in response to various stresses (PubMed:10601325, PubMed:11342101, PubMed:23144760, PubMed:16872277, PubMed:21911472, PubMed:23816881, PubMed:29149604).
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:12808106, PubMed:15738389, PubMed:23144760, PubMed:16872277, PubMed:21911472, PubMed:23816881).
Activates or represses expression of target genes, depending on the context (PubMed:12808106, PubMed:15738389, PubMed:23144760, PubMed:16872277, PubMed:21911472, PubMed:23816881).
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 (PubMed:29149604).
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 (PubMed:29149604).
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 (PubMed:10601325, PubMed:11342101, PubMed:12968018, PubMed:15738389, PubMed:18826952).
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 (PubMed:9501099, PubMed:12808106, PubMed:15738389, PubMed:18826952, PubMed:22586274).
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:20385086, PubMed:21536885, PubMed:23816881).
Also involved in regulating glucose flux (PubMed:25041126).
Together with CEBPB; represses expression of DSPP during odontoblast differentiation (By similarity).
In response to ascorbic acid induction, activates expression of SP7/Osterix in osteoblasts (PubMed:17510056).
By similarity17 PublicationsTranscription factor that binds the antioxidant response elements (ARE) consensus sequence on promoters and activates their expression.
2 PublicationsTranscription factor that binds the extended kappa 3 site of the TNF-alpha promoter after Fc gamma RIII stimulation and participates in the induction of this cytokine (PubMed:9580677).
1 PublicationCaution
GO - Molecular functioni
- cholesterol binding Source: UniProtKB
- chromatin binding Source: MGI
- DNA-binding transcription activator activity, RNA polymerase II-specific Source: NTNU_SB
- DNA-binding transcription factor activity, RNA polymerase II-specific Source: GO_Central
- DNA-binding transcription repressor activity, RNA polymerase II-specific Source: UniProtKB
- identical protein binding Source: MGI
- promoter-specific chromatin binding Source: MGI
- protein-containing complex binding Source: CAFA
- protein domain specific binding Source: CAFA
- protein heterodimerization activity Source: MGI
- RNA polymerase II cis-regulatory region sequence-specific DNA binding Source: NTNU_SB
GO - Biological processi
- cell redox homeostasis Source: UniProtKB
- cellular homeostasis Source: MGI
- cellular response to cholesterol Source: UniProtKB
- cellular response to cold Source: MGI
- cellular response to copper ion Source: MGI
- cellular response to oxidative stress Source: UniProtKB
- cholesterol homeostasis Source: UniProtKB
- cholesterol metabolic process Source: UniProtKB-KW
- cysteine transport Source: MGI
- erythrocyte differentiation Source: MGI
- fructose 6-phosphate metabolic process Source: MGI
- glial cell fate commitment Source: MGI
- glucose 6-phosphate metabolic process Source: MGI
- glutathione metabolic process Source: MGI
- 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 by RNA polymerase II Source: NTNU_SB
- positive regulation of transcription from RNA polymerase II promoter in response to stress Source: UniProtKB
- protein polyubiquitination Source: MGI
- regulation of fatty acid metabolic process Source: MGI
- regulation of gene expression Source: MGI
- regulation of glucose metabolic process Source: MGI
- regulation of inflammatory response Source: MGI
- regulation of lipid metabolic process Source: MGI
- regulation of mitotic nuclear division Source: MGI
- regulation of nucleus organization Source: MGI
- regulation of odontoblast differentiation Source: UniProtKB
- regulation of proteasomal protein catabolic process Source: MGI
- regulation of response to endoplasmic reticulum stress Source: MGI
- regulation of transcription by RNA polymerase II Source: MGI
- response to endoplasmic reticulum stress Source: MGI
- spinal cord motor neuron differentiation Source: MGI
Keywordsi
Molecular function | Activator, DNA-binding, Repressor |
Biological process | Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism, Transcription, Transcription regulation |
Ligand | Lipid-binding |
Names & Taxonomyi
Protein namesi | Recommended name: Endoplasmic reticulum membrane sensor NFE2L1CuratedAlternative name(s): Locus control region-factor 11 Publication Short name: LCR-F11 Publication Nuclear factor erythroid 2-related factor 1Curated Short name: NF-E2-related factor 11 Publication Short name: NFE2-related factor 11 Publication Nuclear factor, erythroid derived 2, like 1 Cleaved into the following chain: Transcription factor NRF1Curated |
