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Q14145

- KEAP1_HUMAN

UniProt

Q14145 - KEAP1_HUMAN

Protein

Kelch-like ECH-associated protein 1

Gene

KEAP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 2 (01 May 2007)
      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.5 Publications

    Enzyme regulationi

    Ubiquitination and subsequent degradation of PGAM5 is inhibited by oxidative stress and sulforaphane. Sulforaphane also inhibits ubiquitination of NFE2L2/NRF2.2 Publications

    Pathwayi

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

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

    Keywords - Biological processi

    Transcription, Transcription regulation, Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_75842. 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
    Kelch-like protein 19
    Gene namesi
    Name:KEAP1
    Synonyms:INRF2, KIAA0132, KLHL19
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:23177. KEAP1.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Shuttles between cytoplasm and nucleus.

    GO - Cellular componenti

    1. Cul3-RING ubiquitin ligase complex Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. endoplasmic reticulum Source: Ensembl
    4. microtubule organizing center Source: HPA
    5. midbody Source: UniProtKB
    6. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi125 – 1273IEG → AAA: Increases ubiquitination and proteolytic degradation. 1 Publication
    Mutagenesisi151 – 1511C → S: Constitutive repression of NFE2L2-dependent gene expression. Promotes increased degradation of NFE2L2. Resistance of ubiquitination of PGAM5 to inhibition by oxidative stress and sulforaphane. Does not prevent its ubiquitination and degradation in response to quinone-induced oxidative stress. 4 Publications
    Mutagenesisi162 – 1643YQI → AAA: Increases ubiquitination and proteolytic degradation. 1 Publication
    Mutagenesisi273 – 2731C → S: Abolishes repression of NFE2L2-dependent gene expression. Slows down degradation of NFE2L2. 2 Publications
    Mutagenesisi288 – 2881C → S: Abolishes repression of NFE2L2-dependent gene expression. Slows down degradation of NFE2L2. 2 Publications
    Mutagenesisi308 – 3081L → A: Loss of export from nucleus; when associated with A-310. 2 Publications
    Mutagenesisi310 – 3101L → A: Loss of export from nucleus; when associated with A-308. 2 Publications
    Mutagenesisi334 – 3341Y → A: Loss of interaction with NFE2L2. Strongly reduces repression of NFE2L2-dependent gene expression. Loss of interaction with PGAM5. 3 Publications
    Mutagenesisi380 – 3801R → A: Loss of interaction with NFE2L2. Abolishes repression of NFE2L2-dependent gene expression. 2 Publications
    Mutagenesisi382 – 3821N → A: Loss of interaction with NFE2L2. Strongly reduces repression of NFE2L2-dependent gene expression. 2 Publications
    Mutagenesisi415 – 4151R → A: Loss of interaction with NFE2L2. Abolishes repression of NFE2L2-dependent gene expression. Loss of interaction with PGAM5. 3 Publications
    Mutagenesisi436 – 4361H → A: Loss of interaction with NFE2L2. Abolishes repression of NFE2L2-dependent gene expression. 2 Publications
    Mutagenesisi478 – 4781F → A: Abolishes repression of NFE2L2-dependent gene expression. 2 Publications
    Mutagenesisi483 – 4831R → A: Loss of interaction with NFE2L2. Abolishes repression of NFE2L2-dependent gene expression. Loss of interaction with PGAM5. 3 Publications
    Mutagenesisi525 – 5251Y → A: Loss of interaction with NFE2L2. Strongly reduces repression of NFE2L2-dependent gene expression. 2 Publications
    Mutagenesisi572 – 5721Y → A: Loss of interaction with NFE2L2. Strongly reduces repression of NFE2L2-dependent gene expression. Loss of interaction with PGAM5. 3 Publications

    Organism-specific databases

    PharmGKBiPA134887774.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 624624Kelch-like ECH-associated protein 1PRO_0000119093Add
    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.2 Publications

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiQ14145.
    PaxDbiQ14145.
    PRIDEiQ14145.

    PTM databases

    PhosphoSiteiQ14145.

    Expressioni

    Tissue specificityi

    Broadly expressed, with highest levels in skeletal muscle.1 Publication

    Gene expression databases

    ArrayExpressiQ14145.
    BgeeiQ14145.
    CleanExiHS_KEAP1.
    GenevestigatoriQ14145.

