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HUMAN:KEAP1

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) KEAP1 (synonyms: INRF2, KIAA0132, KLHL19)
Protein Name(s) Kelch-like ECH-associated protein 1

Cytosolic inhibitor of Nrf2 INrf2 Kelch-like protein 19

External Links
UniProt Q14145
EMBL AF361892
AF361888
AF361889
AF361890
AF361891
AF361886
D50922
AK056204
AC011461
BC002417
BC002930
BC015945
BC021957
CCDS CCDS12239.1
RefSeq NP_036421.2
NP_987096.1
XP_005260230.1
XP_005260231.1
UniGene Hs.465870
PDB 1U6D
1ZGK
2FLU
3VNG
3VNH
3ZGC
3ZGD
4CXI
4CXJ
4CXT
4IFJ
4IFL
4IFN
4IN4
4IQK
4L7B
4L7C
4L7D
4N1B
PDBsum 1U6D
1ZGK
2FLU
3VNG
3VNH
3ZGC
3ZGD
4CXI
4CXJ
4CXT
4IFJ
4IFL
4IFN
4IN4
4IQK
4L7B
4L7C
4L7D
4N1B
ProteinModelPortal Q14145
SMR Q14145
BioGrid 115156
DIP DIP-42134N
IntAct Q14145
MINT MINT-1197065
STRING 9606.ENSP00000171111
ChEMBL CHEMBL3038498
DrugBank DB08908
PhosphoSite Q14145
DMDM 146345444
MaxQB Q14145
PaxDb Q14145
PRIDE Q14145
DNASU 9817
Ensembl ENST00000171111
ENST00000393623
GeneID 9817
KEGG hsa:9817
UCSC uc002moq.1
CTD 9817
GeneCards GC19M010596
HGNC HGNC:23177
HPA CAB025337
HPA005558
MIM 606016
neXtProt NX_Q14145
PharmGKB PA134887774
eggNOG NOG255039
GeneTree ENSGT00760000118931
HOGENOM HOG000230814
HOVERGEN HBG014286
InParanoid Q14145
KO K10456
OMA ERYEPEG
OrthoDB EOG76739M
PhylomeDB Q14145
TreeFam TF329218
Reactome REACT_75842
UniPathway UPA00143
EvolutionaryTrace Q14145
GeneWiki KEAP1
GenomeRNAi 9817
NextBio 36968
PRO PR:Q14145
Proteomes UP000005640
Bgee Q14145
CleanEx HS_KEAP1
ExpressionAtlas Q14145
Genevestigator Q14145
GO GO:0031463
GO:0005737
GO:0005829
GO:0005783
GO:0005815
GO:0030496
GO:0005634
GO:0008134
GO:0071353
GO:0001701
GO:0043433
GO:0032436
GO:0010499
GO:0016567
GO:0045604
GO:0006351
Gene3D 2.130.10.80
InterPro IPR011705
IPR000210
IPR011333
IPR013069
IPR015916
IPR017096
IPR006652
Pfam PF07707
PF00651
PF01344
PIRSF PIRSF037037
SMART SM00875
SM00225
SM00612
SUPFAM SSF54695
PROSITE PS50097

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

enables

GO:0008134

transcription factor binding

PMID:17015834[1]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q16236

F

Seeded From UniProt

complete

part_of

GO:0031463

Cul3-RING ubiquitin ligase complex

PMID:15983046[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0030496

midbody

PMID:15166316[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0016567

protein ubiquitination

PMID:15983046[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0010499

proteasomal ubiquitin-independent protein catabolic process

PMID:15983046[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:19424503[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0042994

cytoplasmic sequestering of transcription factor

PMID:21873635[5]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000697162
RGD:621619

P

Seeded From UniProt

complete

enables

GO:0008134

transcription factor binding

PMID:21873635[5]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000697162
UniProtKB:Q14145

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005815

microtubule organizing center

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

GO:0030972

cleavage of cytosolic proteins involved in apoptosis

PMID:22072718[6]

ECO:0000315

P

Fig. 8D

complete
CACAO 3012

part_of

GO:0005654

nucleoplasm

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0097718

disordered domain specific binding

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q9Z2X8
ensembl:ENSMUSP00000131029

F

Seeded From UniProt

complete

GO:0032270

positive regulation of cellular protein metabolic process

PMID:22072718[6]

