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Nuclear factor erythroid 2-related factor 2 (NF-E2-related factor 2) (NFE2-related factor 2) (HEBP1) (Nuclear factor, erythroid derived 2, like 2)

 NF2L2_HUMAN             Reviewed;         605 AA.
Q16236; B2RBU2; B4E338; E9PGJ7; Q53RW6; Q59HH2; Q96F71;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
25-NOV-2002, sequence version 3.
12-SEP-2018, entry version 185.
RecName: Full=Nuclear factor erythroid 2-related factor 2;
Short=NF-E2-related factor 2;
Short=NFE2-related factor 2;
AltName: Full=HEBP1;
AltName: Full=Nuclear factor, erythroid derived 2, like 2;
Name=NFE2L2; Synonyms=NRF2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Tongue, and Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Myeloid leukemia cell;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-202 (ISOFORM 1).
TISSUE=Melanoma;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-605 (ISOFORM 1).
TISSUE=Fetal liver;
PubMed=7937919; DOI=10.1073/pnas.91.21.9926;
Moi P., Chan K., Asunis I., Cao A., Kan Y.W.;
"Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic
leucine zipper transcriptional activator that binds to the tandem NF-
E2/AP1 repeat of the beta-globin locus control region.";
Proc. Natl. Acad. Sci. U.S.A. 91:9926-9930(1994).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION BY PKC.
PubMed=11035812; DOI=10.1073/pnas.220418997;
Huang H.-C., Nguyen T., Pickett C.B.;
"Regulation of the antioxidant response element by protein kinase C-
mediated phosphorylation of NF-E2-related factor 2.";
Proc. Natl. Acad. Sci. U.S.A. 97:12475-12480(2000).
[9]
INTERACTION WITH PMF1.
PubMed=11256947; DOI=10.1042/0264-6021:3550045;
Wang Y., Devereux W., Stewart T.M., Casero R.A. Jr.;
"Characterization of the interaction between the transcription factors
human polyamine modulated factor (PMF-1) and NF-E2-related factor 2
(Nrf-2) in the transcriptional regulation of the spermidine/spermine
N1-acetyltransferase (SSAT) gene.";
Biochem. J. 355:45-49(2001).
[10]
UBIQUITINATION.
PubMed=15983046; DOI=10.1074/jbc.M501279200;
Zhang D.D., Lo S.C., Sun Z., Habib G.M., Lieberman M.W., Hannink M.;
"Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for
Cul3, targets Keap1 for degradation by a proteasome-independent
pathway.";
J. Biol. Chem. 280:30091-30099(2005).
[11]
INTERACTION WITH PGAM5 AND KEAP1.
PubMed=18387606; DOI=10.1016/j.yexcr.2008.02.014;
Lo S.-C., Hannink M.;
"PGAM5 tethers a ternary complex containing Keap1 and Nrf2 to
mitochondria.";
Exp. Cell Res. 314:1789-1803(2008).
[12]
DOWN-REGULATION BY ENC1.
PubMed=19424503; DOI=10.1371/journal.pone.0005492;
Wang X.J., Zhang D.D.;
"Ectodermal-neural cortex 1 down-regulates Nrf2 at the translational
level.";
PLoS ONE 4:E5492-E5492(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[14]
INTERACTION WITH EEF1D.
PubMed=21597468; DOI=10.1038/embor.2011.82;
Kaitsuka T., Tomizawa K., Matsushita M.;
"Transformation of eEF1Bdelta into heat-shock response transcription
factor by alternative splicing.";
EMBO Rep. 12:673-681(2011).
[15]
ACETYLATION AT LYS-596 AND LYS-599, DEACETYLATION BY SIRT1, AND
SUBCELLULAR LOCATION.
PubMed=21196497; DOI=10.1074/jbc.M110.208173;
Kawai Y., Garduno L., Theodore M., Yang J., Arinze I.J.;
"Acetylation-deacetylation of the transcription factor Nrf2 (nuclear
factor erythroid 2-related factor 2) regulates its transcriptional
activity and nucleocytoplasmic localization.";
J. Biol. Chem. 286:7629-7640(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
INTERACTION WITH HERPES VIRUS 8 PROTEIN LANA1 (MICROBIAL INFECTION),
AND SUBCELLULAR LOCATION.
