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UniProtKB - Q14145 (KEAP1_HUMAN)

Entry version 209 (12 Aug 2020)
Sequence version 2 (01 May 2007)
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Protein

Kelch-like ECH-associated protein 1

Gene

KEAP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that regulates the response to oxidative stress by targeting NFE2L2/NRF2 for ubiquitination (PubMed:14585973, PubMed:15379550, PubMed:15572695, PubMed:15983046, PubMed:15601839). KEAP1 acts as a key sensor of oxidative and electrophilic stress: in normal conditions, the BCR(KEAP1) complex mediates ubiquitination and degradation of NFE2L2/NRF2, a transcription factor regulating expression of many cytoprotective genes (PubMed:15601839, PubMed:16006525). In response to oxidative stress, different electrophile metabolites trigger non-enzymatic covalent modifications of highly reactive cysteine residues in KEAP1, leading to inactivate the ubiquitin ligase activity of the BCR(KEAP1) complex, promoting NFE2L2/NRF2 nuclear accumulation and expression of phase II detoxifying enzymes (PubMed:19489739, PubMed:16006525, PubMed:17127771, PubMed:18251510, PubMed:29590092). In response to selective autophagy, KEAP1 is sequestered in inclusion bodies following its interaction with SQSTM1/p62, leading to inactivation of the BCR(KEAP1) complex and activation of NFE2L2/NRF2 (PubMed:20452972). The BCR(KEAP1) complex also mediates ubiquitination of SQSTM1/p62, increasing SQSTM1/p62 sequestering activity and degradation (PubMed:28380357). The BCR(KEAP1) complex also targets BPTF and PGAM5 for ubiquitination and degradation by the proteasome (PubMed:15379550, PubMed:17046835).13 Publications

Caution

The mechanism of inactivation of the BCR(KEAP1) complex by covalent modifications of reactive cysteines is unclear. Covalent modifications were initially thought to disrupt interaction between KEAP1 and NFE2L2/NRF2 (By similarity). Recent publications suggest that cysteine modifications disrupt the interaction between KEAP1 and CUL3 without affecting the interaction between KEAP1 and NFE2L2/NRF2 (PubMed:16006525, PubMed:17127771, PubMed:18251510, PubMed:24896564).By similarity4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Ubiquitin ligase activity of the BCR(KEAP1) complex is inhibited by oxidative stress and electrophile metabolites such as sulforaphane (PubMed:15983046, PubMed:17046835, PubMed:29590092, PubMed:30323285). Electrophile metabolites react with reactive cysteine residues in KEAP1 and trigger non-enzymatic covalent modifications of these cysteine residues, leading to inactivate the ubiquitin ligase activity of the BCR(KEAP1) complex (PubMed:19489739, PubMed:17127771, PubMed:18251510, PubMed:29590092, PubMed:30323285). Selective autophagy also inactivates the BCR(KEAP1) complex via interaction between KEAP1 and SQSTM1/p62, which sequesters the complex in inclusion bodies and promotes its degradation (PubMed:20495340, PubMed:20452972).9 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.5 Publications
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei151Sensor for electrophilic agents2 Publications1
Sitei257Sensor for electrophilic agents1 Publication1
Sitei273Sensor for electrophilic agents1 Publication1
Sitei288Sensor for electrophilic agents1 Publication1
Sitei434Sensor for electrophilic agentsBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processHost-virus interaction, Ubl conjugation pathway

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q14145

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-5689880, Ub-specific processing proteases
R-HSA-8951664, Neddylation
R-HSA-983168, Antigen processing: Ubiquitination & Proteasome degradation

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q14145

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00143

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Kelch-like ECH-associated protein 11 Publication
Alternative name(s):
Cytosolic inhibitor of Nrf21 Publication
Short name:
INrf21 Publication
Kelch-like protein 19Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:KEAP11 PublicationImported
Synonyms:INRF21 Publication, KIAA01321 Publication, KLHL19Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 19

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000079999.13

Human Gene Nomenclature Database

More...HGNCi		HGNC:23177, KEAP1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		606016, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q14145