    Organism-specific databases

    HPAiCAB025337.
    HPA005558.

    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. Interacts with NFE2L1 and MAP1LC3B. Interacts indirectly with ENC1.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DPP3Q9NY332EBI-751001,EBI-718333
    IKBKBO149206EBI-751001,EBI-81266
    IkbkbO883512EBI-751001,EBI-447960From a different organism.
    Irf1P153142EBI-751001,EBI-6115486From a different organism.
    NFE2L2Q1623617EBI-751001,EBI-2007911
    RELAQ042064EBI-751001,EBI-73886
    SQSTM1Q135018EBI-751001,EBI-307104
    Sqstm1Q643372EBI-751001,EBI-645025From a different organism.
    TSC22D4Q9Y3Q83EBI-751001,EBI-739485

    Protein-protein interaction databases

    BioGridi115156. 73 interactions.
    DIPiDIP-42134N.
    IntActiQ14145. 57 interactions.
    MINTiMINT-1197065.
    STRINGi9606.ENSP00000171111.

    Structurei

    Secondary structure

    1
    624
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi327 – 3315
    Beta strandi334 – 3385
    Beta strandi342 – 3454
    Turni347 – 3493
    Beta strandi352 – 3543
    Beta strandi362 – 3643
    Beta strandi366 – 3705
    Beta strandi373 – 3775
    Beta strandi380 – 3834
    Beta strandi386 – 3894
    Beta strandi393 – 3964
    Turni398 – 4003
    Beta strandi403 – 4053
    Beta strandi417 – 4215
    Beta strandi424 – 4285
    Beta strandi440 – 4445
    Turni445 – 4484
    Beta strandi449 – 4524
    Beta strandi464 – 4685
    Beta strandi471 – 4755
    Beta strandi480 – 4834
    Beta strandi487 – 4915
    Turni492 – 4954
    Beta strandi496 – 4994
    Beta strandi511 – 5155
    Beta strandi518 – 5225
    Beta strandi527 – 5304
    Beta strandi534 – 5385
    Turni539 – 5424
    Beta strandi543 – 5475
    Beta strandi558 – 5625
    Beta strandi565 – 5695
    Beta strandi574 – 5774
    Beta strandi580 – 5856
    Turni586 – 5894
    Beta strandi590 – 5967
    Beta strandi605 – 6095

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1U6DX-ray1.85X321-609[»]
    1ZGKX-ray1.35A321-609[»]
    2FLUX-ray1.50X321-609[»]
    3VNGX-ray2.10A321-609[»]
    3VNHX-ray2.10A321-609[»]
    3ZGCX-ray2.20A/B321-609[»]
    3ZGDX-ray1.98A/B321-609[»]
    4CXIX-ray2.35A48-180[»]
    4CXJX-ray2.80A48-180[»]
    4CXTX-ray2.66A48-180[»]
    4IFLX-ray1.80X321-609[»]
    4IFNX-ray2.40X321-609[»]
    4IN4X-ray2.59A/B/C321-609[»]
    4IQKX-ray1.97A321-609[»]
    4L7BX-ray2.41A/B321-609[»]
    4L7CX-ray2.40A/B/C321-609[»]
    4L7DX-ray2.25A/B/C321-609[»]
    4N1BX-ray2.55A/B/C321-609[»]
    ProteinModelPortaliQ14145.
    SMRiQ14145. Positions 59-297, 322-609.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ14145.

    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
    Repeati518 – 56447Kelch 5Add
    BLAST
    Repeati565 – 61147Kelch 6Add
    BLAST

    Motif

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

    Domaini

    The Kelch repeats mediate interaction with NF2L2/NRF2, BPTF and PGAM5.1 Publication

    Sequence similaritiesi

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

    Keywords - Domaini

    Kelch repeat, Repeat

    Phylogenomic databases

    eggNOGiNOG255039.
    HOGENOMiHOG000230814.
    HOVERGENiHBG014286.
    InParanoidiQ14145.
    KOiK10456.
    OMAiQIGCTEL.
    OrthoDBiEOG76739M.
    PhylomeDBiQ14145.
    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.

