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Q9Z2X8

- KEAP1_MOUSE

UniProt

Q9Z2X8 - KEAP1_MOUSE

Protein

Kelch-like ECH-associated protein 1

Gene

Keap1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Acts as a substrate adapter protein for the E3 ubiquitin ligase complex formed by CUL3 and RBX1 and targets NFE2L2/NRF2 for ubiquitination and degradation by the proteasome, thus resulting in the suppression of its transcriptional activity and the repression of antioxidant response element-mediated detoxifying enzyme gene expression. Retains NFE2L2/NRF2 and may also retain BPTF in the cytosol. Targets PGAM5 for ubiquitination and degradation by the proteasome By similarity.By similarity

    Pathwayi

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. cellular response to interleukin-4 Source: MGI
    2. in utero embryonic development Source: MGI
    3. proteasomal ubiquitin-independent protein catabolic process Source: UniProtKB
    4. protein ubiquitination Source: UniProtKB
    5. regulation of epidermal cell differentiation Source: MGI
    6. regulation of transcription, DNA-templated Source: MGI
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    Transcription, Transcription regulation, Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kelch-like ECH-associated protein 1
    Alternative name(s):
    Cytosolic inhibitor of Nrf2
    Short name:
    INrf2
    Gene namesi
    Name:Keap1
    Synonyms:Inrf2, Kiaa0132
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:1858732. Keap1.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Shuttles between cytoplasm and nucleus.By similarity

    GO - Cellular componenti

    1. centrosome Source: Ensembl
    2. Cul3-RING ubiquitin ligase complex Source: UniProtKB
    3. cytoplasm Source: MGI
    4. endoplasmic reticulum Source: MGI
    5. midbody Source: Ensembl
    6. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi599 – 6013SGR → AAA: Decreases repression of NFE2L2-dependent gene expression. 1 Publication
    Mutagenesisi602 – 6043SGV → AAA: Abolishes repression of NFE2L2-dependent gene expression. 1 Publication
    Mutagenesisi605 – 6084GVAV → AAAA: Decreases repression of NFE2L2-dependent gene expression. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 624624Kelch-like ECH-associated protein 1PRO_0000119094Add
    BLAST

    Post-translational modificationi

    Ubiquitinated by the E3 ubiquitin ligase complex formed by CUL3 and RBX1 and is subject to proteasomal-independent degradation. Quinone-induced oxidative stress, but not sulforaphane, increases its ubiquitination. Ubiquitination and subsequent degradation is most pronounced following prolonged exposure of cells to oxidative stress, particularly in glutathione-deficient cells that are highly susceptible to oxidative stress By similarity.By similarity

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiQ9Z2X8.
    PaxDbiQ9Z2X8.
    PRIDEiQ9Z2X8.

    PTM databases

    PhosphoSiteiQ9Z2X8.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Z2X8.
    BgeeiQ9Z2X8.
    CleanExiMM_KEAP1.
    GenevestigatoriQ9Z2X8.

    Interactioni

    Subunit structurei

    Homodimer. Forms a ternary complex with NFE2L2 and PGAM5. Interacts with the N-terminal regulatory domain of NFE2L2/NRF2. Interacts with BPTF and PTMA. Interacts with CUL3. Part of a complex that contains KEAP1, CUL3 and RBX1 By similarity. Interacts indirectly with ENC1 By similarity. Interacts with MAP1LC3B By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SQSTM1Q135012EBI-647110,EBI-307104From a different organism.
    Sqstm1Q643376EBI-647110,EBI-645025

    Protein-protein interaction databases

    BioGridi206135. 14 interactions.
    DIPiDIP-49698N.
    IntActiQ9Z2X8. 5 interactions.
    MINTiMINT-4111966.
    STRINGi10090.ENSMUSP00000062467.

