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Q16236 (NF2L2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear factor erythroid 2-related factor 2

Short name=NF-E2-related factor 2
Short name=NFE2-related factor 2
Alternative name(s):
HEBP1
Nuclear factor, erythroid derived 2, like 2
Gene names
Name:NFE2L2
Synonyms:NRF2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length605 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. 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. Ref.8

Subunit structure

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. Ref.9 Ref.11 Ref.14

Subcellular location

Cytoplasmcytosol. Nucleus. Note: Cytosolic under unstressed conditions, translocates into the nucleus upon induction by electrophilic agents. Ref.8 Ref.15

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. Ref.12

Domain

Acidic activation domain in the N-terminus, and DNA binding domain in the C-terminus.

Post-translational modification

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-596 and Lys-599 increases nuclear localization whereas deacetylation by SIRT1 enhances cytoplasmic presence. Ref.15

Ubiquitinated by the KEAP1-CUL3-RBX1 E3 ubiquitin ligase complex and subject to proteasomal degradation. Ubiquitination is inhibited by sulforaphane. Ref.10

Sequence similarities

Belongs to the bZIP family. CNC subfamily.

Contains 1 bZIP (basic-leucine zipper) domain.

Sequence caution

The sequence AAB32188.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAD92023.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandDNA-binding
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to hydrogen peroxide

Inferred from mutant phenotype PubMed 23043106. Source: BHF-UCL

cellular response to laminar fluid shear stress

Inferred from mutant phenotype PubMed 23043106. Source: BHF-UCL

cellular response to tumor necrosis factor

Inferred from mutant phenotype PubMed 18202225. Source: BHF-UCL

endoplasmic reticulum unfolded protein response

Inferred from electronic annotation. Source: Ensembl

negative regulation of endothelial cell apoptotic process

Inferred from mutant phenotype PubMed 23043106. Source: BHF-UCL

negative regulation of intrinsic apoptotic signaling pathway in response to oxidative stress

Inferred from mutant phenotype PubMed 23043106. Source: BHF-UCL

positive regulation of blood coagulation

Inferred from electronic annotation. Source: Ensembl

positive regulation of reactive oxygen species metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 18202225. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter in response to stress

Inferred from mutant phenotype PubMed 23043106. Source: BHF-UCL

proteasomal ubiquitin-independent protein catabolic process

Inferred from direct assay Ref.12. Source: UniProtKB

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.10. Source: UniProtKB

protein ubiquitination

Inferred from direct assay Ref.10. Source: UniProtKB

regulation of embryonic development

Inferred from electronic annotation. Source: Ensembl

regulation of removal of superoxide radicals

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Traceable author statement Ref.7. Source: ProtInc

   Cellular_componentcentrosome

Inferred from direct assay. Source: HPA

chromatin

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from direct assay PubMed 23043106. Source: BHF-UCL

nucleus

Inferred from direct assay PubMed 18554677. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionDNA binding

Inferred from direct assay PubMed 18554677. Source: UniProtKB

RNA polymerase II activating transcription factor binding

Inferred from physical interaction PubMed 23043106. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.16PubMed 21988832. Source: IntAct

protein domain specific binding

Inferred from physical interaction Ref.9. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.7. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

KEAP1Q1414517EBI-2007911,EBI-751001

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q16236-1)

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.
Isoform 2 (identifier: Q16236-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: Missing.
Isoform 3 (identifier: Q16236-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: Missing.
     135-141: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 605605Nuclear factor erythroid 2-related factor 2
PRO_0000076449

Regions

Domain497 – 56064bZIP
Region499 – 51820Basic motif By similarity
Region522 – 5298Leucine-zipper By similarity
Region591 – 5966Mediates interaction with CHD6 and is necessary to activate transcription By similarity

Amino acid modifications

Modified residue401Phosphoserine; by PKC
Modified residue2151Phosphoserine Ref.13
Modified residue5961N6-acetyllysine; by CREBBP Ref.15
Modified residue5991N6-acetyllysine; by CREBBP Ref.15

Natural variations

Alternative sequence1 – 1616Missing in isoform 2 and isoform 3.
VSP_025045
Alternative sequence135 – 1417Missing in isoform 3.
VSP_046168
Natural variant431R → Q.
Corresponds to variant rs35248500 [ dbSNP | Ensembl ].
VAR_032110
Natural variant991S → P.
Corresponds to variant rs5031039 [ dbSNP | Ensembl ].
VAR_020322
Natural variant2681V → M.
Corresponds to variant rs34154613 [ dbSNP | Ensembl ].
VAR_032111