    Q14145-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQPDPRPSGA GACCRFLPLQ SQCPEGAGDA VMYASTECKA EVTPSQHGNR    50
    TFSYTLEDHT KQAFGIMNEL RLSQQLCDVT LQVKYQDAPA AQFMAHKVVL 100
    ASSSPVFKAM FTNGLREQGM EVVSIEGIHP KVMERLIEFA YTASISMGEK 150
    CVLHVMNGAV MYQIDSVVRA CSDFLVQQLD PSNAIGIANF AEQIGCVELH 200
    QRAREYIYMH FGEVAKQEEF FNLSHCQLVT LISRDDLNVR CESEVFHACI 250
    NWVKYDCEQR RFYVQALLRA VRCHSLTPNF LQMQLQKCEI LQSDSRCKDY 300
    LVKIFEELTL HKPTQVMPCR APKVGRLIYT AGGYFRQSLS YLEAYNPSDG 350
    TWLRLADLQV PRSGLAGCVV GGLLYAVGGR NNSPDGNTDS SALDCYNPMT 400
    NQWSPCAPMS VPRNRIGVGV IDGHIYAVGG SHGCIHHNSV ERYEPERDEW 450
    HLVAPMLTRR IGVGVAVLNR LLYAVGGFDG TNRLNSAECY YPERNEWRMI 500
    TAMNTIRSGA GVCVLHNCIY AAGGYDGQDQ LNSVERYDVE TETWTFVAPM 550
    KHRRSALGIT VHQGRIYVLG GYDGHTFLDS VECYDPDTDT WSEVTRMTSG 600
    RSGVGVAVTM EPCRKQIDQQ NCTC 624
    Length:624
    Mass (Da):69,666
    Last modified:May 1, 2007 - v2
    Checksum:iCE180F3897BB8C97
    GO

    Sequence cautioni

    The sequence BAA09481.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti504 – 5041N → S in BAG51647. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti23 – 231C → Y in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036084
    Natural varianti167 – 1671V → F in a lung adenocarcinoma patient. 1 Publication
    VAR_032102
    Natural varianti236 – 2361D → H in a NSCLC cell line. 1 Publication
    VAR_032103
    Natural varianti284 – 2841Q → L in a lung adenocarcinoma patient. 1 Publication
    VAR_032104
    Natural varianti333 – 3331G → C in a NSCLC cell line; strongly reduces interaction with NFE2L2 and reduces repression of NFE2L2-dependent gene expression. 1 Publication
    VAR_032105
    Natural varianti349 – 3491D → N.1 Publication
    Corresponds to variant rs1048289 [ dbSNP | Ensembl ].
    VAR_032106
    Natural varianti350 – 3501G → S in a NSCLC cell line. 1 Publication
    VAR_032107
    Natural varianti364 – 3641G → C in a lung adenocarcinoma cell line; also in NSCLC cell lines; may be a polymorphism; strongly reduces interaction with NFE2L2 and reduces repression of NFE2L2-dependent gene expression. 1 Publication
    VAR_032108
    Natural varianti430 – 4301G → C in a lung adenocarcinoma patient; somatic mutation; strongly reduces interaction with NFE2L2 and reduces repression of NFE2L2-dependent gene expression. 1 Publication
    VAR_032109
    Natural varianti522 – 5221A → V in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036085

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF361892
    , AF361888, AF361889, AF361890, AF361891 Genomic DNA. Translation: AAK43722.1.
    AF361886 mRNA. Translation: AAK51082.1.
    D50922 mRNA. Translation: BAA09481.3. Different initiation.
    AK056204 mRNA. Translation: BAG51647.1.
    AC011461 Genomic DNA. No translation available.
    BC002417 mRNA. Translation: AAH02417.1.
    BC002930 mRNA. Translation: AAH02930.1.
    BC015945 mRNA. Translation: AAH15945.1.
    BC021957 mRNA. Translation: AAH21957.2.
    CCDSiCCDS12239.1.
    RefSeqiNP_036421.2. NM_012289.3.
    NP_987096.1. NM_203500.1.
    XP_005260230.1. XM_005260173.1.
    XP_005260231.1. XM_005260174.1.
    UniGeneiHs.465870.

