CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012255
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Kelch-like ECH-associated protein 1 
Protein Synonyms/Alias
 Cytosolic inhibitor of Nrf2; INrf2; Kelch-like protein 19 
Gene Name
 KEAP1 
Gene Synonyms/Alias
 INRF2; KIAA0132; KLHL19 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
61YTLEDHTKQAFGIMNubiquitination[1, 2, 3]
84CDVTLQVKYQDAPAAubiquitination[2]
97AAQFMAHKVVLASSSubiquitination[2, 3]
108ASSSPVFKAMFTNGLubiquitination[2, 3, 4, 5]
287FLQMQLQKCEILQSDubiquitination[1, 6]
298LQSDSRCKDYLVKIFubiquitination[2, 7]
312FEELTLHKPTQVMPCubiquitination[1, 2, 6, 7]
615VTMEPCRKQIDQQNCubiquitination[2, 8, 9]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [8] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [9] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional Description
 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. 
Sequence Annotation
 DOMAIN 77 149 BTB.
 DOMAIN 184 286 BACK.
 REPEAT 327 372 Kelch 1.
 REPEAT 373 423 Kelch 2.
 REPEAT 424 470 Kelch 3.
 REPEAT 471 517 Kelch 4.
 REPEAT 518 564 Kelch 5.
 REPEAT 565 611 Kelch 6.
 MOTIF 301 310 Nuclear export signal.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Kelch repeat; Nucleus; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation; Ubl conjugation; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 624 AA 
Protein Sequence
MQPDPRPSGA GACCRFLPLQ SQCPEGAGDA VMYASTECKA EVTPSQHGNR TFSYTLEDHT 60
KQAFGIMNEL RLSQQLCDVT LQVKYQDAPA AQFMAHKVVL ASSSPVFKAM FTNGLREQGM 120
EVVSIEGIHP KVMERLIEFA YTASISMGEK CVLHVMNGAV MYQIDSVVRA CSDFLVQQLD 180
PSNAIGIANF AEQIGCVELH QRAREYIYMH FGEVAKQEEF FNLSHCQLVT LISRDDLNVR 240
CESEVFHACI NWVKYDCEQR RFYVQALLRA VRCHSLTPNF LQMQLQKCEI LQSDSRCKDY 300
LVKIFEELTL HKPTQVMPCR APKVGRLIYT AGGYFRQSLS YLEAYNPSDG TWLRLADLQV 360
PRSGLAGCVV GGLLYAVGGR NNSPDGNTDS SALDCYNPMT NQWSPCAPMS VPRNRIGVGV 420
IDGHIYAVGG SHGCIHHNSV ERYEPERDEW HLVAPMLTRR IGVGVAVLNR LLYAVGGFDG 480
TNRLNSAECY YPERNEWRMI TAMNTIRSGA GVCVLHNCIY AAGGYDGQDQ LNSVERYDVE 540
TETWTFVAPM KHRRSALGIT VHQGRIYVLG GYDGHTFLDS VECYDPDTDT WSEVTRMTSG 600
RSGVGVAVTM EPCRKQIDQQ NCTC 624 
Gene Ontology
 GO:0005813; C:centrosome; IDA:HPA.
 GO:0031463; C:Cul3-RING ubiquitin ligase complex; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005783; C:endoplasmic reticulum; IEA:Compara.
 GO:0030496; C:midbody; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0001701; P:in utero embryonic development; IEA:Compara.
 GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IDA:UniProtKB.
 GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
 GO:0045604; P:regulation of epidermal cell differentiation; IEA:Compara.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR011705; BACK.
 IPR000210; BTB/POZ-like.
 IPR011333; BTB/POZ_fold.
 IPR013069; BTB_POZ.
 IPR015916; Gal_Oxidase_b-propeller.
 IPR017096; Kelch-like_gigaxonin.
 IPR006652; Kelch_1. 
Pfam
 PF07707; BACK
 PF00651; BTB
 PF01344; Kelch_1 
SMART
 SM00875; BACK
 SM00225; BTB
 SM00612; Kelch 
PROSITE
 PS50097; BTB 
PRINTS