Gene namesi | |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:99421, Nfe2l1 |
VEuPathDBi | HostDB:ENSMUSG00000038615 |
Subcellular locationi
Endoplasmic reticulum
- Endoplasmic reticulum membrane 6 Publications; Single-pass type II membrane protein By similarity
- Endoplasmic reticulum membrane 6 Publications; Single-pass type III membrane protein By similarity
Note: In normal conditions, probably has a single-pass type II membrane protein topology, with the DNA-binding domain facing the endoplasmic reticulum lumen (By similarity). 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 (By similarity). Retrotranslocated proteins are normally rapidly degraded by the proteasome and active species do not accumulate (By similarity). 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 (By similarity).By similarity
Nucleus
- Nucleus PROSITE-ProRule annotation3 Publications
Note: Translocates into the nucleus following cleavage of Endoplasmic reticulum membrane sensor NFE2L1 by aspartyl protease DDI2.1 Publication
Cytosol
- cytosol Source: MGI
Endoplasmic reticulum
- endoplasmic reticulum Source: MGI
- endoplasmic reticulum membrane Source: MGI
- integral component of endoplasmic reticulum membrane Source: UniProtKB
Nucleus
- nucleoplasm Source: MGI
- nucleus Source: UniProtKB
- RNA polymerase II transcription regulator complex Source: MGI
Other locations
- protein-containing complex Source: CAFA
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
Cytoplasm, Endoplasmic reticulum, Membrane, NucleusPathology & Biotechi
Disruption phenotypei
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 350 – 354 | Missing : Abolishes interaction with FBXW7. 1 Publication | 5 | |
Mutagenesisi | 448 – 451 | SGLS → AGLA: Abolishes ubiquitination and degradation by the SCF(BTRC) complex. 1 Publication | 4 | |
Mutagenesisi | 496 | S → A: Does not affect phosphorylation by CK2. 1 Publication | 1 | |
Mutagenesisi | 497 | S → A: Abolishes phosphorylation by CK2. 1 Publication | 1 | |
Mutagenesisi | 499 | S → A: Does not affect phosphorylation by CK2. 1 Publication | 1 | |
Mutagenesisi | 501 | T → A: Does not affect phosphorylation by CK2. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000076448 | 1 – 741 | Endoplasmic reticulum membrane sensor NFE2L1Add BLAST | 741 | |
ChainiPRO_0000443104 | 104 – 741 | Transcription factor NRF1By similarityAdd BLAST | 638 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 319 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 331 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 394 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 497 | Phosphoserine; by CK21 Publication | 1 | |
Modified residuei | 568 | PhosphoserineBy similarity | 1 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 103 – 104 | Cleavage; by DDI2By similarity | 2 |
Keywords - PTMi
Glycoprotein, Phosphoprotein, Ubl conjugationProteomic databases
MaxQBi | Q61985 |
PaxDbi | Q61985 |
PRIDEi | Q61985 |
ProteomicsDBi | 287393 [Q61985-1] 287394 [Q61985-3] 287395 [Q61985-2] |
PTM databases
GlyGeni | Q61985, 3 sites |
iPTMneti | Q61985 |
PhosphoSitePlusi | Q61985 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSMUSG00000038615, Expressed in muscle tissue and 339 other tissues |
ExpressionAtlasi | Q61985, baseline and differential |
Genevisiblei | Q61985, MM |
Interactioni
Subunit structurei
Interacts with KEAP1.
By similarityInteracts (via CPD region) with FBXW7; leading to its ubiquitination and degradation (PubMed:21953459).
Interacts with SYVN1/HRD1; leading to its ubiquitination and degradation (PubMed:21911472).
Interacts (when ubiquitinated) with DDI2; leading to its cleavage (By similarity).
By similarity2 PublicationsInteracts (via the bZIP domain) with small MAF protein (MAFF, MAFG or MAFK); required for binding to antioxidant response elements (AREs) on DNA (PubMed:11342101, PubMed:18990090, PubMed:23144760).
Interacts (via Destruction motif) with BTRC; leading to its ubiquitination and degradation (PubMed:21911472).
Interacts with CEBPB; the heterodimer represses expression of DSPP during odontoblast differentiation (By similarity).
Interacts with MOTS-c, a peptide produced by the mitochondrially encoded 12S rRNA MT-RNR1 (By similarity).