    Structurei

    Secondary structure

    1
    624
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi328 – 3314
    Beta strandi334 – 3385
    Beta strandi342 – 3454
    Turni347 – 3493
    Beta strandi352 – 3543
    Beta strandi366 – 3705
    Beta strandi373 – 3775
    Beta strandi380 – 3834
    Beta strandi386 – 3894
    Beta strandi393 – 3975
    Turni398 – 4014
    Beta strandi402 – 4054
    Beta strandi417 – 4215
    Beta strandi424 – 4285
    Beta strandi440 – 4445
    Turni445 – 4484
    Beta strandi449 – 4535
    Beta strandi464 – 4685
    Beta strandi471 – 4788
    Beta strandi483 – 4919
    Turni492 – 4954
    Beta strandi496 – 4994
    Beta strandi511 – 5155
    Beta strandi518 – 5225
    Beta strandi527 – 5304
    Beta strandi534 – 5385
    Turni539 – 5424
    Beta strandi543 – 5464
    Beta strandi558 – 5625
    Beta strandi565 – 5695
    Beta strandi574 – 5774
    Beta strandi581 – 5855
    Turni586 – 5894
    Beta strandi590 – 5934
    Beta strandi605 – 6084

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X2JX-ray1.60A309-624[»]
    1X2RX-ray1.70A309-624[»]
    2DYHX-ray1.90A309-624[»]
    2Z32X-ray2.00A309-624[»]
    3ADEX-ray2.80A309-624[»]
    3WDZX-ray2.60A321-609[»]
    3WN7X-ray1.57A/L321-609[»]
    ProteinModelPortaliQ9Z2X8.
    SMRiQ9Z2X8. Positions 59-297, 324-609.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Z2X8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini77 – 14973BTBPROSITE-ProRule annotationAdd
    BLAST
    Domaini184 – 286103BACKAdd
    BLAST
    Repeati327 – 37246Kelch 1Add
    BLAST
    Repeati373 – 42351Kelch 2Add
    BLAST
    Repeati424 – 47047Kelch 3Add
    BLAST
    Repeati471 – 51747Kelch 4Add
    BLAST
    Repeati519 – 56446Kelch 5Add
    BLAST
    Repeati565 – 61147Kelch 6Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi301 – 31010Nuclear export signalBy similarity

    Domaini

    The Kelch repeats mediate interaction with NF2L2/NRF2, BPTF and PGAM5.By similarity

    Sequence similaritiesi

    Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
    Contains 6 Kelch repeats.Curated

    Keywords - Domaini

    Kelch repeat, Repeat

    Phylogenomic databases

    eggNOGiNOG255039.
    GeneTreeiENSGT00740000115088.
    HOGENOMiHOG000230814.
    HOVERGENiHBG014286.
    InParanoidiQ9Z2X8.
    KOiK10456.
    OMAiQIGCTEL.
    OrthoDBiEOG76739M.
    PhylomeDBiQ9Z2X8.
    TreeFamiTF329218.

    Family and domain databases

    Gene3Di2.130.10.80. 1 hit.
    3.30.710.10. 1 hit.
    InterProiIPR011705. BACK.
    IPR000210. BTB/POZ-like.
    IPR011333. BTB/POZ_fold.
    IPR013069. BTB_POZ.
    IPR015916. Gal_Oxidase_b-propeller.
    IPR017096. Kelch-like_gigaxonin-typ.
    IPR006652. Kelch_1.
    [Graphical view]
    PfamiPF07707. BACK. 1 hit.
    PF00651. BTB. 1 hit.
    PF01344. Kelch_1. 6 hits.
    [Graphical view]
    PIRSFiPIRSF037037. Kelch-like_protein_gigaxonin. 1 hit.
    SMARTiSM00875. BACK. 1 hit.
    SM00225. BTB. 1 hit.
    SM00612. Kelch. 6 hits.
    [Graphical view]
    SUPFAMiSSF54695. SSF54695. 1 hit.
    PROSITEiPS50097. BTB. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9Z2X8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQPEPKLSGA PRSSQFLPLW SKCPEGAGDA VMYASTECKA EVTPSQDGNR    50
    TFSYTLEDHT KQAFGVMNEL RLSQQLCDVT LQVKYEDIPA AQFMAHKVVL 100
    ASSSPVFKAM FTNGLREQGM EVVSIEGIHP KVMERLIEFA YTASISVGEK 150
    CVLHVMNGAV MYQIDSVVRA CSDFLVQQLD PSNAIGIANF AEQIGCTELH 200
    QRAREYIYMH FGEVAKQEEF FNLSHCQLAT LISRDDLNVR CESEVFHACI 250
    DWVKYDCPQR RFYVQALLRA VRCHALTPRF LQTQLQKCEI LQADARCKDY 300
    LVQIFQELTL HKPTQAVPCR APKVGRLIYT AGGYFRQSLS YLEAYNPSNG 350
    SWLRLADLQV PRSGLAGCVV GGLLYAVGGR NNSPDGNTDS SALDCYNPMT 400
    NQWSPCASMS VPRNRIGVGV IDGHIYAVGG SHGCIHHSSV ERYEPERDEW 450
    HLVAPMLTRR IGVGVAVLNR LLYAVGGFDG TNRLNSAECY YPERNEWRMI 500
    TPMNTIRSGA GVCVLHNCIY AAGGYDGQDQ LNSVERYDVE TETWTFVAPM 550
    RHHRSALGIT VHQGKIYVLG GYDGHTFLDS VECYDPDSDT WSEVTRMTSG 600
    RSGVGVAVTM EPCRKQIDQQ NCTC 624
    Length:624
    Mass (Da):69,553
    Last modified:May 1, 1999 - v1
    Checksum:i4645DB0122FB5F54
    GO