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi15R → A: Reduced formation of a high-molecular mass KEAP1 molecule when methylglyoxal accumulates. 1 Publication1
Mutagenesisi123 – 127VSIEG → ASAEA: Abolished interaction with NFE2L2/NRF2; when associated with 161-A-A-162. 1 Publication5
Mutagenesisi125 – 127IEG → AAA: Increases ubiquitination and proteolytic degradation. 1 Publication3
Mutagenesisi135R → A: Reduced formation of a high-molecular mass KEAP1 molecule when methylglyoxal accumulates. 1 Publication1
Mutagenesisi151C → S, N, D or L: Substitution with a small side chain that prevents covalent modification by an electrophile; promotes constitutive ubiquitination of NFE2L2/NRF2 and subsequent repression of phase 2 detoxifying enzymes. Resistance of ubiquitination of PGAM5 to inhibition by oxidative stress and sulforaphane. Impaired interaction with CUL3. Reduced formation of a high-molecular mass KEAP1 molecule when methylglyoxal accumulates. 7 Publications1
Mutagenesisi151C → W or Y: Substitution with a bulky side chain that mimicks covalent modification by an electrophile; prevents ubiquitination and degradation of NFE2L2/NRF2, leading to constitutive activation of NFE2L2/NRF2 and subsequent expression of phase 2 detoxifying enzymes. 2 Publications1
Mutagenesisi161 – 162MY → AA: Abolished interaction with NFE2L2/NRF2; when associated with 123-A--A-127. 1 Publication2
Mutagenesisi162 – 164YQI → AAA: Increases ubiquitination and proteolytic degradation. 1 Publication3
Mutagenesisi273C → S: Abolishes repression of NFE2L2/NRF2-dependent gene expression. Slows down degradation of NFE2L2/NRF2. 1 Publication1
Mutagenesisi288C → S: Abolishes repression of NFE2L2/NRF2-dependent gene expression. Slows down degradation of NFE2L2/NRF2. 1 Publication1
Mutagenesisi308L → A: Loss of export from nucleus; when associated with A-310. 1 Publication1
Mutagenesisi310L → A: Loss of export from nucleus; when associated with A-308. 1 Publication1
Mutagenesisi334Y → A: Loss of interaction with NFE2L2/NRF2. Strongly reduces repression of NFE2L2/NRF2-dependent gene expression. Loss of interaction with PGAM5. 2 Publications1
Mutagenesisi380R → A: Loss of interaction with NFE2L2/NRF2. Abolishes repression of NFE2L2/NRF2-dependent gene expression. Impaired interaction with SQSTM1/p62. 2 Publications1
Mutagenesisi382N → A: Loss of interaction with NFE2L2/NRF2. Strongly reduces repression of NFE2L2/NRF2-dependent gene expression. Impaired interaction with SQSTM1/p62. 2 Publications1
Mutagenesisi415R → A: Loss of interaction with NFE2L2/NRF2. Abolishes repression of NFE2L2/NRF2-dependent gene expression. Loss of interaction with PGAM5. Does not affect interaction with SQSTM1/p62. 3 Publications1
Mutagenesisi436H → A: Loss of interaction with NFE2L2/NRF2. Abolishes repression of NFE2L2/NRF2-dependent gene expression. Does not affect interaction with SQSTM1/p62. 2 Publications1
Mutagenesisi478F → A: Abolishes repression of NFE2L2/NRF2-dependent gene expression. 1 Publication1
Mutagenesisi483R → A: Loss of interaction with NFE2L2/NRF2. Abolishes repression of NFE2L2/NRF2-dependent gene expression. Loss of interaction with PGAM5. Does not affect interaction with SQSTM1/p62. 3 Publications1
Mutagenesisi525Y → A: Loss of interaction with NFE2L2/NRF2. Strongly reduces repression of NFE2L2/NRF2-dependent gene expression. Abolishes interaction with SQSTM1/p62. 2 Publications1
Mutagenesisi572Y → A: Loss of interaction with NFE2L2/NRF2. Strongly reduces repression of NFE2L2/NRF2-dependent gene expression. Loss of interaction with PGAM5. Abolishes interaction with SQSTM1/p62. 3 Publications1

Organism-specific databases

DisGeNET

More...DisGeNETi		9817

MalaCards human disease database

More...MalaCardsi		KEAP1

Open Targets

More...OpenTargetsi		ENSG00000079999

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		276399, Familial multinodular goiter

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA134887774

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q14145, Tclin

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2069156

Drug and drug target database

More...DrugBanki		DB08908, Dimethyl fumarate

DrugCentral

More...DrugCentrali		Q14145

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2757

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		KEAP1

Domain mapping of disease mutations (DMDM)

More...DMDMi		146345444

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001190931 – 624Kelch-like ECH-associated protein 1Add BLAST624

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei38S-(2-succinyl)cysteineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki135N5-[4-(S-L-cysteinyl)-5-methyl-1H-imidazol-2-yl]-L-ornithine (Arg-Cys) (interchain with C-151 in KEAP1)1 Publication
Modified residuei151S-(2,3-dicarboxypropyl)cysteine; alternate1 Publication1
Modified residuei151S-(2-succinyl)cysteine; alternateBy similarity1
Modified residuei151S-nitrosocysteine; alternateBy similarity1
Cross-linki151N5-[4-(S-L-cysteinyl)-5-methyl-1H-imidazol-2-yl]-L-ornithine (Cys-Arg) (interchain with R-135 in KEAP1)1 Publication
Modified residuei241S-(2-succinyl)cysteineBy similarity1
Modified residuei257S-(2,3-dicarboxypropyl)cysteine1 Publication1
Modified residuei273S-(2,3-dicarboxypropyl)cysteine1 Publication1
Modified residuei288S-(2,3-dicarboxypropyl)cysteine; alternate1 Publication1
Modified residuei288S-(2-succinyl)cysteine; alternateBy similarity1
Modified residuei319S-(2-succinyl)cysteineBy similarity1
Modified residuei434S-cGMP-cysteineBy similarity1
Modified residuei613S-(2-succinyl)cysteineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Non-enzymatic covalent modifications of reactive cysteines by electrophile metabolites inactivate the BCR(KEAP1) complex (PubMed:17127771, PubMed:18251510, PubMed:29590092, PubMed:30323285). Accumulation of fumarate promotes the formation of cysteine S-succination (S-(2-succinyl)cysteine), leading to inactivate the BCR(KEAP1) complex and promote NFE2L2/NRF2 nuclear accumulation and activation (By similarity). Nitric oxide-dependent 8-Nitro-cGMP formation promotes cysteine guanylation (S-cGMP-cysteine), leading to NFE2L2/NRF2 nuclear accumulation and activation (By similarity). Itaconate, an anti-inflammatory metabolite generated in response to lipopolysaccharide, alkylates cysteines, activating NFE2L2/NRF2 (PubMed:29590092). Methylglyoxal, a reactive metabolite that accumulates when the glycolytic enzyme PGK1 is inhibited, promotes formation of a methylimidazole cross-link between proximal Cys-151 and Arg-135 on another KEAP1 molecule, resulting in an inactive dimer that inactivates the BCR(KEAP1) complex (PubMed:30323285).By similarity4 Publications
Degraded via a proteasomal-independent process during selective autophagy: interaction with phosphorylated SQSTM1/p62 sequesters KEAP1 in inclusion bodies, leading to its degradation.2 Publications
Auto-ubiquitinated by the BCR(KEAP1) complex (PubMed:15572695, PubMed:15983046). Quinone-induced oxidative stress, but not sulforaphane, increases its ubiquitination (PubMed:15572695, PubMed:15983046). 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 (PubMed:15572695, PubMed:15983046).2 Publications

Keywords - PTMi

S-nitrosylation, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q14145

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q14145

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q14145

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q14145

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q14145

PeptideAtlas

More...PeptideAtlasi		Q14145

PRoteomics IDEntifications database

More...PRIDEi		Q14145

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		59849

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q14145

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q14145

SwissPalm database of S-palmitoylation events

More...SwissPalmi		Q14145

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000079999, Expressed in hindlimb stylopod muscle and 244 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q14145, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q14145, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000079999, Low tissue specificity

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the BCR(KEAP1) E3 ubiquitin ligase complex, at least composed of 2 molecules of CUL3, 2 molecules of KEAP1, and RBX1 (PubMed:15572695, PubMed:15983046, PubMed:15601839, PubMed:17127771, PubMed:18251510, PubMed:24896564).

Interacts with NFE2L2/NRF2; the interaction is direct (PubMed:15379550, PubMed:15601839, PubMed:16006525, PubMed:18387606, PubMed:16888629).

Forms a ternary complex with NFE2L2/NRF2 and PGAM5 (PubMed:17046835).

Interacts with (phosphorylated) SQSTM1/p62; the interaction is direct and inactivates the BCR(KEAP1) complex by sequestering it in inclusion bodies, promoting its degradation (PubMed:20495340, PubMed:20452972).

Interacts with NFE2L1 (PubMed:16687406).

Interacts with BPTF and PTMA (PubMed:15657435).

Interacts with MAP1LC3B (PubMed:24089205).

Interacts indirectly with ENC1 (PubMed:19424503).

Interacts with SESN1 and SESN2 (PubMed:23274085).

Interacts with HSP90AA1 and HSP90AB1 (PubMed:26517842).

19 Publications

(Microbial infection) Interacts with ebolavirus protein VP24; this interaction activates transcription factor NFE2L2/NRF2 by blocking its interaction with KEAP1.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Q14145
With#Exp.IntAct
AMER1 [Q5JTC6]2EBI-751001,EBI-6169747
ANKS1A [Q49AR9]3EBI-751001,EBI-11954519
ASPA [P45381]4EBI-751001,EBI-750475
ATG5 [A9UGY9]3EBI-751001,EBI-10175276
ATG5 [Q9H1Y0]3EBI-751001,EBI-1047414
C2orf68 [Q2NKX9]3EBI-751001,EBI-11603468
CARD10 [Q9BWT7]3EBI-751001,EBI-3866279
CCNB1IP1 [Q9NPC3]4EBI-751001,EBI-745269
COL1A1 [P02452]3EBI-751001,EBI-982999
COL2A1 - isoform 1 [P02458-1]3EBI-751001,EBI-12375799
CSNK2A1 [P68400]3EBI-751001,EBI-347804
CUL3 [Q13618]5EBI-751001,EBI-456129
DPP3 [Q9NY33]8EBI-751001,EBI-718333
EAF1 [Q96JC9]3EBI-751001,EBI-769261
ERICH5 [Q6P6B1]3EBI-751001,EBI-11343491
ETF1 [P62495]8EBI-751001,EBI-750990
FAM117B [Q6P1L5]6EBI-751001,EBI-3893327
GPErik [Q14440]3EBI-751001,EBI-10232920
GPR151 [Q8TDV0]3EBI-751001,EBI-11955647
GYPA [A0A0C4DFT7]3EBI-751001,EBI-12044847
GYPA [B8Q183]4EBI-751001,EBI-10176190
GYPA [P02724]4EBI-751001,EBI-702665
ICAM1 [P05362]3EBI-751001,EBI-1035358
IFIH1 [Q9BYX4]3EBI-751001,EBI-6115771
IKBKB [O14920]6EBI-751001,EBI-81266
IQCC [Q4KMZ1]3EBI-751001,EBI-12206419
KLHL2 [O95198]3EBI-751001,EBI-746999
KLHL3 [Q8N4I8]3EBI-751001,EBI-10230467
KLHL3 [Q9UH77]3EBI-751001,EBI-8524663
LSM3 [P62310]6EBI-751001,EBI-348239
MAD2L1 [Q13257]8EBI-751001,EBI-78203
MAPKBP1 [O60336]3EBI-751001,EBI-947402
MCMBP - isoform 2 [Q9BTE3-2]3EBI-751001,EBI-9384556
NFE2L2 [Q16236]24EBI-751001,EBI-2007911
NUDT4 [Q9NZJ9]3EBI-751001,EBI-4280066
NUP50 [Q9UKX7]3EBI-751001,EBI-2371082
OXR1 - isoform 5 [Q8N573-5]3EBI-751001,EBI-10265887
PALB2 [Q86YC2]4EBI-751001,EBI-1222653
PRKAG1 [P54619]6EBI-751001,EBI-1181439
PTMA - isoform 2 [P06454-2]6EBI-751001,EBI-10194874
RECK [Q6P9E2]6EBI-751001,EBI-10253121
RELA [Q04206]4EBI-751001,EBI-73886
SESN2 [P58004]3EBI-751001,EBI-3939642
SMARCD1 [Q96GM5]3EBI-751001,EBI-358489
SQSTM1 [Q13501]17EBI-751001,EBI-307104
STAP2 [Q9UGK3]3EBI-751001,EBI-1553984
TBC1D7 [Q9P0N9]3EBI-751001,EBI-3258000
TERF1 [P54274]2EBI-751001,EBI-710997
TSC22D4 [Q9Y3Q8]3EBI-751001,EBI-739485
WDR83 [Q9BRX9]7EBI-751001,EBI-7705033
WDYHV1 [Q96HA8]3EBI-751001,EBI-741158
WHRN [Q9P202]3EBI-751001,EBI-310886
ZNF121 [P58317]3EBI-751001,EBI-1228269
ZSCAN32 [Q9NX65]3EBI-751001,EBI-739949
Ikbkb [O88351] from Mus musculus.2EBI-751001,EBI-447960
Irf1 [P15314] from Mus musculus.2EBI-751001,EBI-6115486
Sqstm1 [Q64337] from Mus musculus.2EBI-751001,EBI-645025