PubMed=25995248; DOI=10.1128/JVI.00895-15;
Gjyshi O., Roy A., Dutta S., Veettil M.V., Dutta D., Chandran B.;
"Activated Nrf2 Interacts with Kaposi's Sarcoma-Associated Herpesvirus
Latency Protein LANA-1 and Host Protein KAP1 To Mediate Global Lytic
Gene Repression.";
J. Virol. 89:7874-7892(2015).
[18]
FUNCTION, INVOLVEMENT IN IMDDHH, VARIANTS IMDDHH ARG-31; LYS-79;
LYS-80 AND SER-81, AND CHARACTERIZATION OF VARIANT IMDDHH LYS-80.
PubMed=29018201; DOI=10.1038/s41467-017-00932-7;
Huppke P., Weissbach S., Church J.A., Schnur R., Krusen M.,
Dreha-Kulaczewski S., Kuehn-Velten W.N., Wolf A., Huppke B.,
Millan F., Begtrup A., Almusafri F., Thiele H., Altmueller J.,
Nuernberg P., Mueller M., Gaertner J.;
"Activating de novo mutations in NFE2L2 encoding NRF2 cause a
multisystem disorder.";
Nat. Commun. 8:818-818(2017).
[19]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 69-84 IN COMPLEX WITH KEAP1,
AND MUTAGENESIS OF THR-80.
PubMed=16888629; DOI=10.1038/sj.emboj.7601243;
Lo S.-C., Li X., Henzl M.T., Beamer L.J., Hannink M.;
"Structure of the Keap1:Nrf2 interface provides mechanistic insight
into Nrf2 signaling.";
EMBO J. 25:3605-3617(2006).
-!- FUNCTION: Transcription activator that binds to antioxidant
response (ARE) elements in the promoter regions of target genes.
Important for the coordinated up-regulation of genes in response
to oxidative stress and the regulation of cellular redox
conditions. May be involved in the transcriptional activation of
genes of the beta-globin cluster by mediating enhancer activity of
hypersensitive site 2 of the beta-globin locus control region.
{ECO:0000269|PubMed:11035812, ECO:0000269|PubMed:29018201}.
-!- SUBUNIT: Heterodimer. Forms a ternary complex with PGAM5 and
KEAP1. May bind DNA with an unknown protein. Interacts via its
leucine-zipper domain with the coiled-coil domain of PMF1.
Interacts with EEF1D at heat shock promoter elements (HSE).
Interacts (via the bZIP domain) with MAFK; required for binding to
antioxidant response (ARE) elements on DNA. Interacts with CHD6;
involved in activation of the transcription. Interacts with ESRRB;
represses NFE2L2 transcriptional activity (By similarity).
{ECO:0000250|UniProtKB:Q60795, ECO:0000269|PubMed:11256947,
ECO:0000269|PubMed:16888629, ECO:0000269|PubMed:18387606,
ECO:0000269|PubMed:21597468}.
-!- SUBUNIT: (Microbial infection) Interacts with herpes virus 8
protein LANA1. {ECO:0000269|PubMed:25995248}.
-!- INTERACTION:
P18848:ATF4; NbExp=4; IntAct=EBI-2007911, EBI-492498;
Q14145:KEAP1; NbExp=22; IntAct=EBI-2007911, EBI-751001;
O15525:MAFG; NbExp=5; IntAct=EBI-2007911, EBI-713514;
O60675:MAFK; NbExp=3; IntAct=EBI-2007911, EBI-2559512;
P10276:RARA; NbExp=2; IntAct=EBI-2007911, EBI-413374;
P13805:TNNT1; NbExp=3; IntAct=EBI-2007911, EBI-726527;
Q9BTA9:WAC; NbExp=3; IntAct=EBI-2007911, EBI-749118;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:11035812, ECO:0000269|PubMed:21196497}.
Nucleus {ECO:0000269|PubMed:11035812,
ECO:0000269|PubMed:21196497}. Note=Cytosolic under unstressed
conditions, translocates into the nucleus upon induction by
electrophilic agents. {ECO:0000269|PubMed:21196497}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q16236-1; Sequence=Displayed;
Name=2;
IsoId=Q16236-2; Sequence=VSP_025045;
Name=3;
IsoId=Q16236-3; Sequence=VSP_025045, VSP_046168;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed. Highest expression in adult
muscle, kidney, lung, liver and in fetal muscle.
-!- INDUCTION: Down-regulated by ENC1 via a proteasomal ubiquitin-
independent protein catabolic process.
-!- DOMAIN: Acidic activation domain in the N-terminus, and DNA
binding domain in the C-terminus.
