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Q60795

- NF2L2_MOUSE

UniProt

Q60795 - NF2L2_MOUSE

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Protein

Nuclear factor erythroid 2-related factor 2

Gene

Nfe2l2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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. 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.1 Publication

GO - Molecular functioni

  1. DNA binding Source: MGI
  2. RNA polymerase II distal enhancer sequence-specific DNA binding Source: NTNU_SB
  3. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
  4. sequence-specific DNA binding transcription factor activity Source: MGI

GO - Biological processi

  1. cellular response to hydrogen peroxide Source: Ensembl
  2. cellular response to laminar fluid shear stress Source: Ensembl
  3. cellular response to oxidative stress Source: BHF-UCL
  4. cellular response to tumor necrosis factor Source: Ensembl
  5. endoplasmic reticulum unfolded protein response Source: MGI
  6. negative regulation of endothelial cell apoptotic process Source: Ensembl
  7. negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: Ensembl
  8. positive regulation of blood coagulation Source: BHF-UCL
  9. positive regulation of reactive oxygen species metabolic process Source: BHF-UCL
  10. positive regulation of transcription, DNA-templated Source: MGI
  11. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  12. positive regulation of transcription from RNA polymerase II promoter in response to stress Source: Ensembl
  13. proteasomal ubiquitin-independent protein catabolic process Source: UniProtKB
  14. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  15. protein ubiquitination Source: UniProtKB
  16. regulation of embryonic development Source: MGI
  17. regulation of removal of superoxide radicals Source: BHF-UCL
  18. regulation of transcription, DNA-templated Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear factor erythroid 2-related factor 2
Short name:
NF-E2-related factor 2
Short name:
NFE2-related factor 2
Alternative name(s):
Nuclear factor, erythroid derived 2, like 2
Gene namesi
Name:Nfe2l2
Synonyms:Nrf-2, Nrf2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:108420. Nfe2l2.

Subcellular locationi

Cytoplasmcytosol 1 Publication. Nucleus 1 PublicationPROSITE-ProRule annotation
Note: Cytosolic under unstressed conditions, translocates into the nucleus upon induction by electrophilic agents.

GO - Cellular componenti

  1. centrosome Source: Ensembl
  2. chromatin Source: BHF-UCL
  3. cytoplasm Source: BHF-UCL
  4. cytosol Source: BHF-UCL
  5. nucleus Source: BHF-UCL
  6. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 597597Nuclear factor erythroid 2-related factor 2PRO_0000076450Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei40 – 401PhosphoserineBy similarity
Modified residuei207 – 2071PhosphoserineBy similarity
Modified residuei588 – 5881N6-acetyllysine; by CREBBPBy similarity
Modified residuei591 – 5911N6-acetyllysine; by CREBBPBy similarity

Post-translational modificationi

Phosphorylation of Ser-40 by PKC in response to oxidative stress dissociates NFE2L2 from its cytoplasmic inhibitor KEAP1, promoting its translocation into the nucleus.By similarity
Acetylation at Lys-588 and Lys-591 increases nuclear localization whereas deacetylation by SIRT1 enhances cytoplasmic presence.By similarity
Ubiquitinated by the KEAP1-CUL3-RBX1 E3 ubiquitin ligase complex and subject to proteasomal degradation. Ubiquitination is inhibited by sulforaphane By similarity.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ60795.
PRIDEiQ60795.

PTM databases

PhosphoSiteiQ60795.

Expressioni

Tissue specificityi

Widely expressed. Highest expression in liver, skeletal muscle, luminal cells of the stomach and intestine, lining of the bronchi and alveoli, and in renal tubules; followed by heart, spleen, testis and brain.

Gene expression databases

BgeeiQ60795.
CleanExiMM_NFE2L2.
GenevestigatoriQ60795.

Interactioni

Subunit structurei

Heterodimer. Forms a ternary complex with PGAM5 and KEAP1. Interacts with EEF1D at heat shock promoter elements (HSE). Interacts with KEAP1. Interacts via its leucine-zipper domain with the coiled-coil domain of PMF1. 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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Arrb1Q8BWG84EBI-642563,EBI-641778

Protein-protein interaction databases

BioGridi201744. 24 interactions.
IntActiQ60795. 1 interaction.
MINTiMINT-1744109.

