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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-Experimental evidence at protein leveli

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: protein ubiquitination

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

GO - Molecular functioni

  • transcription factor binding Source: ParkinsonsUK-UCL

GO - Biological processi

Keywordsi

Biological processTranscription, Transcription regulation, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-HSA-5689880. Ub-specific processing proteases.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SIGNORiQ14145.
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
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:23177. KEAP1.

Subcellular locationi

GO - Cellular componenti

  • actin filament Source: Ensembl
  • Cul3-RING ubiquitin ligase complex Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: ParkinsonsUK-UCL
  • endoplasmic reticulum Source: Ensembl
  • microtubule organizing center Source: HPA
  • midbody Source: UniProtKB
  • nucleoplasm Source: HPA

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi125 – 127IEG → AAA: Increases ubiquitination and proteolytic degradation. 1 Publication3
Mutagenesisi151C → 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. 3 Publications1
Mutagenesisi162 – 164YQI → AAA: Increases ubiquitination and proteolytic degradation. 1 Publication3
Mutagenesisi273C → S: Abolishes repression of NFE2L2-dependent gene expression. Slows down degradation of NFE2L2. 1 Publication1
Mutagenesisi288C → S: Abolishes repression of NFE2L2-dependent gene expression. Slows down degradation of NFE2L2. 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. Strongly reduces repression of NFE2L2-dependent gene expression. Loss of interaction with PGAM5. 2 Publications1
Mutagenesisi380R → A: Loss of interaction with NFE2L2. Abolishes repression of NFE2L2-dependent gene expression. 1 Publication1
Mutagenesisi382N → A: Loss of interaction with NFE2L2. Strongly reduces repression of NFE2L2-dependent gene expression. 1 Publication1
Mutagenesisi415R → A: Loss of interaction with NFE2L2. Abolishes repression of NFE2L2-dependent gene expression. Loss of interaction with PGAM5. 2 Publications1
Mutagenesisi436H → A: Loss of interaction with NFE2L2. Abolishes repression of NFE2L2-dependent gene expression. 1 Publication1
Mutagenesisi478F → A: Abolishes repression of NFE2L2-dependent gene expression. 1 Publication1
Mutagenesisi483R → A: Loss of interaction with NFE2L2. Abolishes repression of NFE2L2-dependent gene expression. Loss of interaction with PGAM5. 2 Publications1
Mutagenesisi525Y → A: Loss of interaction with NFE2L2. Strongly reduces repression of NFE2L2-dependent gene expression. 1 Publication1
Mutagenesisi572Y → A: Loss of interaction with NFE2L2. Strongly reduces repression of NFE2L2-dependent gene expression. Loss of interaction with PGAM5. 2 Publications1

Organism-specific databases

DisGeNETi9817.
OpenTargetsiENSG00000079999.
PharmGKBiPA134887774.

Chemistry databases

ChEMBLiCHEMBL2069156.
DrugBankiDB08908. Dimethyl fumarate.
GuidetoPHARMACOLOGYi2757.

Polymorphism and mutation databases

BioMutaiKEAP1.
DMDMi146345444.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001190931 – 624Kelch-like ECH-associated protein 1Add BLAST624

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

EPDiQ14145.
MaxQBiQ14145.
PaxDbiQ14145.
PeptideAtlasiQ14145.
PRIDEiQ14145.

PTM databases

iPTMnetiQ14145.
PhosphoSitePlusiQ14145.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000079999.
CleanExiHS_KEAP1.
ExpressionAtlasiQ14145. baseline and differential.
GenevisibleiQ14145. HS.

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. Interacts with SESN1 and SESN2 (PubMed:23274085). Interacts with HSP90AA1 and HSP90AB1 (PubMed:26517842).12 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • transcription factor binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi115156. 116 interactors.
DIPiDIP-42134N.
IntActiQ14145. 122 interactors.
MINTiMINT-1197065.
STRINGi9606.ENSP00000171111.

Chemistry databases

BindingDBiQ14145.

Structurei

Secondary structure

1624
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi59 – 73Combined sources15
Beta strandi79 – 85Combined sources7
Beta strandi88 – 95Combined sources8
Helixi97 – 103Combined sources7
Helixi105 – 111Combined sources7
Beta strandi121 – 128Combined sources8
Helixi130 – 142Combined sources13
Turni149 – 151Combined sources3
Helixi152 – 162Combined sources11
Helixi165 – 177Combined sources13
Beta strandi327 – 331Combined sources5
Beta strandi334 – 338Combined sources5
Beta strandi342 – 345Combined sources4
Turni347 – 349Combined sources3
Beta strandi352 – 354Combined sources3
Beta strandi362 – 364Combined sources3
Beta strandi366 – 370Combined sources5
Beta strandi373 – 377Combined sources5
Beta strandi380 – 383Combined sources4
Beta strandi386 – 389Combined sources4
Beta strandi393 – 396Combined sources4
Turni398 – 400Combined sources3
Beta strandi403 – 405Combined sources3
Beta strandi417 – 421Combined sources5
Beta strandi424 – 428Combined sources5
Beta strandi440 – 444Combined sources5
Turni445 – 448Combined sources4
Beta strandi449 – 452Combined sources4
Beta strandi464 – 468Combined sources5
Beta strandi471 – 475Combined sources5
Beta strandi480 – 483Combined sources4
Beta strandi487 – 491Combined sources5
Turni492 – 495Combined sources4
Beta strandi496 – 499Combined sources4
Beta strandi511 – 515Combined sources5
Beta strandi518 – 522Combined sources5
Beta strandi527 – 530Combined sources4
Beta strandi534 – 538Combined sources5
Turni539 – 542Combined sources4
Beta strandi543 – 547Combined sources5
Beta strandi558 – 562Combined sources5
Beta strandi565 – 569Combined sources5
Beta strandi574 – 577Combined sources4
Beta strandi580 – 585Combined sources6
Turni586 – 589Combined sources4
Beta strandi590 – 596Combined sources7
Beta strandi605 – 609Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliQ14145.
SMRiQ14145.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14145.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini77 – 149BTBPROSITE-ProRule annotationAdd BLAST73
Domaini184 – 286BACKAdd BLAST103
Repeati327 – 372Kelch 1Add BLAST46
Repeati373 – 423Kelch 2Add BLAST51
Repeati424 – 470Kelch 3Add BLAST47
Repeati471 – 517Kelch 4Add BLAST47
Repeati518 – 564Kelch 5Add BLAST47
Repeati565 – 611Kelch 6Add BLAST47

