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Q9Z2X8

- KEAP1_MOUSE

UniProt

Q9Z2X8 - KEAP1_MOUSE

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Protein

Kelch-like ECH-associated protein 1

Gene
Keap1, Inrf2, Kiaa0132
Organism
Mus musculus (Mouse)
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 By similarity.2 Publications

Pathwayi

GO - Molecular functioni

  1. protein binding Source: IntAct

GO - Biological processi

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

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Enzyme and pathway databases

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

Names & Taxonomyi

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

Organism-specific databases

MGIiMGI:1858732. Keap1.

Subcellular locationi

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

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

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

PTM / Processingi

Molecule processing

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

Post-translational modificationi

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

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiQ9Z2X8.
PaxDbiQ9Z2X8.
PRIDEiQ9Z2X8.

PTM databases

PhosphoSiteiQ9Z2X8.

Expressioni

Gene expression databases

ArrayExpressiQ9Z2X8.
BgeeiQ9Z2X8.
CleanExiMM_KEAP1.
GenevestigatoriQ9Z2X8.

Interactioni

Subunit structurei

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

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9Z2X8.

Family & Domainsi

Domains and Repeats

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

Motif

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

Domaini

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

Sequence similaritiesi

Contains 1 BTB (POZ) domain.
Contains 6 Kelch repeats.

Keywords - Domaini

Kelch repeat, Repeat

Phylogenomic databases

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

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q9Z2X8-1 [UniParc]FASTAAdd to Basket

« Hide

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

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431T → A in BAE29559. 1 Publication
Sequence conflicti43 – 431T → A in BAE30980. 1 Publication
Sequence conflicti348 – 3481S → G in BAC32621. 1 Publication
Sequence conflicti361 – 3611P → T in BAE29559. 1 Publication
Sequence conflicti361 – 3611P → T in BAE30980. 1 Publication
Sequence conflicti579 – 5791D → V in BAE32581. 1 Publication
Sequence conflicti579 – 5791D → V in BAE33299. 1 Publication

Sequence databases

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

Genome annotation databases

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

Cross-referencesi

Sequence databases

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

3D structure databases

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

Protein-protein interaction databases

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

PTM databases

PhosphoSitei Q9Z2X8.

Proteomic databases

MaxQBi Q9Z2X8.
PaxDbi Q9Z2X8.
PRIDEi Q9Z2X8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

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

Phylogenomic databases

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

Enzyme and pathway databases

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

Miscellaneous databases

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

Gene expression databases

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

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain."
    Itoh K., Wakabayashi N., Katoh Y., Ishii T., Igarashi K., Engel J.D., Yamamoto M.
    Genes Dev. 13:76-86(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Tissue: Embryo.
  2. "Mouse INrf2 gene structure."
    Dhakshinamoorthy S., Jaiswal A.K.
    Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: C57BL/6.
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Fetal brain.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow, Corpora quadrigemina, Dendritic cell, Liver and Lung.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Brain.
  6. "Keap1-dependent proteasomal degradation of transcription factor Nrf2 contributes to the negative regulation of antioxidant response element-driven gene expression."
    McMahon M., Itoh K., Yamamoto M., Hayes J.D.
    J. Biol. Chem. 278:21592-21600(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Fetal Alz-50 clone 1 interacts with the human orthologue of the Kelch-like Ech-associated protein."
    Strachan G.D., Morgan K.L., Otis L.L., Caltagarone J., Gittis A., Bowser R., Jordan-Sciutto K.L.
    Biochemistry 43:12113-12122(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "Structural basis for defects of Keap1 activity provoked by its point mutations in lung cancer."
    Padmanabhan B., Tong K.I., Ohta T., Nakamura Y., Scharlock M., Ohtsuji M., Kang M., Kobayashi A., Yokoyama S., Yamamoto M.
    Mol. Cell 21:689-700(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 309-624 IN COMPLEX WITH NFE2L2, MUTAGENESIS OF 599-SER--ARG-601; 602-SER--VAL-604 AND 605-GLY--VAL-608.

Entry informationi

Entry nameiKEAP1_MOUSE
AccessioniPrimary (citable) accession number: Q9Z2X8
Secondary accession number(s): Q3U243
, Q3U8N7, Q547S3, Q6ZQI6, Q8BQY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 1999
Last modified: September 3, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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