Experimental info

Mutagenesis801T → A: Loss of interaction with KEAP1. Ref.16
Sequence conflict721A → T in AAB32188. Ref.7
Sequence conflict921I → T in AAB32188. Ref.7
Sequence conflict1781D → Y in AL135266. Ref.3
Sequence conflict5211N → D in BAG65350. Ref.1

Secondary structure

........... 605
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 25, 2002. Version 3.
Checksum: 99FAFD811B6C1416

FASTA60567,827
        10         20         30         40         50         60 
MMDLELPPPG LPSQQDMDLI DILWRQDIDL GVSREVFDFS QRRKEYELEK QKKLEKERQE 

        70         80         90        100        110        120 
QLQKEQEKAF FAQLQLDEET GEFLPIQPAQ HIQSETSGSA NYSQVAHIPK SDALYFDDCM 

       130        140        150        160        170        180 
QLLAQTFPFV DDNEVSSATF QSLVPDIPGH IESPVFIATN QAQSPETSVA QVAPVDLDGM 

       190        200        210        220        230        240 
QQDIEQVWEE LLSIPELQCL NIENDKLVET TMVPSPEAKL TEVDNYHFYS SIPSMEKEVG 

       250        260        270        280        290        300 
NCSPHFLNAF EDSFSSILST EDPNQLTVNS LNSDATVNTD FGDEFYSAFI AEPSISNSMP 

       310        320        330        340        350        360 
SPATLSHSLS ELLNGPIDVS DLSLCKAFNQ NHPESTAEFN DSDSGISLNT SPSVASPEHS 

       370        380        390        400        410        420 
VESSSYGDTL LGLSDSEVEE LDSAPGSVKQ NGPKTPVHSS GDMVQPLSPS QGQSTHVHDA 

       430        440        450        460        470        480 
QCENTPEKEL PVSPGHRKTP FTKDKHSSRL EAHLTRDELR AKALHIPFPV EKIINLPVVD 

       490        500        510        520        530        540 
FNEMMSKEQF NEAQLALIRD IRRRGKNKVA AQNCRKRKLE NIVELEQDLD HLKDEKEKLL 

       550        560        570        580        590        600 
KEKGENDKSL HLLKKQLSTL YLEVFSMLRD EDGKPYSPSE YSLQQTRDGN VFLVPKSKKP 


DVKKN 

« Hide

Isoform 2 [UniParc].

Checksum: C0154E60AC7C138C
Show »

FASTA58966,076
Isoform 3 [UniParc].

Checksum: 8C560533CEB5E2F8
Show »

