Q16236 (NF2L2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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):
HEBP1
Nuclear factor, erythroid derived 2, like 2

Gene names

Name:	NFE2L2
Synonyms:	NRF2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	605 AA.
Sequence status	Complete.
Protein existence	Evidence 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). Ref.9 Ref.11 Ref.14
Subcellular location	Cytoplasm › cytosol. 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. 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 process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	DNA-binding
Molecular function	Activator
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular 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 endoplasmic reticulum unfolded protein response Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from mutant phenotype PubMed 23043106. Source: BHF-UCL positive regulation of blood coagulation Inferred from electronic annotation. Source: Compara positive regulation of reactive oxygen species metabolic process Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter in response to stress Inferred from mutant phenotype PubMed 23043106. Source: BHF-UCL proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.10. Source: UniProtKB proteasomal ubiquitin-independent protein catabolic process Inferred from direct assay Ref.12. Source: UniProtKB protein ubiquitination Inferred from direct assay Ref.10. Source: UniProtKB regulation of embryonic development Inferred from electronic annotation. Source: Compara regulation of removal of superoxide radicals Inferred from electronic annotation. Source: Compara transcription from RNA polymerase II promoter Traceable author statement Ref.7. Source: ProtInc
Cellular_component	centrosome Inferred from direct assay. Source: HPA chromatin Inferred from electronic annotation. Source: Compara 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_function	DNA binding Inferred from direct assay PubMed 18554677. 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...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 605

605

Nuclear factor erythroid 2-related factor 2

PRO_0000076449

Regions

Domain

497 – 560

64

bZIP

Region

499 – 518

20

Basic motif By similarity

Region

522 – 529

8

Leucine-zipper By similarity

Amino acid modifications

Modified residue

40

1

Phosphoserine; by PKC

Modified residue

215

1

Phosphoserine Ref.13

Modified residue

596

1

N6-acetyllysine; by CREBBP Ref.15

Modified residue

599

1

N6-acetyllysine; by CREBBP Ref.15

Natural variations

Alternative sequence

1 – 16

16

Missing in isoform 2 and isoform 3.

VSP_025045

Alternative sequence

135 – 141

7

Missing in isoform 3.

VSP_046168

Natural variant

43

1

R → Q.
Corresponds to variant rs35248500 [ dbSNP | Ensembl ].

VAR_032110

Natural variant

99

1

S → P.
Corresponds to variant rs5031039 [ dbSNP | Ensembl ].

VAR_020322

Natural variant

268

1

V → M.
Corresponds to variant rs34154613 [ dbSNP | Ensembl ].

VAR_032111

Experimental info

Mutagenesis

80

1

T → A: Loss of interaction with KEAP1. Ref.16

Sequence conflict

72

1

A → T in AAB32188. Ref.7

Sequence conflict

92

1

I → T in AAB32188. Ref.7

Sequence conflict

178

1

D → Y in AL135266. Ref.3

Sequence conflict

521

1

N → D in BAG65350. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

605

Helix Strand Turn

Details...

