Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q14145

- KEAP1_HUMAN

UniProt

Q14145 - KEAP1_HUMAN

(max 400 entries)x

Your basket is currently empty.

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

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

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 - 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
Complete GO annotation...

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
Complete GO annotation...

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. 3 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. 1 Publication
Mutagenesisi288 – 2881C → S: Abolishes repression of NFE2L2-dependent gene expression. Slows down degradation of NFE2L2. 1 Publication
Mutagenesisi308 – 3081L → A: Loss of export from nucleus; when associated with A-310. 1 Publication
Mutagenesisi310 – 3101L → A: Loss of export from nucleus; when associated with A-308. 1 Publication
Mutagenesisi334 – 3341Y → A: Loss of interaction with NFE2L2. Strongly reduces repression of NFE2L2-dependent gene expression. Loss of interaction with PGAM5. 2 Publications
Mutagenesisi380 – 3801R → A: Loss of interaction with NFE2L2. Abolishes repression of NFE2L2-dependent gene expression. 1 Publication
Mutagenesisi382 – 3821N → A: Loss of interaction with NFE2L2. Strongly reduces repression of NFE2L2-dependent gene expression. 1 Publication
Mutagenesisi415 – 4151R → A: Loss of interaction with NFE2L2. Abolishes repression of NFE2L2-dependent gene expression. Loss of interaction with PGAM5. 2 Publications
Mutagenesisi436 – 4361H → A: Loss of interaction with NFE2L2. Abolishes repression of NFE2L2-dependent gene expression. 1 Publication
Mutagenesisi478 – 4781F → A: Abolishes repression of NFE2L2-dependent gene expression. 1 Publication
Mutagenesisi483 – 4831R → A: Loss of interaction with NFE2L2. Abolishes repression of NFE2L2-dependent gene expression. Loss of interaction with PGAM5. 2 Publications
Mutagenesisi525 – 5251Y → A: Loss of interaction with NFE2L2. Strongly reduces repression of NFE2L2-dependent gene expression. 1 Publication
Mutagenesisi572 – 5721Y → A: Loss of interaction with NFE2L2. Strongly reduces repression of NFE2L2-dependent gene expression. Loss of interaction with PGAM5. 2 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

BgeeiQ14145.
CleanExiHS_KEAP1.
ExpressionAtlasiQ14145. baseline and differential.
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. 79 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[»]
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[»]
ProteinModelPortaliQ14145.
SMRiQ14145. Positions 49-297, 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.
GeneTreeiENSGT00760000118931.
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

        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 BAA09481.3 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 [» ]
4IFJ X-ray 1.80 A 321-609 [» ]
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 49-297, 322-609.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115156. 79 interactions.
DIPi DIP-42134N.
IntActi Q14145. 57 interactions.
MINTi MINT-1197065.
STRINGi 9606.ENSP00000171111.

Chemistry

ChEMBLi CHEMBL3038498.
DrugBanki DB08908. Dimethyl fumarate.

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.
GeneTreei ENSGT00760000118931.
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

Bgeei Q14145.
CleanExi HS_KEAP1.
ExpressionAtlasi Q14145. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 151 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