| UniProt ID | KEAP1_HUMAN | |
|---|---|---|
| UniProt AC | Q14145 | |
| Protein Name | Kelch-like ECH-associated protein 1 | |
| Gene Name | KEAP1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 624 | |
| Subcellular Localization | Cytoplasm. Nucleus. Shuttles between cytoplasm and nucleus. | |
| Protein 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.. | |
| Protein Sequence | MQPDPRPSGAGACCRFLPLQSQCPEGAGDAVMYASTECKAEVTPSQHGNRTFSYTLEDHTKQAFGIMNELRLSQQLCDVTLQVKYQDAPAAQFMAHKVVLASSSPVFKAMFTNGLREQGMEVVSIEGIHPKVMERLIEFAYTASISMGEKCVLHVMNGAVMYQIDSVVRACSDFLVQQLDPSNAIGIANFAEQIGCVELHQRAREYIYMHFGEVAKQEEFFNLSHCQLVTLISRDDLNVRCESEVFHACINWVKYDCEQRRFYVQALLRAVRCHSLTPNFLQMQLQKCEILQSDSRCKDYLVKIFEELTLHKPTQVMPCRAPKVGRLIYTAGGYFRQSLSYLEAYNPSDGTWLRLADLQVPRSGLAGCVVGGLLYAVGGRNNSPDGNTDSSALDCYNPMTNQWSPCAPMSVPRNRIGVGVIDGHIYAVGGSHGCIHHNSVERYEPERDEWHLVAPMLTRRIGVGVAVLNRLLYAVGGFDGTNRLNSAECYYPERNEWRMITAMNTIRSGAGVCVLHNCIYAAGGYDGQDQLNSVERYDVETETWTFVAPMKHRRSALGITVHQGRIYVLGGYDGHTFLDSVECYDPDTDTWSEVTRMTSGRSGVGVAVTMEPCRKQIDQQNCTC | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 33 | Phosphorylation | GAGDAVMYASTECKA CCCCEEEEEECEEEE | 7.27 | 29978859 | |
| 35 | Phosphorylation | GDAVMYASTECKAEV CCEEEEEECEEEEEE | 13.78 | 28348404 | |
| 36 | Phosphorylation | DAVMYASTECKAEVT CEEEEEECEEEEEEC | 36.91 | 29978859 | |
| 38 | Succinylation | VMYASTECKAEVTPS EEEEECEEEEEECCC | 5.25 | - | |
| 39 | Ubiquitination | MYASTECKAEVTPSQ EEEECEEEEEECCCC | 41.15 | - | |
| 43 | Phosphorylation | TECKAEVTPSQHGNR CEEEEEECCCCCCCE | 14.55 | 25159151 | |
| 53 | Phosphorylation | QHGNRTFSYTLEDHT CCCCEEEEEECCHHH | 19.32 | - | |
| 54 | Phosphorylation | HGNRTFSYTLEDHTK CCCEEEEEECCHHHH | 15.91 | 21214269 | |
| 55 | Phosphorylation | GNRTFSYTLEDHTKQ CCEEEEEECCHHHHH | 23.60 | - | |
| 60 | Phosphorylation | SYTLEDHTKQAFGIM EEECCHHHHHHHHHH | 36.85 | - | |
| 61 | Ubiquitination | YTLEDHTKQAFGIMN EECCHHHHHHHHHHH | 35.89 | 21906983 | |
| 77 | Glutathionylation | LRLSQQLCDVTLQVK HHHHHHHCCEEEEEE | 3.25 | 22833525 | |
| 84 | Ubiquitination | CDVTLQVKYQDAPAA CCEEEEEECCCCCHH | 25.00 | - | |
| 97 | Ubiquitination | AAQFMAHKVVLASSS HHHHHEEEHHHHCCC | 25.21 | - | |
| 102 | O-linked_Glycosylation | AHKVVLASSSPVFKA EEEHHHHCCCHHHHH | 27.47 | 28663241 | |
| 103 | O-linked_Glycosylation | HKVVLASSSPVFKAM EEHHHHCCCHHHHHH | 32.81 | 28663241 | |
| 104 | O-linked_Glycosylation | KVVLASSSPVFKAMF EHHHHCCCHHHHHHC | 23.69 | 28663241 | |