-!- PTM: Phosphorylation of Ser-40 by PKC in response to oxidative
stress dissociates NFE2L2 from its cytoplasmic inhibitor KEAP1,
promoting its translocation into the nucleus.
{ECO:0000250|UniProtKB:O54968}.
-!- PTM: Acetylation at Lys-596 and Lys-599 increases nuclear
localization whereas deacetylation by SIRT1 enhances cytoplasmic
presence. {ECO:0000269|PubMed:21196497}.
-!- PTM: Ubiquitinated by the KEAP1-CUL3-RBX1 E3 ubiquitin ligase
complex and subject to proteasomal degradation. Ubiquitination is
inhibited by sulforaphane. {ECO:0000269|PubMed:15983046}.
-!- DISEASE: Immunodeficiency, developmental delay, and
hypohomocysteinemia (IMDDHH) [MIM:617744]: An early onset
multisystem disorder characterized by immunodeficiency, recurrent
infections, developmental delay, poor growth, intellectual
disability, and hypohomocysteinemia. Some patients manifest
congenital cardiac defects. IMDDHH inheritance pattern is
autosomal dominant. {ECO:0000269|PubMed:29018201}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the bZIP family. CNC subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB32188.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAD92023.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AK304555; BAG65350.1; -; mRNA.
EMBL; AK314816; BAG37339.1; -; mRNA.
EMBL; AB208786; BAD92023.1; ALT_INIT; mRNA.
EMBL; AC019080; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC079305; AAY14710.1; -; Genomic_DNA.
EMBL; CH471058; EAX11062.1; -; Genomic_DNA.
EMBL; BC011558; AAH11558.1; -; mRNA.
EMBL; AL135266; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; S74017; AAB32188.1; ALT_INIT; mRNA.
CCDS; CCDS42782.1; -. [Q16236-1]
CCDS; CCDS46457.1; -. [Q16236-2]
CCDS; CCDS46458.1; -. [Q16236-3]
RefSeq; NP_001138884.1; NM_001145412.3. [Q16236-2]
RefSeq; NP_001138885.1; NM_001145413.3. [Q16236-3]
RefSeq; NP_001300829.1; NM_001313900.1. [Q16236-2]
RefSeq; NP_001300830.1; NM_001313901.1. [Q16236-2]
RefSeq; NP_006155.2; NM_006164.4. [Q16236-1]
UniGene; Hs.744006; -.
PDB; 2FLU; X-ray; 1.50 A; P=69-84.
PDB; 2LZ1; NMR; -; A=445-523.
PDB; 3ZGC; X-ray; 2.20 A; C=76-82.
PDB; 4IFL; X-ray; 1.80 A; P=69-84.
PDBsum; 2FLU; -.
PDBsum; 2LZ1; -.
PDBsum; 3ZGC; -.
PDBsum; 4IFL; -.
ProteinModelPortal; Q16236; -.
SMR; Q16236; -.
BioGrid; 110852; 71.
CORUM; Q16236; -.
DIP; DIP-29971N; -.
ELM; Q16236; -.
IntAct; Q16236; 24.
MINT; Q16236; -.
STRING; 9606.ENSP00000380252; -.
BindingDB; Q16236; -.
ChEMBL; CHEMBL1075094; -.
iPTMnet; Q16236; -.
PhosphoSitePlus; Q16236; -.
BioMuta; NFE2L2; -.
DMDM; 25453452; -.
EPD; Q16236; -.
MaxQB; Q16236; -.
PaxDb; Q16236; -.
PeptideAtlas; Q16236; -.
PRIDE; Q16236; -.
ProteomicsDB; 60843; -.
ProteomicsDB; 60844; -. [Q16236-2]
DNASU; 4780; -.
Ensembl; ENST00000397062; ENSP00000380252; ENSG00000116044. [Q16236-1]
Ensembl; ENST00000397063; ENSP00000380253; ENSG00000116044. [Q16236-2]
Ensembl; ENST00000446151; ENSP00000411575; ENSG00000116044. [Q16236-3]
Ensembl; ENST00000464747; ENSP00000467401; ENSG00000116044. [Q16236-2]
GeneID; 4780; -.
KEGG; hsa:4780; -.
UCSC; uc002ulg.6; human. [Q16236-1]
CTD; 4780; -.
DisGeNET; 4780; -.
EuPathDB; HostDB:ENSG00000116044.15; -.
GeneCards; NFE2L2; -.
HGNC; HGNC:7782; NFE2L2.