    Sequence cautioni

    The sequence BAC97871.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti43 – 431T → A in BAE29559. (PubMed:16141072)Curated
    Sequence conflicti43 – 431T → A in BAE30980. (PubMed:16141072)Curated
    Sequence conflicti348 – 3481S → G in BAC32621. (PubMed:16141072)Curated
    Sequence conflicti361 – 3611P → T in BAE29559. (PubMed:16141072)Curated
    Sequence conflicti361 – 3611P → T in BAE30980. (PubMed:16141072)Curated
    Sequence conflicti579 – 5791D → V in BAE32581. (PubMed:16141072)Curated
    Sequence conflicti579 – 5791D → V in BAE33299. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB020063 mRNA. Translation: BAA34639.1.
    AF454353 Genomic DNA. Translation: AAL84711.1.
    AK129061 mRNA. Translation: BAC97871.1. Different initiation.
    AK046178 mRNA. Translation: BAC32621.1.
    AK076234 mRNA. Translation: BAC36267.1.
    AK150437 mRNA. Translation: BAE29559.1.
    AK150485 mRNA. Translation: BAE29601.1.
    AK152142 mRNA. Translation: BAE30980.1.
    AK154430 mRNA. Translation: BAE32581.1.
    AK155507 mRNA. Translation: BAE33299.1.
    AK159858 mRNA. Translation: BAE35433.1.
    BC055732 mRNA. Translation: AAH55732.1.
    CCDSiCCDS22897.1.
    RefSeqiNP_001103775.1. NM_001110305.1.
    NP_001103776.1. NM_001110306.1.
    NP_001103777.1. NM_001110307.1.
    NP_057888.1. NM_016679.4.
    UniGeneiMm.248266.

    Genome annotation databases

    EnsembliENSMUST00000049567; ENSMUSP00000062467; ENSMUSG00000003308.
    ENSMUST00000164812; ENSMUSP00000131029; ENSMUSG00000003308.
    GeneIDi50868.
    KEGGimmu:50868.
    UCSCiuc009oko.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB020063 mRNA. Translation: BAA34639.1 .
    AF454353 Genomic DNA. Translation: AAL84711.1 .
    AK129061 mRNA. Translation: BAC97871.1 . Different initiation.
    AK046178 mRNA. Translation: BAC32621.1 .
    AK076234 mRNA. Translation: BAC36267.1 .
    AK150437 mRNA. Translation: BAE29559.1 .
    AK150485 mRNA. Translation: BAE29601.1 .
    AK152142 mRNA. Translation: BAE30980.1 .
    AK154430 mRNA. Translation: BAE32581.1 .
    AK155507 mRNA. Translation: BAE33299.1 .
    AK159858 mRNA. Translation: BAE35433.1 .
    BC055732 mRNA. Translation: AAH55732.1 .
    CCDSi CCDS22897.1.
    RefSeqi NP_001103775.1. NM_001110305.1.
    NP_001103776.1. NM_001110306.1.
    NP_001103777.1. NM_001110307.1.
    NP_057888.1. NM_016679.4.
    UniGenei Mm.248266.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X2J X-ray 1.60 A 309-624 [» ]
    1X2R X-ray 1.70 A 309-624 [» ]
    2DYH X-ray 1.90 A 309-624 [» ]
    2Z32 X-ray 2.00 A 309-624 [» ]
    3ADE X-ray 2.80 A 309-624 [» ]
    3WDZ X-ray 2.60 A 321-609 [» ]
    3WN7 X-ray 1.57 A/L 321-609 [» ]
    ProteinModelPortali Q9Z2X8.
    SMRi Q9Z2X8. Positions 59-297, 324-609.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 206135. 14 interactions.
    DIPi DIP-49698N.
    IntActi Q9Z2X8. 5 interactions.
    MINTi MINT-4111966.
    STRINGi 10090.ENSMUSP00000062467.