Turn

78 – 80

3

Helix

456 – 464

9

Helix

470 – 475

6

Helix

478 – 487

10

Helix

492 – 504

13

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 25, 2002. Version 3. Checksum: 99FAFD811B6C1416	FASTA	605	67,827
	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
	Isoform 2 [UniParc]. Checksum: C0154E60AC7C138C	FASTA	589	66,076
	10 20 30 40 50 60 MDLIDILWRQ DIDLGVSREV FDFSQRRKEY ELEKQKKLEK ERQEQLQKEQ EKAFFAQLQL 70 80 90 100 110 120 DEETGEFLPI QPAQHIQSET SGSANYSQVA HIPKSDALYF DDCMQLLAQT FPFVDDNEVS 130 140 150 160 170 180 SATFQSLVPD IPGHIESPVF IATNQAQSPE TSVAQVAPVD LDGMQQDIEQ VWEELLSIPE 190 200 210 220 230 240 LQCLNIENDK LVETTMVPSP EAKLTEVDNY HFYSSIPSME KEVGNCSPHF LNAFEDSFSS 250 260 270 280 290 300 ILSTEDPNQL TVNSLNSDAT VNTDFGDEFY SAFIAEPSIS NSMPSPATLS HSLSELLNGP 310 320 330 340 350 360 IDVSDLSLCK AFNQNHPEST AEFNDSDSGI SLNTSPSVAS PEHSVESSSY GDTLLGLSDS 370 380 390 400 410 420 EVEELDSAPG SVKQNGPKTP VHSSGDMVQP LSPSQGQSTH VHDAQCENTP EKELPVSPGH 430 440 450 460 470 480 RKTPFTKDKH SSRLEAHLTR DELRAKALHI PFPVEKIINL PVVDFNEMMS KEQFNEAQLA 490 500 510 520 530 540 LIRDIRRRGK NKVAAQNCRK RKLENIVELE QDLDHLKDEK EKLLKEKGEN DKSLHLLKKQ 550 560 570 580 LSTLYLEVFS MLRDEDGKPY SPSEYSLQQT RDGNVFLVPK SKKPDVKKN
	Isoform 3 [UniParc]. Checksum: 8C560533CEB5E2F8	FASTA	582	65,356
	10 20 30 40 50 60 MDLIDILWRQ DIDLGVSREV FDFSQRRKEY ELEKQKKLEK ERQEQLQKEQ EKAFFAQLQL 70 80 90 100 110 120 DEETGEFLPI QPAQHIQSET SGSANYSQVA HIPKSDALYF DDCMQLLAQT FPFVDDNESL 130 140 150 160 170 180 VPDIPGHIES PVFIATNQAQ SPETSVAQVA PVDLDGMQQD IEQVWEELLS IPELQCLNIE 190 200 210 220 230 240 NDKLVETTMV PSPEAKLTEV DNYHFYSSIP SMEKEVGNCS PHFLNAFEDS FSSILSTEDP 250 260 270 280 290 300 NQLTVNSLNS DATVNTDFGD EFYSAFIAEP SISNSMPSPA TLSHSLSELL NGPIDVSDLS 310 320 330 340 350 360 LCKAFNQNHP ESTAEFNDSD SGISLNTSPS VASPEHSVES SSYGDTLLGL SDSEVEELDS 370 380 390 400 410 420 APGSVKQNGP KTPVHSSGDM VQPLSPSQGQ STHVHDAQCE NTPEKELPVS PGHRKTPFTK 430 440 450 460 470 480 DKHSSRLEAH LTRDELRAKA LHIPFPVEKI INLPVVDFNE MMSKEQFNEA QLALIRDIRR 490 500 510 520 530 540 RGKNKVAAQN CRKRKLENIV ELEQDLDHLK DEKEKLLKEK GENDKSLHLL KKQLSTLYLE 550 560 570 580 VFSMLRDEDG KPYSPSEYSL QQTRDGNVFL VPKSKKPDVK KN

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, MASS SPECTROMETRY. 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.

IPI

IPI00000712.
IPI00915403.
IPI00921938.

RefSeq

NP_001138884.1. NM_001145412.2.
NP_001138885.1. NM_001145413.2.
NP_006155.2. NM_006164.4.

UniGene

Hs.155396.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FLU	X-ray	1.50	P	69-84	[»]
2LZ1	NMR	-	A	445-523	[»]

ProteinModelPortal

Q16236.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29971N.

IntAct

Q16236. 7 interactions.

MINT

MINT-2844437.

STRING

9606.ENSP00000380252.

PTM databases

PhosphoSite

Q16236.

Polymorphism databases

DMDM

25453452.

Proteomic databases

PaxDb

Q16236.

PRIDE

Q16236.

Protocols and materials databases

DNASU

4780.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000397062; ENSP00000380252; ENSG00000116044.
ENST00000397063; ENSP00000380253; ENSG00000116044.
ENST00000446151; ENSP00000411575; ENSG00000116044.
ENST00000464747; ENSP00000467401; ENSG00000116044.

GeneID

4780.

KEGG

hsa:4780.

UCSC

uc002ulg.4. human.

Organism-specific databases

CTD

4780.

GeneCards

GC02M178092.

HGNC

HGNC:7782. NFE2L2.

HPA

CAB020317.
HPA002990.

MIM

600492. gene.

neXtProt

NX_Q16236.

PharmGKB

PA31588.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG309753.

HOGENOM

HOG000234410.

HOVERGEN

HBG052609.

InParanoid

Q16236.

KO

K05638.

OMA

ALHIPFP.

OrthoDB

EOG4JT05F.

Gene expression databases

ArrayExpress

Q16236.

Bgee

Q16236.

CleanEx

HS_NFE2L2.

Genevestigator

Q16236.

GermOnline

ENSG00000116044. Homo sapiens.

Family and domain databases

Gene3D

1.10.880.10. 1 hit.

InterPro

IPR004827. bZIP.
IPR008917. Euk_TF_DNA-bd.
[Graphical view]

Pfam

PF00170. bZIP_1. 1 hit.
[Graphical view]

SMART

SM00338. BRLZ. 1 hit.
[Graphical view]

SUPFAM

SSF47454. Euk_transcr_DNA. 1 hit.

PROSITE

PS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1075094.

ChiTaRS

NFE2L2. human.

EvolutionaryTrace

Q16236.

GenomeRNAi

4780.

NextBio

18432.

PMAP-CutDB

Q16236.

SOURCE

Search...

Entry information

Entry name

NF2L2_HUMAN

Accession

Primary (citable) accession number: Q16236
Secondary accession number(s): B2RBU2 , B4E338, E9PGJ7, Q53RW6, Q59HH2, Q96F71

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	November 25, 2002
Last modified:	May 1, 2013
This is version 130 of the entry and version 3 of the sequence. [Complete history]

Entry status

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.