    Genome annotation databases

    EnsembliENST00000171111; ENSP00000171111; ENSG00000079999.
    ENST00000393623; ENSP00000377245; ENSG00000079999.
    GeneIDi9817.
    KEGGihsa:9817.
    UCSCiuc002moq.1. human.

    Polymorphism databases

    DMDMi146345444.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF361892
    , AF361888 , AF361889 , AF361890 , AF361891 Genomic DNA. Translation: AAK43722.1 .
    AF361886 mRNA. Translation: AAK51082.1 .
    D50922 mRNA. Translation: BAA09481.3 . Different initiation.
    AK056204 mRNA. Translation: BAG51647.1 .
    AC011461 Genomic DNA. No translation available.
    BC002417 mRNA. Translation: AAH02417.1 .
    BC002930 mRNA. Translation: AAH02930.1 .
    BC015945 mRNA. Translation: AAH15945.1 .
    BC021957 mRNA. Translation: AAH21957.2 .
    CCDSi CCDS12239.1.
    RefSeqi NP_036421.2. NM_012289.3.
    NP_987096.1. NM_203500.1.
    XP_005260230.1. XM_005260173.1.
    XP_005260231.1. XM_005260174.1.
    UniGenei Hs.465870.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1U6D X-ray 1.85 X 321-609 [» ]
    1ZGK X-ray 1.35 A 321-609 [» ]
    2FLU X-ray 1.50 X 321-609 [» ]
    3VNG X-ray 2.10 A 321-609 [» ]
    3VNH X-ray 2.10 A 321-609 [» ]
    3ZGC X-ray 2.20 A/B 321-609 [» ]
    3ZGD X-ray 1.98 A/B 321-609 [» ]
    4CXI X-ray 2.35 A 48-180 [» ]
    4CXJ X-ray 2.80 A 48-180 [» ]
    4CXT X-ray 2.66 A 48-180 [» ]
    4IFL X-ray 1.80 X 321-609 [» ]
    4IFN X-ray 2.40 X 321-609 [» ]
    4IN4 X-ray 2.59 A/B/C 321-609 [» ]
    4IQK X-ray 1.97 A 321-609 [» ]
    4L7B X-ray 2.41 A/B 321-609 [» ]
    4L7C X-ray 2.40 A/B/C 321-609 [» ]
    4L7D X-ray 2.25 A/B/C 321-609 [» ]
    4N1B X-ray 2.55 A/B/C 321-609 [» ]
    ProteinModelPortali Q14145.
    SMRi Q14145. Positions 59-297, 322-609.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115156. 73 interactions.
    DIPi DIP-42134N.
    IntActi Q14145. 57 interactions.
    MINTi MINT-1197065.
    STRINGi 9606.ENSP00000171111.

    Chemistry

    ChEMBLi CHEMBL3038498.

    PTM databases

    PhosphoSitei Q14145.

    Polymorphism databases

    DMDMi 146345444.

    Proteomic databases

    MaxQBi Q14145.
    PaxDbi Q14145.
    PRIDEi Q14145.

    Protocols and materials databases

    DNASUi 9817.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000171111 ; ENSP00000171111 ; ENSG00000079999 .
    ENST00000393623 ; ENSP00000377245 ; ENSG00000079999 .
    GeneIDi 9817.
    KEGGi hsa:9817.
    UCSCi uc002moq.1. human.

    Organism-specific databases

    CTDi 9817.
    GeneCardsi GC19M010596.
    HGNCi HGNC:23177. KEAP1.
    HPAi CAB025337.
    HPA005558.
    MIMi 606016. gene.
    neXtProti NX_Q14145.
    PharmGKBi PA134887774.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG255039.
    HOGENOMi HOG000230814.
    HOVERGENi HBG014286.
    InParanoidi Q14145.
    KOi K10456.
    OMAi QIGCTEL.
    OrthoDBi EOG76739M.
    PhylomeDBi Q14145.
    TreeFami TF329218.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    EvolutionaryTracei Q14145.
    GeneWikii KEAP1.
    GenomeRNAii 9817.
    NextBioi 36968.
    PROi Q14145.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14145.
    Bgeei Q14145.
    CleanExi HS_KEAP1.
    Genevestigatori Q14145.