FASTA58265,356

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Tissue: Tongue and Uterus.
[2]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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Myeloid leukemia cell.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
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. expand/collapse author list , 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.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM 1).
Tissue: Lung.
[6]"The full-ORF clone resource of the German cDNA consortium."
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.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-202 (ISOFORM 1).
Tissue: Melanoma.
[7]"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."
Moi P., Chan K., Asunis I., Cao A., Kan Y.W.
Proc. Natl. Acad. Sci. U.S.A. 91:9926-9930(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-605 (ISOFORM 1).
Tissue: Fetal liver.
[8]"Regulation of the antioxidant response element by protein kinase C-mediated phosphorylation of NF-E2-related factor 2."
Huang H.-C., Nguyen T., Pickett C.B.
Proc. Natl. Acad. Sci. U.S.A. 97:12475-12480(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION BY PKC.
[9]"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."
Wang Y., Devereux W., Stewart T.M., Casero R.A. Jr.
Biochem. J. 355:45-49(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PMF1.
[10]"Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for Cul3, targets Keap1 for degradation by a proteasome-independent pathway."
Zhang D.D., Lo S.C., Sun Z., Habib G.M., Lieberman M.W., Hannink M.
J. Biol. Chem. 280:30091-30099(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[11]"PGAM5 tethers a ternary complex containing Keap1 and Nrf2 to mitochondria."
Lo S.-C., Hannink M.
Exp. Cell Res. 314:1789-1803(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PGAM5 AND KEAP1.
[12]"Ectodermal-neural cortex 1 down-regulates Nrf2 at the translational level."
Wang X.J., Zhang D.D.
PLoS ONE 4:E5492-E5492(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: DOWN-REGULATION BY ENC1.
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Transformation of eEF1Bdelta into heat-shock response transcription factor by alternative splicing."
Kaitsuka T., Tomizawa K., Matsushita M.
EMBO Rep. 12:673-681(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EEF1D.
[15]"Acetylation-deacetylation of the transcription factor Nrf2 (nuclear factor erythroid 2-related factor 2) regulates its transcriptional activity and nucleocytoplasmic localization."
Kawai Y., Garduno L., Theodore M., Yang J., Arinze I.J.
J. Biol. Chem. 286:7629-7640(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-596 AND LYS-599, DEACETYLATION BY SIRT1, SUBCELLULAR LOCATION.
[16]"Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signaling."
Lo S.-C., Li X., Henzl M.T., Beamer L.J., Hannink M.
EMBO J. 25:3605-3617(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 69-84 IN COMPLEX WITH KEAP1, MUTAGENESIS OF THR-80.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK304555 mRNA. Translation: BAG65350.1.
AK314816 mRNA. Translation: BAG37339.1.
AB208786 mRNA. Translation: BAD92023.1. Different initiation.
AC019080 Genomic DNA. No translation available.
AC079305 Genomic DNA. Translation: AAY14710.1.
CH471058 Genomic DNA. Translation: EAX11062.1.
BC011558 mRNA. Translation: AAH11558.1.
AL135266 mRNA. No translation available.
S74017 mRNA. Translation: AAB32188.1. Different initiation.
CCDSCCDS42782.1. [Q16236-1]
CCDS46457.1. [Q16236-2]
CCDS46458.1. [Q16236-3]
RefSeqNP_001138884.1. NM_001145412.2. [Q16236-2]
NP_001138885.1. NM_001145413.2. [Q16236-3]
NP_006155.2. NM_006164.4. [Q16236-1]
UniGeneHs.744006.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FLUX-ray1.50P69-84[»]
2LZ1NMR-A445-523[»]
3ZGCX-ray2.20C76-82[»]
4IFLX-ray1.80P69-84[»]
ProteinModelPortalQ16236.
SMRQ16236. Positions 449-557.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110852. 51 interactions.
DIPDIP-29971N.
IntActQ16236. 8 interactions.
MINTMINT-2844437.
STRING9606.ENSP00000380252.

Chemistry

ChEMBLCHEMBL1075094.

PTM databases

PhosphoSiteQ16236.

Polymorphism databases

DMDM25453452.

Proteomic databases

MaxQBQ16236.
PaxDbQ16236.
PRIDEQ16236.

Protocols and materials databases

DNASU4780.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000397062; ENSP00000380252; ENSG00000116044. [Q16236-1]
ENST00000397063; ENSP00000380253; ENSG00000116044. [Q16236-2]
ENST00000446151; ENSP00000411575; ENSG00000116044. [Q16236-3]
ENST00000464747; ENSP00000467401; ENSG00000116044. [Q16236-2]
GeneID4780.
KEGGhsa:4780.
UCSCuc002ulg.5. human. [Q16236-1]

Organism-specific databases

CTD4780.
GeneCardsGC02M178092.
HGNCHGNC:7782. NFE2L2.
HPACAB020317.
HPA002990.
HPA043438.
MIM600492. gene.
neXtProtNX_Q16236.
PharmGKBPA31588.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG309753.
HOGENOMHOG000234410.
HOVERGENHBG052609.
InParanoidQ16236.
KOK05638.
OMAALHIPFP.
OrthoDBEOG715Q3N.
PhylomeDBQ16236.
TreeFamTF326681.

Enzyme and pathway databases

SignaLinkQ16236.

Gene expression databases

ArrayExpressQ16236.
BgeeQ16236.
CleanExHS_NFE2L2.
GenevestigatorQ16236.

Family and domain databases

Gene3D1.10.880.10. 1 hit.
InterProIPR004827. bZIP.
IPR004826. bZIP_Maf.
IPR008917. TF_DNA-bd.
[Graphical view]
PfamPF03131. bZIP_Maf. 1 hit.
[Graphical view]
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
SUPFAMSSF47454. SSF47454. 1 hit.
PROSITEPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNFE2L2. human.
EvolutionaryTraceQ16236.
GeneWikiNFE2L2.
GenomeRNAi4780.
NextBio18432.
PMAP-CutDBQ16236.
PROQ16236.
SOURCESearch...

Entry information

Entry nameNF2L2_HUMAN
AccessionPrimary (citable) accession number: Q16236
Secondary accession number(s): B2RBU2 expand/collapse secondary AC list , B4E338, E9PGJ7, Q53RW6, Q59HH2, Q96F71
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 25, 2002
Last modified: July 9, 2014
This is version 143 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM