Tag | Content |
---|---|
UniProt Accession | KEAP1_HUMAN; Q14145; |
Entrez ID | 9817 |
GenBank Protein ID | NM_012289.3; NM_203500.1; XM_005260173.1; XM_005260174.1; XM_011528452.1; |
GenBank Nucleotide ID | NP_036421.2; NP_987096.1; XP_005260230.1; XP_005260231.1; XP_011526754.1; |
Protein Name | Kelch-like ECH-associated protein 1 (Cytosolic inhibitor of Nrf2) (INrf2) (Kelch-like protein 19) |
Gene Name | KEAP1; INRF2; KIAA0132; KLHL19 |
Organism | Homo sapiens |
NCBI Taxa ID | 9606 |
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 (Fasta) | 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 625 |
|
Database | Annotation |
---|---|
Cancer Gene Census | NSCLC, breast carcinoma |
CTD (Curated) (count: 8) (view all) | MESH:D002292
; Carcinoma, Renal Cell MESH:D018450 ; Disease Progression MESH:D005706 ; Gallbladder Neoplasms MESH:D005767 ; Gastrointestinal Diseases MESH:D006505 ; Hepatitis MESH:D007642 ; Keratosis |
PTM | Modification Sites |
---|---|
Phosphorylation (count: 14) (view all) | 112 PVFKAMFTNGLREQG dbPAF
277 AVRCHSLTPNFLQMQ dbPAF 293 QKCEILQSDSRCKDY dbPAF 295 CEILQSDSRCKDYLV dbPAF 33 GAGDAVMYASTECKA dbPAF 43 TECKAEVTPSQHGNR dbPAF |
Acetylation (count: 1) | 131 SIEGIHPKVMERLIE PLMD |
Ubiquitination (count: 11) (view all) | 108 ASSSPVFKAMFTNGL PLMD
254 HACINWVKYDCEQRR PLMD 287 FLQMQLQKCEILQSD PLMD 298 LQSDSRCKDYLVKIF PLMD 303 RCKDYLVKIFEELTL PLMD 312 FEELTLHKPTQVMPC PLMD |
Malonylation (count: 1) | 131 SIEGIHPKVMERLIE PLMD |
Network | Interaction | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
A | B | Source | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
|