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi301 – 310Nuclear export signal10

Domaini

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

Keywords - Domaini

Kelch repeat, Repeat

Phylogenomic databases

eggNOGiKOG4441. Eukaryota.
ENOG410XNX8. LUCA.
GeneTreeiENSGT00760000118931.
HOGENOMiHOG000230814.
HOVERGENiHBG014286.
InParanoidiQ14145.
KOiK10456.
OMAiHTQFLPL.
OrthoDBiEOG091G02T3.
PhylomeDBiQ14145.
TreeFamiTF329218.

Family and domain databases

Gene3Di2.120.10.80. 1 hit.
2.130.10.80. 1 hit.
InterProiView protein in InterPro
IPR011705. BACK.
IPR017096. BTB-kelch_protein.
IPR000210. BTB/POZ_dom.
IPR015916. Gal_Oxidase_b-propeller.
IPR030563. KEAP1.
IPR015915. Kelch-typ_b-propeller.
IPR006652. Kelch_1.
IPR011333. SKP1/BTB/POZ.
PANTHERiPTHR24412:SF341. PTHR24412:SF341. 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.
SUPFAMiSSF54695. SSF54695. 1 hit.
PROSITEiView protein in PROSITE
PS50097. BTB. 1 hit.

Sequencei

Sequence statusi: Complete.

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
Checksum:iCE180F3897BB8C97
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti504N → S in BAG51647 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 and reduces repression of NFE2L2-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 and reduces repression of NFE2L2-dependent gene expression. 1 Publication1
Natural variantiVAR_032109430G → C in a lung adenocarcinoma patient; somatic mutation; strongly reduces interaction with NFE2L2 and reduces repression of NFE2L2-dependent gene expression. 1 Publication1
Natural variantiVAR_036085522A → V in a breast cancer sample; somatic mutation. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
XP_011526754.1. XM_011528452.1.
UniGeneiHs.465870.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
XP_011526754.1. XM_011528452.1.
UniGeneiHs.465870.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliQ14145.
SMRiQ14145.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115156. 116 interactors.
DIPiDIP-42134N.
IntActiQ14145. 122 interactors.
MINTiMINT-1197065.
STRINGi9606.ENSP00000171111.

Chemistry databases

BindingDBiQ14145.
ChEMBLiCHEMBL2069156.
DrugBankiDB08908. Dimethyl fumarate.
GuidetoPHARMACOLOGYi2757.

PTM databases

iPTMnetiQ14145.
PhosphoSitePlusiQ14145.

Polymorphism and mutation databases

BioMutaiKEAP1.
DMDMi146345444.

Proteomic databases

EPDiQ14145.
MaxQBiQ14145.
PaxDbiQ14145.
PeptideAtlasiQ14145.
PRIDEiQ14145.

Protocols and materials databases

DNASUi9817.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi9817.
DisGeNETi9817.
GeneCardsiKEAP1.
HGNCiHGNC:23177. KEAP1.
HPAiCAB025337.
HPA005558.
MIMi606016. gene.
neXtProtiNX_Q14145.
OpenTargetsiENSG00000079999.
PharmGKBiPA134887774.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4441. Eukaryota.
ENOG410XNX8. LUCA.
GeneTreeiENSGT00760000118931.
HOGENOMiHOG000230814.
HOVERGENiHBG014286.
InParanoidiQ14145.
KOiK10456.
OMAiHTQFLPL.
OrthoDBiEOG091G02T3.
PhylomeDBiQ14145.
TreeFamiTF329218.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-5689880. Ub-specific processing proteases.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SIGNORiQ14145.

Miscellaneous databases

EvolutionaryTraceiQ14145.
GeneWikiiKEAP1.
GenomeRNAii9817.
PROiPR:Q14145.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000079999.
CleanExiHS_KEAP1.
ExpressionAtlasiQ14145. baseline and differential.
GenevisibleiQ14145. HS.

Family and domain databases

Gene3Di2.120.10.80. 1 hit.
2.130.10.80. 1 hit.
InterProiView protein in InterPro
IPR011705. BACK.
IPR017096. BTB-kelch_protein.
IPR000210. BTB/POZ_dom.
IPR015916. Gal_Oxidase_b-propeller.
IPR030563. KEAP1.
IPR015915. Kelch-typ_b-propeller.
IPR006652. Kelch_1.
IPR011333. SKP1/BTB/POZ.
PANTHERiPTHR24412:SF341. PTHR24412:SF341. 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.
SUPFAMiSSF54695. SSF54695. 1 hit.
PROSITEiView protein in PROSITE
PS50097. BTB. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiKEAP1_HUMAN
AccessioniPrimary (citable) accession number: Q14145
Secondary accession number(s): B3KPD5
, Q6LEP0, Q8WTX1, Q9BPY9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 2007
Last modified: April 12, 2017
This is version 178 of the entry and version 2 of the sequence. See 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.