    PTM databases

    PhosphoSitei Q9Z2X8.

    Proteomic databases

    MaxQBi Q9Z2X8.
    PaxDbi Q9Z2X8.
    PRIDEi Q9Z2X8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000049567 ; ENSMUSP00000062467 ; ENSMUSG00000003308 .
    ENSMUST00000164812 ; ENSMUSP00000131029 ; ENSMUSG00000003308 .
    GeneIDi 50868.
    KEGGi mmu:50868.
    UCSCi uc009oko.2. mouse.

    Organism-specific databases

    CTDi 9817.
    MGIi MGI:1858732. Keap1.
    Rougei Search...

    Phylogenomic databases

    eggNOGi NOG255039.
    GeneTreei ENSGT00740000115088.
    HOGENOMi HOG000230814.
    HOVERGENi HBG014286.
    InParanoidi Q9Z2X8.
    KOi K10456.
    OMAi QIGCTEL.
    OrthoDBi EOG76739M.
    PhylomeDBi Q9Z2X8.
    TreeFami TF329218.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    EvolutionaryTracei Q9Z2X8.
    NextBioi 307831.
    PROi Q9Z2X8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Z2X8.
    Bgeei Q9Z2X8.
    CleanExi MM_KEAP1.
    Genevestigatori Q9Z2X8.

    Family and domain databases

    Gene3Di 2.130.10.80. 1 hit.
    3.30.710.10. 1 hit.
    InterProi IPR011705. BACK.
    IPR000210. BTB/POZ-like.
    IPR011333. BTB/POZ_fold.
    IPR013069. BTB_POZ.
    IPR015916. Gal_Oxidase_b-propeller.
    IPR017096. Kelch-like_gigaxonin-typ.
    IPR006652. Kelch_1.
    [Graphical view ]
    Pfami PF07707. BACK. 1 hit.
    PF00651. BTB. 1 hit.
    PF01344. Kelch_1. 6 hits.
    [Graphical view ]
    PIRSFi PIRSF037037. Kelch-like_protein_gigaxonin. 1 hit.
    SMARTi SM00875. BACK. 1 hit.
    SM00225. BTB. 1 hit.
    SM00612. Kelch. 6 hits.
    [Graphical view ]
    SUPFAMi SSF54695. SSF54695. 1 hit.
    PROSITEi PS50097. BTB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
      Tissue: Embryo.
    2. "Mouse INrf2 gene structure."
      Dhakshinamoorthy S., Jaiswal A.K.
      Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: C57BL/6.
    3. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
      DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Fetal brain.
    4. "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 and NOD.
      Tissue: Bone marrow, Corpora quadrigemina, Dendritic cell, Liver and Lung.
    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].
      Strain: C57BL/6.
      Tissue: Brain.
    6. "Keap1-dependent proteasomal degradation of transcription factor Nrf2 contributes to the negative regulation of antioxidant response element-driven gene expression."
      McMahon M., Itoh K., Yamamoto M., Hayes J.D.
      J. Biol. Chem. 278:21592-21600(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Fetal Alz-50 clone 1 interacts with the human orthologue of the Kelch-like Ech-associated protein."
      Strachan G.D., Morgan K.L., Otis L.L., Caltagarone J., Gittis A., Bowser R., Jordan-Sciutto K.L.
      Biochemistry 43:12113-12122(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    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 309-624 IN COMPLEX WITH NFE2L2, MUTAGENESIS OF 599-SER--ARG-601; 602-SER--VAL-604 AND 605-GLY--VAL-608.

    Entry informationi

    Entry nameiKEAP1_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z2X8
    Secondary accession number(s): Q3U243
    , Q3U8N7, Q547S3, Q6ZQI6, Q8BQY3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 135 of the entry and version 1 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3