| 108 | Ubiquitination | ASSSPVFKAMFTNGL HCCCHHHHHHCCCCH | 38.89 | 21906983 | |
| 108 | Ubiquitination | ASSSPVFKAMFTNGL HCCCHHHHHHCCCCH | 38.89 | 21890473 | |
| 108 | Ubiquitination | ASSSPVFKAMFTNGL HCCCHHHHHHCCCCH | 38.89 | 21890473 | |
| 112 | Phosphorylation | PVFKAMFTNGLREQG HHHHHHCCCCHHHCC | 18.45 | 23663014 | |
| 131 | Acetylation | SIEGIHPKVMERLIE EEECCCHHHHHHHHH | 39.80 | 23954790 | |
| 131 | Malonylation | SIEGIHPKVMERLIE EEECCCHHHHHHHHH | 39.80 | 26320211 | |
| 151 | S-nitrosylation | SISMGEKCVLHVMNG CCCCCCCEEEEECCC | 3.24 | - | |
| 151 | Succinylation | SISMGEKCVLHVMNG CCCCCCCEEEEECCC | 3.24 | - | |
| 151 | Other | SISMGEKCVLHVMNG CCCCCCCEEEEECCC | 3.24 | 29590092 | |
| 166 | O-linked_Glycosylation | AVMYQIDSVVRACSD CHHHCHHHHHHHHHH | 24.92 | 28663241 | |
| 241 | Succinylation | RDDLNVRCESEVFHA CCCCCCCCCHHHHHH | 6.17 | - | |
| 257 | Other | INWVKYDCEQRRFYV HHHHCCCHHHHHHHH | 4.33 | 29590092 | |
| 273 | Other | ALLRAVRCHSLTPNF HHHHHHHHHCCCCCH | 1.74 | 29590092 | |
| 273 | S-nitrosylation | ALLRAVRCHSLTPNF HHHHHHHHHCCCCCH | 1.74 | 14585973 | |
| 277 | Phosphorylation | AVRCHSLTPNFLQMQ HHHHHCCCCCHHHHH | 21.14 | - | |
| 287 | Ubiquitination | FLQMQLQKCEILQSD HHHHHHHHCCHHCCC | 42.29 | 21906983 | |
| 288 | Succinylation | LQMQLQKCEILQSDS HHHHHHHCCHHCCCC | 2.25 | - | |
| 288 | Other | LQMQLQKCEILQSDS HHHHHHHCCHHCCCC | 2.25 | 29590092 | |
| 288 | S-nitrosylation | LQMQLQKCEILQSDS HHHHHHHCCHHCCCC | 2.25 | 14585973 | |
| 293 | Phosphorylation | QKCEILQSDSRCKDY HHCCHHCCCCCCHHH | 33.82 | 17192257 | |
| 295 | Phosphorylation | CEILQSDSRCKDYLV CCHHCCCCCCHHHHH | 44.84 | 17192257 | |
| 297 | Glutathionylation | ILQSDSRCKDYLVKI HHCCCCCCHHHHHHH | 4.56 | 22833525 | |
| 298 | Ubiquitination | LQSDSRCKDYLVKIF HCCCCCCHHHHHHHH | 48.58 | - | |
| 312 | Ubiquitination | FEELTLHKPTQVMPC HHHHCCCCCCEEECC | 53.53 | 21906983 | |
| 319 | Succinylation | KPTQVMPCRAPKVGR CCCEEECCCCCCCCC | 2.90 | - | |
| 319 | Glutathionylation | KPTQVMPCRAPKVGR CCCEEECCCCCCCCC | 2.90 | 22833525 | |
| 334 | Phosphorylation | LIYTAGGYFRQSLSY EEEECCHHHHHHHHH | 8.48 | 20071362 | |
| 345 | Nitration | SLSYLEAYNPSDGTW HHHHHHEECCCCCCE | 20.45 | - | |
| 368 | Glutathionylation | PRSGLAGCVVGGLLY CCCCHHHHHHHHHHE | 1.54 | 22833525 | |
| 388 | O-linked_Glycosylation | NNSPDGNTDSSALDC CCCCCCCCCCCHHHC | 42.67 | 28663241 | |
| 390 | O-linked_Glycosylation | SPDGNTDSSALDCYN CCCCCCCCCHHHCCC | 18.57 | 28663241 | |
