Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q16236

- NF2L2_HUMAN

UniProt

Q16236 - NF2L2_HUMAN

Protein

Nuclear factor erythroid 2-related factor 2

Gene

NFE2L2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 3 (25 Nov 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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: UniProtKB
    2. protein binding Source: IntAct
    3. protein domain specific binding Source: UniProtKB
    4. RNA polymerase II activating transcription factor binding Source: BHF-UCL
    5. sequence-specific DNA binding Source: InterPro
    6. sequence-specific DNA binding transcription factor activity Source: ProtInc

    GO - Biological processi

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

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    SignaLinkiQ16236.

    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):
    HEBP1
    Nuclear factor, erythroid derived 2, like 2
    Gene namesi
    Name:NFE2L2
    Synonyms:NRF2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:7782. NFE2L2.

    Subcellular locationi

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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi80 – 801T → A: Loss of interaction with KEAP1. 1 Publication

    Organism-specific databases

    PharmGKBiPA31588.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 605605Nuclear factor erythroid 2-related factor 2PRO_0000076449Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei40 – 401Phosphoserine; by PKC1 Publication
    Modified residuei215 – 2151Phosphoserine2 Publications
    Modified residuei596 – 5961N6-acetyllysine; by CREBBP1 Publication
    Modified residuei599 – 5991N6-acetyllysine; by CREBBP1 Publication

    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-596 and Lys-599 increases nuclear localization whereas deacetylation by SIRT1 enhances cytoplasmic presence.1 Publication
    Ubiquitinated by the KEAP1-CUL3-RBX1 E3 ubiquitin ligase complex and subject to proteasomal degradation. Ubiquitination is inhibited by sulforaphane.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ16236.
    PaxDbiQ16236.
    PRIDEiQ16236.

    PTM databases

    PhosphoSiteiQ16236.

    Miscellaneous databases

    PMAP-CutDBQ16236.

    Expressioni

    Tissue specificityi

    Widely expressed. Highest expression in adult muscle, kidney, lung, liver and in fetal muscle.

    Inductioni

    Down-regulated by ENC1 via a proteasomal ubiquitin-independent protein catabolic process.

    Gene expression databases

    ArrayExpressiQ16236.
    BgeeiQ16236.
    CleanExiHS_NFE2L2.
    GenevestigatoriQ16236.

    Organism-specific databases

    HPAiCAB020317.
    HPA002990.
    HPA043438.

    Interactioni

    Subunit structurei

    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.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    KEAP1Q1414517EBI-2007911,EBI-751001

    Protein-protein interaction databases

    BioGridi110852. 56 interactions.
    DIPiDIP-29971N.
    IntActiQ16236. 9 interactions.
    MINTiMINT-2844437.
    STRINGi9606.ENSP00000380252.

    Structurei

    Secondary structure

    1
    605
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni78 – 803
    Helixi456 – 4649
    Helixi470 – 4756
    Helixi478 – 48710
    Helixi492 – 50413

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FLUX-ray1.50P69-84[»]
    2LZ1NMR-A445-523[»]
    3ZGCX-ray2.20C76-82[»]
    4IFLX-ray1.80P69-84[»]
    ProteinModelPortaliQ16236.
    SMRiQ16236. Positions 449-557.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16236.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini497 – 56064bZIPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni499 – 51820Basic motifPROSITE-ProRule annotationAdd
    BLAST
    Regioni522 – 5298Leucine-zipperPROSITE-ProRule annotation
    Regioni591 – 5966Mediates interaction with CHD6 and is necessary to activate transcriptionBy similarity

    Domaini

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

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG309753.
    HOGENOMiHOG000234410.
    HOVERGENiHBG052609.
    InParanoidiQ16236.
    KOiK05638.
    OMAiALHIPFP.
    OrthoDBiEOG715Q3N.
    PhylomeDBiQ16236.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q16236-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MMDLELPPPG LPSQQDMDLI DILWRQDIDL GVSREVFDFS QRRKEYELEK    50
    QKKLEKERQE QLQKEQEKAF FAQLQLDEET GEFLPIQPAQ HIQSETSGSA 100
    NYSQVAHIPK SDALYFDDCM QLLAQTFPFV DDNEVSSATF QSLVPDIPGH 150
    IESPVFIATN QAQSPETSVA QVAPVDLDGM QQDIEQVWEE LLSIPELQCL 200
    NIENDKLVET TMVPSPEAKL TEVDNYHFYS SIPSMEKEVG NCSPHFLNAF 250
    EDSFSSILST EDPNQLTVNS LNSDATVNTD FGDEFYSAFI AEPSISNSMP 300
    SPATLSHSLS ELLNGPIDVS DLSLCKAFNQ NHPESTAEFN DSDSGISLNT 350
    SPSVASPEHS VESSSYGDTL LGLSDSEVEE LDSAPGSVKQ NGPKTPVHSS 400
    GDMVQPLSPS QGQSTHVHDA QCENTPEKEL PVSPGHRKTP FTKDKHSSRL 450
    EAHLTRDELR AKALHIPFPV EKIINLPVVD FNEMMSKEQF NEAQLALIRD 500
    IRRRGKNKVA AQNCRKRKLE NIVELEQDLD HLKDEKEKLL KEKGENDKSL 550
    HLLKKQLSTL YLEVFSMLRD EDGKPYSPSE YSLQQTRDGN VFLVPKSKKP 600
    DVKKN 605
    Length:605
    Mass (Da):67,827
    Last modified:November 25, 2002 - v3
    Checksum:i99FAFD811B6C1416
    GO
    Isoform 2 (identifier: Q16236-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-16: Missing.