HPA; CAB020317; -.
HPA; HPA002990; -.
HPA; HPA043438; -.
MalaCards; NFE2L2; -.
MIM; 600492; gene.
MIM; 617744; phenotype.
neXtProt; NX_Q16236; -.
OpenTargets; ENSG00000116044; -.
PharmGKB; PA31588; -.
eggNOG; ENOG410ISV3; Eukaryota.
eggNOG; ENOG41100FB; LUCA.
GeneTree; ENSGT00920000148991; -.
HOGENOM; HOG000234410; -.
HOVERGEN; HBG052609; -.
InParanoid; Q16236; -.
KO; K05638; -.
OMA; ALHIPFP; -.
OrthoDB; EOG091G02EB; -.
PhylomeDB; Q16236; -.
TreeFam; TF326681; -.
SignaLink; Q16236; -.
SIGNOR; Q16236; -.
ChiTaRS; NFE2L2; human.
EvolutionaryTrace; Q16236; -.
GeneWiki; NFE2L2; -.
GenomeRNAi; 4780; -.
PMAP-CutDB; Q16236; -.
PRO; PR:Q16236; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000116044; Expressed in 244 organ(s), highest expression level in epithelium of nasopharynx.
CleanEx; HS_NFE2L2; -.
ExpressionAtlas; Q16236; baseline and differential.
Genevisible; Q16236; HS.
GO; GO:0005813; C:centrosome; IDA:HPA.
GO; GO:0000785; C:chromatin; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0032993; C:protein-DNA complex; ISS:ParkinsonsUK-UCL.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:ParkinsonsUK-UCL.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IPI:BHF-UCL.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0001221; F:transcription cofactor binding; IEA:Ensembl.
GO; GO:0044212; F:transcription regulatory region DNA binding; TAS:ParkinsonsUK-UCL.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; TAS:ParkinsonsUK-UCL.
GO; GO:0001205; F:transcriptional activator activity, RNA polymerase II distal enhancer sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0046223; P:aflatoxin catabolic process; IEA:Ensembl.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0045454; P:cell redox homeostasis; IMP:UniProtKB.
GO; GO:1904385; P:cellular response to angiotensin; IEA:Ensembl.
GO; GO:0071498; P:cellular response to fluid shear stress; IDA:UniProtKB.
GO; GO:0042149; P:cellular response to glucose starvation; IEA:Ensembl.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IMP:BHF-UCL.
GO; GO:0071499; P:cellular response to laminar fluid shear stress; IMP:BHF-UCL.
GO; GO:0034599; P:cellular response to oxidative stress; TAS:ParkinsonsUK-UCL.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IMP:BHF-UCL.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISS:ParkinsonsUK-UCL.
GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IEA:Ensembl.
GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IMP:BHF-UCL.
GO; GO:1902037; P:negative regulation of hematopoietic stem cell differentiation; IEA:Ensembl.
GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; IGI:ParkinsonsUK-UCL.
GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IMP:BHF-UCL.
GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; IEA:Ensembl.
GO; GO:0036499; P:PERK-mediated unfolded protein response; ISS:ParkinsonsUK-UCL.
GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
GO; GO:0030194; P:positive regulation of blood coagulation; IEA:Ensembl.
GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IEA:Ensembl.
GO; GO:1903071; P:positive regulation of ER-associated ubiquitin-dependent protein catabolic process; TAS:ParkinsonsUK-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IGI:ParkinsonsUK-UCL.
GO; GO:0046326; P:positive regulation of glucose import; IEA:Ensembl.
GO; GO:1903788; P:positive regulation of glutathione biosynthetic process; IEA:Ensembl.
GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ParkinsonsUK-UCL.
GO; GO:0061419; P:positive regulation of transcription from RNA polymerase II promoter in response to hypoxia; IMP:BHF-UCL.
GO; GO:0036091; P:positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IEA:Ensembl.
GO; GO:0036003; P:positive regulation of transcription from RNA polymerase II promoter in response to stress; IMP:BHF-UCL.
GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IDA:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0045995; P:regulation of embryonic development; IEA:Ensembl.
GO; GO:2000121; P:regulation of removal of superoxide radicals; IEA:Ensembl.
GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR004827; bZIP.
InterPro; IPR004826; bZIP_Maf.
InterPro; IPR029845; Nrf2.
InterPro; IPR008917; TF_DNA-bd_sf.
PANTHER; PTHR24411:SF3; PTHR24411:SF3; 1.