By similarity4 PublicationsGO - Molecular functioni
- identical protein binding Source: MGI
- protein domain specific binding Source: CAFA
- protein heterodimerization activity Source: MGI
Protein-protein interaction databases
STRINGi | 10090.ENSMUSP00000103286 |
Miscellaneous databases
RNActi | Q61985, protein |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 623 – 686 | bZIPPROSITE-ProRule annotationAdd BLAST | 64 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 108 – 148 | DisorderedSequence analysisAdd BLAST | 41 | |
Regioni | 191 – 199 | Cholesterol recognition/amino acid consensus (CRAC) region1 Publication | 9 | |
Regioni | 198 – 220 | DisorderedSequence analysisAdd BLAST | 23 | |
Regioni | 350 – 354 | CPD1 Publication | 5 | |
Regioni | 441 – 501 | DisorderedSequence analysisAdd BLAST | 61 | |
Regioni | 551 – 582 | DisorderedSequence analysisAdd BLAST | 32 | |
Regioni | 625 – 644 | Basic motifPROSITE-ProRule annotationAdd BLAST | 20 | |
Regioni | 651 – 665 | Leucine-zipperPROSITE-ProRule annotationAdd BLAST | 15 | |
Regioni | 722 – 741 | DisorderedSequence analysisAdd BLAST | 20 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 447 – 451 | Destruction motif1 Publication | 5 | |
Motifi | 730 – 737 | Nuclear localization signalSequence analysis | 8 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 112 – 141 | Polar residuesSequence analysisAdd BLAST | 30 | |
Compositional biasi | 441 – 495 | Polar residuesSequence analysisAdd BLAST | 55 | |
Compositional biasi | 567 – 582 | Basic and acidic residuesSequence analysisAdd BLAST | 16 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Signal-anchor, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG3863, Eukaryota |
GeneTreei | ENSGT00950000182892 |
HOGENOMi | CLU_024173_1_0_1 |
InParanoidi | Q61985 |
OMAi | LQAMDVN |
Family and domain databases
InterProi | View protein in InterPro IPR004827, bZIP IPR004826, bZIP_Maf IPR029847, 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 |
s (3+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 3 produced by isoformsialternative promoter usage and alternative splicing. AlignAdd to basketThis entry has 3 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
QDVDKELQDG REREDTWSGE GAEALARDLL VDGETGESFP AQFPADVSSI
260 270 280 290 300
PEAVPSESES PALQNSLLSP LLTGTESPFD LEQQWQDLMS IMEMQAMEVN
310 320 330 340 350
TSASEILYNA PPGDPLSTNY SLAPNTPINQ NVSLHQASLG GCSQDFSLFS
360 370 380 390 400
PEVESLPVAS SSTLLPLVPS NSTSLNSTFG STNLAGLFFP SQLNGTANDT
410 420 430 440 450
SGPELPDPLG GLLDEAMLDE ISLMDLAIEE GFNPVQASQL EEEFDSDSGL
460 470 480 490 500
SLDSSHSPSS LSSSEGSSSS SSSSSSSSAS SSASSSFSEE GAVGYSSDSE
510 520 530 540 550
TLDLEEAEGA VGYQPEYSKF CRMSYQDPSQ LSCLPYLEHV GHNHTYNMAP
560 570 580 590 600
SALDSADLPP PSTLKKGSKE KQADFLDKQM SRDEHRARAM KIPFTNDKII
610 620 630 640 650
NLPVEEFNEL LSKYQLSEAQ LSLIRDIRRR GKNKMAAQNC RKRKLDTILN
660 670 680 690 700
LERDVEDLQR DKARLLREKV EFLRSLRQMK QKVQSLYQEV FGRLRDEHGR
710 720 730 740
PYSPSQYALQ YAGDGSVLLI PRTMADQQAR RQERKPKDRR K
Computationally mapped potential isoform sequencesi
There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA2A6D2 | A2A6D2_MOUSE | Endoplasmic reticulum membrane sens... | Nfe2l1 | 742 | Annotation score: | ||
Q3V3M1 | Q3V3M1_MOUSE | Endoplasmic reticulum membrane sens... | Nfe2l1 | 453 | Annotation score: | ||
A2A6D1 | A2A6D1_MOUSE | Endoplasmic reticulum membrane sens... | Nfe2l1 | 152 | Annotation score: | ||
A2A6D0 | A2A6D0_MOUSE | Endoplasmic reticulum membrane sens... | Nfe2l1 | 148 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 318 | T → S in CAA55362 (PubMed:7759107).Curated | 1 | |
Sequence conflicti | 387 | L → P in CAA55362 (PubMed:7759107).Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_000580 | 1 – 158 | Missing in isoform 2 and isoform 3. CuratedAdd BLAST | 158 | |