Structurei

Secondary structure

1
597
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi19 – 257
Helixi28 – 303
Helixi34 – 374
Turni78 – 803

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X2RX-ray1.70B76-84[»]
2DYHX-ray1.90B22-36[»]
3WN7X-ray1.57B/M17-51[»]
ProteinModelPortaliQ60795.
SMRiQ60795. Positions 441-549.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ60795.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini489 – 55264bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni491 – 51020Basic motifPROSITE-ProRule annotationAdd
BLAST
Regioni514 – 5218Leucine-zipperPROSITE-ProRule annotation
Regioni583 – 5886Mediates interaction with CHD6 and is necessary to activate transcriptionBy similarity

Sequence similaritiesi

Belongs to the bZIP family. CNC subfamily.Curated
Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG309753.
GeneTreeiENSGT00550000074399.
HOGENOMiHOG000234410.
HOVERGENiHBG052609.
InParanoidiQ60795.
KOiK05638.
OMAiALHIPFP.
OrthoDBiEOG715Q3N.
PhylomeDBiQ60795.
TreeFamiTF326681.

Family and domain databases

Gene3Di1.10.880.10. 1 hit.
InterProiIPR004827. bZIP.
IPR004826. bZIP_Maf.
IPR008917. TF_DNA-bd.
[Graphical view]
PfamiPF03131. bZIP_Maf. 1 hit.
[Graphical view]
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
SUPFAMiSSF47454. SSF47454. 1 hit.
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q60795-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MMDLELPPPG LQSQQDMDLI DILWRQDIDL GVSREVFDFS QRQKDYELEK
60 70 80 90 100
QKKLEKERQE QLQKEQEKAF FAQFQLDEET GEFLPIQPAQ HIQTDTSGSA
110 120 130 140 150
SYSQVAHIPK QDALYFEDCM QLLAETFPFV DDHESLALDI PSHAESSVFT
160 170 180 190 200
APHQAQSLNS SLEAAMTDLS SIEQDMEQVW QELFSIPELQ CLNTENKQLA
210 220 230 240 250
DTTAVPSPEA TLTEMDSNYH FYSSISSLEK EVGNCGPHFL HGFEDSFSSI
260 270 280 290 300
LSTDDASQLT SLDSNPTLNT DFGDEFYSAF IAEPSDGGSM PSSAAISQSL
310 320 330 340 350
SELLDGTIEG CDLSLCKAFN PKHAEGTMEF NDSDSGISLN TSPSRASPEH
360 370 380 390 400
SVESSIYGDP PPGFSDSEME ELDSAPGSVK QNGPKAQPAH SPGDTVQPLS
410 420 430 440 450
PAQGHSAPMR ESQCENTTKK EVPVSPGHQK APFTKDKHSS RLEAHLTRDE
460 470 480 490 500
LRAKALHIPF PVEKIINLPV DDFNEMMSKE QFNEAQLALI RDIRRRGKNK
510 520 530 540 550
VAAQNCRKRK LENIVELEQD LGHLKDEREK LLREKGENDR NLHLLKRRLS
560 570 580 590
TLYLEVFSML RDEDGKPYSP SEYSLQQTRD GNVFLVPKSK KPDTKKN
Length:597
Mass (Da):66,901
Last modified:January 1, 1998 - v2
Checksum:i6128707C82CAE239
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U70475, U70474 Genomic DNA. Translation: AAC52983.1.
AK142347 mRNA. Translation: BAE25040.1.
AL772404 Genomic DNA. Translation: CAM22493.1.
BC026943 mRNA. Translation: AAH26943.1.
U20532 mRNA. Translation: AAA68291.1.
CCDSiCCDS16150.1.
PIRiI49261.
RefSeqiNP_035032.1. NM_010902.3.
UniGeneiMm.1025.