Pfam; PF03131; bZIP_Maf; 1.
SMART; SM00338; BRLZ; 1.
SUPFAM; SSF47454; SSF47454; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Complete proteome; Cytoplasm; Disease mutation; DNA-binding;
Host-virus interaction; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 605 Nuclear factor erythroid 2-related factor
2.
/FTId=PRO_0000076449.
DOMAIN 497 560 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 499 518 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 522 529 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 591 596 Mediates interaction with CHD6 and is
necessary to activate transcription.
{ECO:0000250}.
MOD_RES 40 40 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:O54968}.
MOD_RES 215 215 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 596 596 N6-acetyllysine; by CREBBP.
{ECO:0000269|PubMed:21196497}.
MOD_RES 599 599 N6-acetyllysine; by CREBBP.
{ECO:0000269|PubMed:21196497}.
VAR_SEQ 1 16 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.2}.
/FTId=VSP_025045.
VAR_SEQ 135 141 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046168.
VARIANT 31 31 G -> R (in IMDDHH).
{ECO:0000269|PubMed:29018201}.
/FTId=VAR_080492.
VARIANT 43 43 R -> Q (in dbSNP:rs35248500).
/FTId=VAR_032110.
VARIANT 79 79 E -> K (in IMDDHH).
{ECO:0000269|PubMed:29018201}.
/FTId=VAR_080493.
VARIANT 80 80 T -> K (in IMDDHH; increased protein
abundance; increased positive regulation
of transcription of target genes; changed
cell redox homeostasis).
{ECO:0000269|PubMed:29018201}.
/FTId=VAR_080494.
VARIANT 81 81 G -> S (in IMDDHH).
{ECO:0000269|PubMed:29018201}.
/FTId=VAR_080495.
VARIANT 99 99 S -> P (in dbSNP:rs5031039).
/FTId=VAR_020322.
VARIANT 268 268 V -> M (in dbSNP:rs34154613).
/FTId=VAR_032111.
MUTAGEN 80 80 T->A: Loss of interaction with KEAP1.
{ECO:0000269|PubMed:16888629}.
CONFLICT 72 72 A -> T (in Ref. 7; AAB32188).
{ECO:0000305}.
CONFLICT 92 92 I -> T (in Ref. 7; AAB32188).
{ECO:0000305}.
CONFLICT 178 178 D -> Y (in Ref. 3; AL135266).
{ECO:0000305}.
CONFLICT 521 521 N -> D (in Ref. 1; BAG65350).
{ECO:0000305}.
TURN 78 80 {ECO:0000244|PDB:2FLU}.
HELIX 456 464 {ECO:0000244|PDB:2LZ1}.
HELIX 470 475 {ECO:0000244|PDB:2LZ1}.
HELIX 478 487 {ECO:0000244|PDB:2LZ1}.
HELIX 492 504 {ECO:0000244|PDB:2LZ1}.
SEQUENCE 605 AA; 67827 MW; 99FAFD811B6C1416 CRC64;
MMDLELPPPG LPSQQDMDLI DILWRQDIDL GVSREVFDFS QRRKEYELEK QKKLEKERQE
QLQKEQEKAF FAQLQLDEET GEFLPIQPAQ HIQSETSGSA NYSQVAHIPK SDALYFDDCM
QLLAQTFPFV DDNEVSSATF QSLVPDIPGH IESPVFIATN QAQSPETSVA QVAPVDLDGM
QQDIEQVWEE LLSIPELQCL NIENDKLVET TMVPSPEAKL TEVDNYHFYS SIPSMEKEVG
NCSPHFLNAF EDSFSSILST EDPNQLTVNS LNSDATVNTD FGDEFYSAFI AEPSISNSMP
SPATLSHSLS ELLNGPIDVS DLSLCKAFNQ NHPESTAEFN DSDSGISLNT SPSVASPEHS
VESSSYGDTL LGLSDSEVEE LDSAPGSVKQ NGPKTPVHSS GDMVQPLSPS QGQSTHVHDA
QCENTPEKEL PVSPGHRKTP FTKDKHSSRL EAHLTRDELR AKALHIPFPV EKIINLPVVD
FNEMMSKEQF NEAQLALIRD IRRRGKNKVA AQNCRKRKLE NIVELEQDLD HLKDEKEKLL
KEKGENDKSL HLLKKQLSTL YLEVFSMLRD EDGKPYSPSE YSLQQTRDGN VFLVPKSKKP
DVKKN


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