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		115156, 166 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q14145

Database of interacting proteins

More...DIPi		DIP-42134N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		Q14145

Protein interaction database and analysis system

More...IntActi		Q14145, 140 interactors

Molecular INTeraction database

More...MINTi		Q14145

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000171111

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q14145

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q14145, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1624
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q14145

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q14145

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini77 – 149BTBPROSITE-ProRule annotationAdd BLAST73
Domaini184 – 286BACKAdd BLAST103
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati327 – 372Kelch 1Add BLAST46
Repeati373 – 423Kelch 2Add BLAST51
Repeati424 – 470Kelch 3Add BLAST47
Repeati471 – 517Kelch 4Add BLAST47
Repeati518 – 564Kelch 5Add BLAST47
Repeati565 – 611Kelch 6Add BLAST47

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

KEAP1 contains reactive cysteine residues that act as sensors for endogenously produced and exogenously encountered small molecules, which react with sulfhydryl groups and modify the cysteine sensors, leading to impair ability of the BCR(KEAP1) complex to ubiquitinate target proteins.5 Publications
The Kelch repeats mediate interaction with NFE2L2/NRF2, BPTF and PGAM5.1 Publication

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the KEAP1 family.Curated

Keywords - Domaini

Kelch repeat, Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG4441, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000159543

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_004253_14_2_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q14145

KEGG Orthology (KO)

More...KOi		K10456

Identification of Orthologs from Complete Genome Data

More...OMAi		CYHPEND

Database of Orthologous Groups

More...OrthoDBi		746011at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q14145

TreeFam database of animal gene trees

More...TreeFami		TF329218

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.120.10.80, 1 hit

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID00384

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR011705, BACK
IPR017096, BTB-kelch_protein
IPR000210, BTB/POZ_dom
IPR030563, KEAP1
IPR015915, Kelch-typ_b-propeller
IPR006652, Kelch_1
IPR011333, SKP1/BTB/POZ_sf

The PANTHER Classification System

More...PANTHERi		PTHR24412:SF162, PTHR24412:SF162, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF07707, BACK, 1 hit
PF00651, BTB, 1 hit
PF01344, Kelch_1, 6 hits

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF037037, Kelch-like_protein_gigaxonin, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00875, BACK, 1 hit
SM00225, BTB, 1 hit
SM00612, Kelch, 6 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF117281, SSF117281, 1 hit
SSF54695, SSF54695, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50097, BTB, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 6 potential isoforms that are computationally mapped.Show allAlign All