    Show »
    Length:589
    Mass (Da):66,076
    Checksum:iC0154E60AC7C138C
    GO
    Isoform 3 (identifier: Q16236-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-16: Missing.
         135-141: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:582
    Mass (Da):65,356
    Checksum:i8C560533CEB5E2F8
    GO

    Sequence cautioni

    The sequence AAB32188.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAD92023.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti72 – 721A → T in AAB32188. (PubMed:7937919)Curated
    Sequence conflicti92 – 921I → T in AAB32188. (PubMed:7937919)Curated
    Sequence conflicti178 – 1781D → Y in AL135266. (PubMed:15815621)Curated
    Sequence conflicti521 – 5211N → D in BAG65350. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti43 – 431R → Q.
    Corresponds to variant rs35248500 [ dbSNP | Ensembl ].
    VAR_032110
    Natural varianti99 – 991S → P.
    Corresponds to variant rs5031039 [ dbSNP | Ensembl ].
    VAR_020322
    Natural varianti268 – 2681V → M.
    Corresponds to variant rs34154613 [ dbSNP | Ensembl ].
    VAR_032111

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1616Missing in isoform 2 and isoform 3. 2 PublicationsVSP_025045Add
    BLAST
    Alternative sequencei135 – 1417Missing in isoform 3. 1 PublicationVSP_046168

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS42782.1. [Q16236-1]
    CCDS46457.1. [Q16236-2]
    CCDS46458.1. [Q16236-3]
    RefSeqiNP_001138884.1. NM_001145412.2. [Q16236-2]
    NP_001138885.1. NM_001145413.2. [Q16236-3]
    NP_006155.2. NM_006164.4. [Q16236-1]
    UniGeneiHs.744006.

    Genome annotation databases

    EnsembliENST00000397062; ENSP00000380252; ENSG00000116044. [Q16236-1]
    ENST00000397063; ENSP00000380253; ENSG00000116044. [Q16236-2]
    ENST00000446151; ENSP00000411575; ENSG00000116044. [Q16236-3]
    ENST00000464747; ENSP00000467401; ENSG00000116044. [Q16236-2]
    GeneIDi4780.
    KEGGihsa:4780.
    UCSCiuc002ulg.5. human. [Q16236-1]

    Polymorphism databases

    DMDMi25453452.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS42782.1. [Q16236-1 ]
    CCDS46457.1. [Q16236-2 ]
    CCDS46458.1. [Q16236-3 ]
    RefSeqi NP_001138884.1. NM_001145412.2. [Q16236-2 ]
    NP_001138885.1. NM_001145413.2. [Q16236-3 ]
    NP_006155.2. NM_006164.4. [Q16236-1 ]
    UniGenei Hs.744006.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FLU X-ray 1.50 P 69-84 [» ]
    2LZ1 NMR - A 445-523 [» ]
    3ZGC X-ray 2.20 C 76-82 [» ]
    4IFL X-ray 1.80 P 69-84 [» ]
    ProteinModelPortali Q16236.
    SMRi Q16236. Positions 449-557.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110852. 56 interactions.
    DIPi DIP-29971N.
    IntActi Q16236. 9 interactions.
    MINTi MINT-2844437.
    STRINGi 9606.ENSP00000380252.

    Chemistry

    ChEMBLi CHEMBL1075094.

    PTM databases

    PhosphoSitei Q16236.

    Polymorphism databases

    DMDMi 25453452.

    Proteomic databases

    MaxQBi Q16236.
    PaxDbi Q16236.
    PRIDEi Q16236.

    Protocols and materials databases

    DNASUi 4780.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000397062 ; ENSP00000380252 ; ENSG00000116044 . [Q16236-1 ]
    ENST00000397063 ; ENSP00000380253 ; ENSG00000116044 . [Q16236-2 ]
    ENST00000446151 ; ENSP00000411575 ; ENSG00000116044 . [Q16236-3 ]
    ENST00000464747 ; ENSP00000467401 ; ENSG00000116044 . [Q16236-2 ]
    GeneIDi 4780.
    KEGGi hsa:4780.
    UCSCi uc002ulg.5. human. [Q16236-1 ]

    Organism-specific databases

    CTDi 4780.
    GeneCardsi GC02M178092.
    HGNCi HGNC:7782. NFE2L2.
    HPAi CAB020317.
    HPA002990.
    HPA043438.
    MIMi 600492. gene.
    neXtProti NX_Q16236.
    PharmGKBi PA31588.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG309753.
    HOGENOMi HOG000234410.
    HOVERGENi HBG052609.
    InParanoidi Q16236.
    KOi K05638.
    OMAi ALHIPFP.
    OrthoDBi EOG715Q3N.
    PhylomeDBi Q16236.
    TreeFami TF326681.

    Enzyme and pathway databases

    SignaLinki Q16236.

    Miscellaneous databases

    ChiTaRSi NFE2L2. human.
    EvolutionaryTracei Q16236.
    GeneWikii NFE2L2.
    GenomeRNAii 4780.
    NextBioi 18432.
    PMAP-CutDB Q16236.
    PROi Q16236.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16236.
    Bgeei Q16236.
    CleanExi HS_NFE2L2.
    Genevestigatori Q16236.

    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

    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. 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. 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.

    Entry informationi

    Entry nameiNF2L2_HUMAN
    AccessioniPrimary (citable) accession number: Q16236
    Secondary accession number(s): B2RBU2
    , B4E338, E9PGJ7, Q53RW6, Q59HH2, Q96F71
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: November 25, 2002
    Last modified: October 1, 2014
    This is version 145 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3