    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. "Human INrf2 gene structure and nucleotide sequence."
      Dhakshinamoorthy S., Jaiswal A.K.
      Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    2. "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
      DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASN-349.
      Tissue: Bone marrow.
    3. Ohara O., Nagase T., Kikuno R., Nomura N.
      Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    4. "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].
    5. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
      Tissue: Brain, Skin and Uterus.
    7. "Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress."
      Zhang D.D., Hannink M.
      Mol. Cell. Biol. 23:8137-8151(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-151; CYS-273 AND CYS-288, SUBCELLULAR LOCATION.
    8. "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: INTERACTION WITH NF2L2/NRF2 AND BPTF, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    9. "Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex."
      Zhang D.D., Lo S.-C., Cross J.V., Templeton D.J., Hannink M.
      Mol. Cell. Biol. 24:10941-10953(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CUL3 AND RBX1, MUTAGENESIS OF 125-ILE--GLY-127 AND 162-TYR--ILE-164, UBIQUITINATION.
    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: FUNCTION, IDENTIFICATION IN A COMPLEX WITH CUL3 AND RBX1, UBIQUITINATION, ENZYME REGULATION, MUTAGENESIS OF CYS-151.
    11. "Nuclear oncoprotein prothymosin alpha is a partner of Keap1: implications for expression of oxidative stress-protecting genes."
      Karapetian R.N., Evstafieva A.G., Abaeva I.S., Chichkova N.V., Filonov G.S., Rubtsov Y.P., Sukhacheva E.A., Melnikov S.V., Schneider U., Wanker E.E., Vartapetian A.B.
      Mol. Cell. Biol. 25:1089-1099(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTMA, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-308 AND LEU-310.
    12. "Nrf1 is targeted to the endoplasmic reticulum membrane by an N-terminal transmembrane domain. Inhibition of nuclear translocation and transacting function."
      Wang W., Chan J.Y.
      J. Biol. Chem. 281:19676-19687(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NFE2L1.
    13. "PGAM5, a Bcl-XL-interacting protein, is a novel substrate for the redox-regulated Keap1-dependent ubiquitin ligase complex."
      Lo S.-C., Hannink M.
      J. Biol. Chem. 281:37893-37903(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PGAM5, FUNCTION, ENZYME REGULATION, DOMAIN, MUTAGENESIS OF CYS-151; TYR-334; ARG-415; ARG-483 AND TYR-572.
    14. "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 NFE2L2 AND PGAM5.
    15. "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: INTERACTION WITH ENC1, SUBCELLULAR LOCATION.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Autophagy promotes primary ciliogenesis by removing OFD1 from centriolar satellites."
      Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B., Zhong Q.
      Nature 502:254-257(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAP1LC3B.
    18. "Crystallization and initial crystallographic analysis of the Kelch domain from human Keap1."
      Li X., Zhang D., Hannink M., Beamer L.J.
      Acta Crystallogr. D 60:2346-2348(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 321-609.
    19. "Conserved solvent and side-chain interactions in the 1.35 Angstrom structure of the Kelch domain of Keap1."
      Beamer L.J., Li X., Bottoms C.A., Hannink M.
      Acta Crystallogr. D 61:1335-1342(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 321-609.
    20. "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 321-609 IN COMPLEX WITH NFE2L2, SUBUNIT, MUTAGENESIS OF TYR-334; ARG-380; ASN-382; ARG-415; HIS-436; PHE-478; ARG-483; TYR-525 AND TYR-572.
    21. "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: VARIANTS CYS-364 AND CYS-430, CHARACTERIZATION OF VARIANTS CYS-364 AND CYS-430.
    22. Cited for: VARIANTS PHE-167; HIS-236; LEU-284; CYS-333 AND SER-350, CHARACTERIZATION OF VARIANTS HIS-236 AND CYS-333.
    23. Cited for: VARIANTS [LARGE SCALE ANALYSIS] TYR-23 AND VAL-522.

    Entry informationi

    Entry nameiKEAP1_HUMAN
    AccessioniPrimary (citable) accession number: Q14145
    Secondary accession number(s): B3KPD5
    , Q6LEP0, Q8WTX1, Q9BPY9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 150 of the entry and version 2 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 19
      Human chromosome 19: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3