ECO:0000315

P

Fig. 8A

complete
CACAO 3030

involved_in

GO:0071353

cellular response to interleukin-4

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q9Z2X8
ensembl:ENSMUSP00000131029

P

Seeded From UniProt

complete

GO:0016567

protein ubiquitination

PMID:22072718[6]

ECO:0000315

P

Fig. 3A

complete
CACAO 3031

involved_in

GO:0045604

regulation of epidermal cell differentiation

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q9Z2X8
ensembl:ENSMUSP00000131029

P

Seeded From UniProt

complete

GO:0045732

positive regulation of protein catabolic process

PMID:22072718[6]

ECO:0000315

P

Fig. 1 and Fig. 8A

complete
CACAO 3016

enables

GO:0042803

protein homodimerization activity

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q9Z2X8
ensembl:ENSMUSP00000131029

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q9Z2X8
ensembl:ENSMUSP00000131029

F

Seeded From UniProt

complete

part_of

GO:0032991

protein-containing complex

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q9Z2X8
ensembl:ENSMUSP00000131029

C

Seeded From UniProt

complete

involved_in

GO:0006355

regulation of transcription, DNA-templated

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q9Z2X8
ensembl:ENSMUSP00000131029

P

Seeded From UniProt

complete

part_of

GO:0005884

actin filament

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q9Z2X8
ensembl:ENSMUSP00000131029

C

Seeded From UniProt

complete

part_of

GO:0005783

endoplasmic reticulum

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q9Z2X8
ensembl:ENSMUSP00000131029

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q9Z2X8
ensembl:ENSMUSP00000131029

C

Seeded From UniProt

complete

involved_in

GO:0001701

in utero embryonic development

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q9Z2X8
ensembl:ENSMUSP00000131029

P

Seeded From UniProt

complete

enables

GO:0008134

transcription factor binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR030563

F

Seeded From UniProt

complete

involved_in

GO:0016567

protein ubiquitination

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR030563

P

Seeded From UniProt

complete

part_of

GO:0031463

Cul3-RING ubiquitin ligase complex

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR030563

C

Seeded From UniProt

complete

involved_in

GO:0032436

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

PMID:17015834[1]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

has_regulation_target:(UniProtKB:Q16236)

Seeded From UniProt

complete

involved_in

GO:0043433

negative regulation of DNA-binding transcription factor activity

PMID:17015834[1]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:17015834[1]
Reactome:R-HSA-8956040
Reactome:R-HSA-8955289
Reactome:R-HSA-8955241
Reactome:R-HSA-6781764

ECO:0000304

author statement supported by traceable reference used in manual assertion





C

Seeded From UniProt

complete

involved_in

GO:0043687

post-translational protein modification

Reactome:R-HSA-597592

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0016579

protein deubiquitination

Reactome:R-HSA-5688426

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0539
UniProtKB-SubCell:SL-0191

C

Seeded From UniProt

complete

involved_in

GO:0016032

viral process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0945

P

Seeded From UniProt

complete

involved_in

GO:0016567

protein ubiquitination

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00143

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 1.3 Clements, CM et al. (2006) DJ-1, a cancer- and Parkinson's disease-associated protein, stabilizes the antioxidant transcriptional master regulator Nrf2. Proc. Natl. Acad. Sci. U.S.A. 103 15091-6 PubMed GONUTS page
  2. 2.0 2.1 2.2 Zhang, DD et al. (2005) Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for Cul3, targets Keap1 for degradation by a proteasome-independent pathway. J. Biol. Chem. 280 30091-9 PubMed GONUTS page
  3. Skop, AR et al. (2004) Dissection of the mammalian midbody proteome reveals conserved cytokinesis mechanisms. Science 305 61-6 PubMed GONUTS page
  4. Wang, XJ & Zhang, DD (2009) Ectodermal-neural cortex 1 down-regulates Nrf2 at the translational level. PLoS ONE 4 e5492 PubMed GONUTS page
  5. 5.0 5.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  6. 6.0 6.1 6.2 6.3 Niture, SK & Jaiswal, AK (2011) Inhibitor of Nrf2 (INrf2 or Keap1) protein degrades Bcl-xL via phosphoglycerate mutase 5 and controls cellular apoptosis. J. Biol. Chem. 286 44542-56 PubMed GONUTS page