Q14145-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQPDPRPSGA GACCRFLPLQ SQCPEGAGDA VMYASTECKA EVTPSQHGNR 
        60         70         80         90        100
TFSYTLEDHT KQAFGIMNEL RLSQQLCDVT LQVKYQDAPA AQFMAHKVVL 
       110        120        130        140        150
ASSSPVFKAM FTNGLREQGM EVVSIEGIHP KVMERLIEFA YTASISMGEK 
       160        170        180        190        200
CVLHVMNGAV MYQIDSVVRA CSDFLVQQLD PSNAIGIANF AEQIGCVELH 
       210        220        230        240        250
QRAREYIYMH FGEVAKQEEF FNLSHCQLVT LISRDDLNVR CESEVFHACI 
       260        270        280        290        300
NWVKYDCEQR RFYVQALLRA VRCHSLTPNF LQMQLQKCEI LQSDSRCKDY 
       310        320        330        340        350
LVKIFEELTL HKPTQVMPCR APKVGRLIYT AGGYFRQSLS YLEAYNPSDG 
       360        370        380        390        400
TWLRLADLQV PRSGLAGCVV GGLLYAVGGR NNSPDGNTDS SALDCYNPMT 
       410        420        430        440        450
NQWSPCAPMS VPRNRIGVGV IDGHIYAVGG SHGCIHHNSV ERYEPERDEW 
       460        470        480        490        500
HLVAPMLTRR IGVGVAVLNR LLYAVGGFDG TNRLNSAECY YPERNEWRMI 
       510        520        530        540        550
TAMNTIRSGA GVCVLHNCIY AAGGYDGQDQ LNSVERYDVE TETWTFVAPM 
       560        570        580        590        600
KHRRSALGIT VHQGRIYVLG GYDGHTFLDS VECYDPDTDT WSEVTRMTSG 
       610        620 
RSGVGVAVTM EPCRKQIDQQ NCTC
Length:624
Mass (Da):69,666
Last modified:May 1, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iCE180F3897BB8C97
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
K7EJ49K7EJ49_HUMAN
Kelch-like ECH-associated protein 1
KEAP1
212Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7ESE0K7ESE0_HUMAN
Kelch-like ECH-associated protein 1
KEAP1
279Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7EJD8K7EJD8_HUMAN
Kelch-like ECH-associated protein 1
KEAP1
213Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7EQX2K7EQX2_HUMAN
Kelch-like ECH-associated protein 1
KEAP1
172Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7EMY1K7EMY1_HUMAN
Kelch-like ECH-associated protein 1
KEAP1
129Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7EPZ3K7EPZ3_HUMAN
Kelch-like ECH-associated protein 1
KEAP1
116Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAA09481 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti504N → S in BAG51647 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_03608423C → Y in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_032102167V → F in a lung adenocarcinoma patient. 1 Publication1
Natural variantiVAR_032103236D → H in a NSCLC cell line. 1 Publication1
Natural variantiVAR_032104284Q → L in a lung adenocarcinoma patient. 1 Publication1
Natural variantiVAR_032105333G → C in a NSCLC cell line; strongly reduces interaction with NFE2L2/NRF2 and reduces repression of NFE2L2/NRF2-dependent gene expression. 1 Publication1
Natural variantiVAR_032106349D → N1 PublicationCorresponds to variant dbSNP:rs1048289Ensembl.1
Natural variantiVAR_032107350G → S in a NSCLC cell line. 1 PublicationCorresponds to variant dbSNP:rs777308626Ensembl.1
Natural variantiVAR_032108364G → C in a lung adenocarcinoma cell line; also in NSCLC cell lines; may be a polymorphism; strongly reduces interaction with NFE2L2/NRF2 and reduces repression of NFE2L2/NRF2-dependent gene expression. 1 PublicationCorresponds to variant dbSNP:rs1397945617Ensembl.1
Natural variantiVAR_032109430G → C in a lung adenocarcinoma patient; somatic mutation; strongly reduces interaction with NFE2L2/NRF2 and reduces repression of NFE2L2/NRF2-dependent gene expression. 1 Publication1
Natural variantiVAR_036085522A → V in a breast cancer sample; somatic mutation. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AF361892 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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS12239.1

NCBI Reference Sequences

More...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
XP_011526754.1, XM_011528452.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000171111; ENSP00000171111; ENSG00000079999
ENST00000393623; ENSP00000377245; ENSG00000079999

Database of genes from NCBI RefSeq genomes

More...GeneIDi		9817

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:9817

UCSC genome browser

More...UCSCi		uc002moq.2, human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF361892 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
XP_011526754.1, XM_011528452.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB 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[»]
4IFJX-ray1.80A321-609[»]
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[»]
4XMBX-ray2.43A321-609[»]
5DADX-ray2.61A49-182[»]
5DAFX-ray2.37A49-182[»]
5F72X-ray1.85C/K321-611[»]
5GITX-ray2.19A48-180[»]
5NLBX-ray3.45A51-204[»]
5WFLX-ray1.93A/B312-624[»]
5WFVX-ray1.91A/B320-612[»]
5WG1X-ray2.02A/B320-612[»]
5WHLX-ray2.50A/B312-624[»]
5WHOX-ray2.23A/B312-624[»]
5WIYX-ray2.23A/B312-624[»]
5X54X-ray2.30A/B321-609[»]
6FFMX-ray2.20A48-180[»]
6FMPX-ray2.92A/B321-609[»]
6FMQX-ray2.10A/B321-609[»]
6HWSX-ray1.75A321-609[»]
6ROGX-ray2.16A/X321-609[»]
6TYMX-ray1.42A321-609[»]
6TYPX-ray2.50A321-609[»]
6UF0X-ray1.96A/B321-609[»]
6V6ZX-ray1.60A/B/C/D321-609[»]
SMRiQ14145
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi115156, 166 interactors
CORUMiQ14145
DIPiDIP-42134N
ELMiQ14145
IntActiQ14145, 140 interactors
MINTiQ14145
STRINGi9606.ENSP00000171111