| 391 | O-linked_Glycosylation | PDGNTDSSALDCYNP CCCCCCCCHHHCCCC | 35.34 | 28663241 | |
| 400 | O-linked_Glycosylation | LDCYNPMTNQWSPCA HHCCCCCCCCCCCCC | 26.05 | 28663241 | |
| 404 | O-linked_Glycosylation | NPMTNQWSPCAPMSV CCCCCCCCCCCCCCC | 10.59 | 28663241 | |
| 410 | O-linked_Glycosylation | WSPCAPMSVPRNRIG CCCCCCCCCCCCCEE | 28.10 | 28663241 | |
| 434 | Other | AVGGSHGCIHHNSVE EECCCCCCCCCCCCC | 1.93 | - | |
| 434 | Glutathionylation | AVGGSHGCIHHNSVE EECCCCCCCCCCCCC | 1.93 | 22833525 | |
| 473 | Nitration | AVLNRLLYAVGGFDG HHHHHHHHHCCCCCC | 12.11 | - | |
| 486 | Phosphorylation | DGTNRLNSAECYYPE CCCCCCCCCEEECCC | 30.00 | 30257219 | |
| 490 | Phosphorylation | RLNSAECYYPERNEW CCCCCEEECCCCCCE | 17.35 | 30257219 | |
| 491 | Nitration | LNSAECYYPERNEWR CCCCEEECCCCCCEE | 15.41 | - | |
| 491 | Phosphorylation | LNSAECYYPERNEWR CCCCEEECCCCCCEE | 15.41 | 30257219 | |
| 533 | O-linked_Glycosylation | DGQDQLNSVERYDVE CCHHHCCCEEEEECC | 33.67 | 28663241 | |
| 537 | Phosphorylation | QLNSVERYDVETETW HCCCEEEEECCCCEE | 15.72 | 25262027 | |
| 537 | Nitration | QLNSVERYDVETETW HCCCEEEEECCCCEE | 15.72 | - | |
| 541 | Phosphorylation | VERYDVETETWTFVA EEEEECCCCEEEEEE | 38.27 | 25262027 | |
| 543 | Phosphorylation | RYDVETETWTFVAPM EEECCCCEEEEEEEC | 36.91 | 25262027 | |
| 545 | Phosphorylation | DVETETWTFVAPMKH ECCCCEEEEEEECCC | 18.69 | 25262027 | |
| 599 | Phosphorylation | SEVTRMTSGRSGVGV HHHHHHCCCCCCCEE | 23.90 | - | |
| 602 | Phosphorylation | TRMTSGRSGVGVAVT HHHCCCCCCCEEEEE | 41.16 | - | |
| 609 | Phosphorylation | SGVGVAVTMEPCRKQ CCCEEEEEEHHHHHH | 13.18 | 20860994 | |
| 613 | Succinylation | VAVTMEPCRKQIDQQ EEEEEHHHHHHCHHC | 5.60 | - | |
| 615 | Ubiquitination | VTMEPCRKQIDQQNC EEEHHHHHHCHHCCC | 59.32 | 21890473 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KEAP1_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of KEAP1_HUMAN !! | ||||||
| Kegg Disease | |
|---|---|
| There are no disease associations of PTM sites. | |
| OMIM Disease | |
| There are no disease associations of PTM sites. | |
| Kegg Drug | |
| There are no disease associations of PTM sites. | |
| DrugBank | |
| DB08908 | Dimethyl fumarate |
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| Phosphorylation | |
| Reference | PubMed |
| "Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293 AND SER-295, ANDMASS SPECTROMETRY. | |