Genome annotation databases

EnsembliENSMUST00000102672; ENSMUSP00000099733; ENSMUSG00000015839.
GeneIDi18024.
KEGGimmu:18024.
UCSCiuc008keq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U70475 , U70474 Genomic DNA. Translation: AAC52983.1 .
AK142347 mRNA. Translation: BAE25040.1 .
AL772404 Genomic DNA. Translation: CAM22493.1 .
BC026943 mRNA. Translation: AAH26943.1 .
U20532 mRNA. Translation: AAA68291.1 .
CCDSi CCDS16150.1.
PIRi I49261.
RefSeqi NP_035032.1. NM_010902.3.
UniGenei Mm.1025.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1X2R X-ray 1.70 B 76-84 [» ]
2DYH X-ray 1.90 B 22-36 [» ]
3WN7 X-ray 1.57 B/M 17-51 [» ]
ProteinModelPortali Q60795.
SMRi Q60795. Positions 441-549.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201744. 24 interactions.
IntActi Q60795. 1 interaction.
MINTi MINT-1744109.

Chemistry

ChEMBLi CHEMBL1075148.

PTM databases

PhosphoSitei Q60795.

Proteomic databases

PaxDbi Q60795.
PRIDEi Q60795.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000102672 ; ENSMUSP00000099733 ; ENSMUSG00000015839 .
GeneIDi 18024.
KEGGi mmu:18024.
UCSCi uc008keq.1. mouse.

Organism-specific databases

CTDi 4780.
MGIi MGI:108420. Nfe2l2.

Phylogenomic databases

eggNOGi NOG309753.
GeneTreei ENSGT00550000074399.
HOGENOMi HOG000234410.
HOVERGENi HBG052609.
InParanoidi Q60795.
KOi K05638.
OMAi ALHIPFP.
OrthoDBi EOG715Q3N.
PhylomeDBi Q60795.
TreeFami TF326681.

Miscellaneous databases

ChiTaRSi NFE2L2. mouse.
EvolutionaryTracei Q60795.
NextBioi 293087.
PROi Q60795.
SOURCEi Search...

Gene expression databases

Bgeei Q60795.
CleanExi MM_NFE2L2.
Genevestigatori Q60795.

Family and domain databases

Gene3Di 1.10.880.10. 1 hit.
InterProi IPR004827. bZIP.
IPR004826. bZIP_Maf.
IPR008917. TF_DNA-bd.
[Graphical view ]
Pfami PF03131. bZIP_Maf. 1 hit.
[Graphical view ]
SMARTi SM00338. BRLZ. 1 hit.
[Graphical view ]
SUPFAMi SSF47454. SSF47454. 1 hit.
PROSITEi PS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "NRF2, a member of the NFE2 family of transcription factors, is not essential for murine erythropoiesis, growth, and development."
    Chan K., Lu R., Chang J.C., Kan Y.W.
    Proc. Natl. Acad. Sci. U.S.A. 93:13943-13948(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/SvJ.
    Tissue: Lung.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryonic lung.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II.
    Tissue: Mammary gland.
  5. "cDNA cloning of murine Nrf 2 gene, coding for a p45 NF-E2 related transcription factor."
    Chui D.H.K., Tang W., Orkin S.H.
    Biochem. Biophys. Res. Commun. 209:40-46(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-597.
    Strain: C57BL/6J.
    Tissue: Erythroblast.
  6. "Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain."
    Itoh K., Wakabayashi N., Katoh Y., Ishii T., Igarashi K., Engel J.D., Yamamoto M.
    Genes Dev. 13:76-86(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KEAP1.
  7. "Cloning and characterization of the mouse polyamine-modulated factor-1 (mPMF-1) gene: an alternatively spliced homologue of the human transcription factor."
    Wang Y., Devereux W., Woster P.M., Casero R.A. Jr.
    Biochem. J. 359:387-392(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NFE2L2.
  8. "Structural basis for defects of Keap1 activity provoked by its point mutations in lung cancer."
    Padmanabhan B., Tong K.I., Ohta T., Nakamura Y., Scharlock M., Ohtsuji M., Kang M., Kobayashi A., Yokoyama S., Yamamoto M.
    Mol. Cell 21:689-700(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 76-84 IN COMPLEX WITH KEAP1.

Entry informationi

Entry nameiNF2L2_MOUSE
AccessioniPrimary (citable) accession number: Q60795
Secondary accession number(s): Q3UQK0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: October 29, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3