Chemistry databases

BindingDBiQ14145
ChEMBLiCHEMBL2069156
DrugBankiDB08908, Dimethyl fumarate
DrugCentraliQ14145
GuidetoPHARMACOLOGYi2757

PTM databases

iPTMnetiQ14145
PhosphoSitePlusiQ14145
SwissPalmiQ14145

Polymorphism and mutation databases

BioMutaiKEAP1
DMDMi146345444

Proteomic databases

EPDiQ14145
jPOSTiQ14145
MassIVEiQ14145
MaxQBiQ14145
PaxDbiQ14145
PeptideAtlasiQ14145
PRIDEiQ14145
ProteomicsDBi59849

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		Q14145, 5 sequenced antibodies

Antibodypedia a portal for validated antibodies

More...Antibodypediai		1418, 670 antibodies

The DNASU plasmid repository

More...DNASUi		9817

Genome annotation databases

EnsembliENST00000171111; ENSP00000171111; ENSG00000079999
ENST00000393623; ENSP00000377245; ENSG00000079999
GeneIDi9817
KEGGihsa:9817
UCSCiuc002moq.2, human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		9817
DisGeNETi9817
EuPathDBiHostDB:ENSG00000079999.13

GeneCards: human genes, protein and diseases

More...GeneCardsi		KEAP1
HGNCiHGNC:23177, KEAP1
HPAiENSG00000079999, Low tissue specificity
MalaCardsiKEAP1
MIMi606016, gene
neXtProtiNX_Q14145
OpenTargetsiENSG00000079999
Orphaneti276399, Familial multinodular goiter
PharmGKBiPA134887774

Human Unidentified Gene-Encoded large proteins database

More...HUGEi		Search...

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG4441, Eukaryota
GeneTreeiENSGT00940000159543
HOGENOMiCLU_004253_14_2_1
InParanoidiQ14145
KOiK10456
OMAiCYHPEND
OrthoDBi746011at2759
PhylomeDBiQ14145
TreeFamiTF329218

Enzyme and pathway databases

UniPathwayiUPA00143
PathwayCommonsiQ14145
ReactomeiR-HSA-5689880, Ub-specific processing proteases
R-HSA-8951664, Neddylation
R-HSA-983168, Antigen processing: Ubiquitination & Proteasome degradation
SIGNORiQ14145

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		9817, 136 hits in 892 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		KEAP1, human
EvolutionaryTraceiQ14145

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		KEAP1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		9817
PharosiQ14145, Tclin

Protein Ontology

More...PROi		PR:Q14145
RNActiQ14145, protein

The Stanford Online Universal Resource for Clones and ESTs

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Gene expression databases

BgeeiENSG00000079999, Expressed in hindlimb stylopod muscle and 244 other tissues
ExpressionAtlasiQ14145, baseline and differential
GenevisibleiQ14145, HS

Family and domain databases

Gene3Di2.120.10.80, 1 hit
IDEALiIID00384
InterProiView protein in InterPro
IPR011705, BACK
IPR017096, BTB-kelch_protein
IPR000210, BTB/POZ_dom
IPR030563, KEAP1
IPR015915, Kelch-typ_b-propeller
IPR006652, Kelch_1
IPR011333, SKP1/BTB/POZ_sf
PANTHERiPTHR24412:SF162, PTHR24412:SF162, 1 hit
PfamiView protein in Pfam
PF07707, BACK, 1 hit
PF00651, BTB, 1 hit
PF01344, Kelch_1, 6 hits
PIRSFiPIRSF037037, Kelch-like_protein_gigaxonin, 1 hit
SMARTiView protein in SMART
SM00875, BACK, 1 hit
SM00225, BTB, 1 hit
SM00612, Kelch, 6 hits
SUPFAMiSSF117281, SSF117281, 1 hit
SSF54695, SSF54695, 1 hit
PROSITEiView protein in PROSITE
PS50097, BTB, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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MobiDB: a database of protein disorder and mobility annotations

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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiKEAP1_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q14145
Secondary accession number(s): B3KPD5
, Q6LEP0, Q8WTX1, Q9BPY9
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 2007
Last modified: August 12, 2020
This is version 209 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, 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
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