Alternative sequenceiVSP_046523 | 159 – 291 | Missing in isoform 3. CuratedAdd BLAST | 133 | |
Alternative sequenceiVSP_046524 | 159 – 170 | VAPPV…DLTKE → MGWESRLTAASA in isoform 2. CuratedAdd BLAST | 12 | |
Alternative sequenceiVSP_000581 | 447 – 583 | Missing in isoform 3. CuratedAdd BLAST | 137 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X78709 mRNA Translation: CAA55362.1 AF015881 Genomic DNA Translation: AAC40108.1 AL596384 Genomic DNA No translation available. |
CCDSi | CCDS25304.1 [Q61985-1] CCDS48894.1 [Q61985-3] |
PIRi | I48694 |
RefSeqi | NP_001123922.1, NM_001130450.1 [Q61985-1] NP_032712.2, NM_008686.3 [Q61985-1] |
Genome annotation databases
Ensembli | ENSMUST00000081775; ENSMUSP00000080467; ENSMUSG00000038615 [Q61985-1] ENSMUST00000107657; ENSMUSP00000103284; ENSMUSG00000038615 [Q61985-1] ENSMUST00000107658; ENSMUSP00000103285; ENSMUSG00000038615 [Q61985-1] ENSMUST00000167110; ENSMUSP00000127804; ENSMUSG00000038615 [Q61985-3] ENSMUST00000167149; ENSMUSP00000128527; ENSMUSG00000038615 [Q61985-1] |
GeneIDi | 18023 |
KEGGi | mmu:18023 |
UCSCi | uc007lcq.2, mouse [Q61985-1] uc011ydl.1, mouse [Q61985-3] |
Keywords - Coding sequence diversityi
Alternative promoter usage, Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X78709 mRNA Translation: CAA55362.1 AF015881 Genomic DNA Translation: AAC40108.1 AL596384 Genomic DNA No translation available. |
CCDSi | CCDS25304.1 [Q61985-1] CCDS48894.1 [Q61985-3] |
PIRi | I48694 |
RefSeqi | NP_001123922.1, NM_001130450.1 [Q61985-1] NP_032712.2, NM_008686.3 [Q61985-1] |
3D structure databases
AlphaFoldDBi | Q61985 |
SMRi | Q61985 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 10090.ENSMUSP00000103286 |
PTM databases
GlyGeni | Q61985, 3 sites |
iPTMneti | Q61985 |
PhosphoSitePlusi | Q61985 |
Proteomic databases
MaxQBi | Q61985 |
PaxDbi | Q61985 |
PRIDEi | Q61985 |
ProteomicsDBi | 287393 [Q61985-1] 287394 [Q61985-3] 287395 [Q61985-2] |
Protocols and materials databases
Antibodypediai | 30234, 248 antibodies from 32 providers |
DNASUi | 18023 |
Genome annotation databases
Ensembli | ENSMUST00000081775; ENSMUSP00000080467; ENSMUSG00000038615 [Q61985-1] ENSMUST00000107657; ENSMUSP00000103284; ENSMUSG00000038615 [Q61985-1] ENSMUST00000107658; ENSMUSP00000103285; ENSMUSG00000038615 [Q61985-1] ENSMUST00000167110; ENSMUSP00000127804; ENSMUSG00000038615 [Q61985-3] ENSMUST00000167149; ENSMUSP00000128527; ENSMUSG00000038615 [Q61985-1] |
GeneIDi | 18023 |
KEGGi | mmu:18023 |
UCSCi | uc007lcq.2, mouse [Q61985-1] uc011ydl.1, mouse [Q61985-3] |
Organism-specific databases
CTDi | 4779 |
MGIi | MGI:99421, Nfe2l1 |
VEuPathDBi | HostDB:ENSMUSG00000038615 |
Phylogenomic databases
eggNOGi | KOG3863, Eukaryota |
GeneTreei | ENSGT00950000182892 |
HOGENOMi | CLU_024173_1_0_1 |
InParanoidi | Q61985 |
OMAi | LQAMDVN |
Miscellaneous databases
BioGRID-ORCSi | 18023, 4 hits in 76 CRISPR screens |
ChiTaRSi | Nfe2l1, mouse |
PROi | PR:Q61985 |
RNActi | Q61985, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000038615, Expressed in muscle tissue and 339 other tissues |
ExpressionAtlasi | Q61985, baseline and differential |
Genevisiblei | Q61985, MM |
Family and domain databases
InterProi | View protein in InterPro IPR004827, bZIP IPR004826, bZIP_Maf IPR029847, 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 |
MobiDBi | Search... |
Entry informationi
Entry namei | NF2L1_MOUSE | |
Accessioni | Q61985Primary (citable) accession number: Q61985 Secondary accession number(s): E9Q038, O70234 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 30, 2000 |
Last sequence update: | May 29, 2013 | |
Last modified: | May 25, 2022 | |
This is version 177 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - SIMILARITY comments
Index of protein domains and families