KEAP1_HUMAN - dbPTM
KEAP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
33PhosphorylationGAGDAVMYASTECKA
CCCCEEEEEECEEEE
7.2729978859
35PhosphorylationGDAVMYASTECKAEV
CCEEEEEECEEEEEE
13.7828348404
36PhosphorylationDAVMYASTECKAEVT
CEEEEEECEEEEEEC
36.9129978859
38SuccinylationVMYASTECKAEVTPS
EEEEECEEEEEECCC
5.25-
39UbiquitinationMYASTECKAEVTPSQ
EEEECEEEEEECCCC
41.15-
43PhosphorylationTECKAEVTPSQHGNR
CEEEEEECCCCCCCE
14.5525159151
53PhosphorylationQHGNRTFSYTLEDHT
CCCCEEEEEECCHHH
19.32-
54PhosphorylationHGNRTFSYTLEDHTK
CCCEEEEEECCHHHH
15.9121214269
55PhosphorylationGNRTFSYTLEDHTKQ
CCEEEEEECCHHHHH
23.60-
60PhosphorylationSYTLEDHTKQAFGIM
EEECCHHHHHHHHHH
36.85-
61UbiquitinationYTLEDHTKQAFGIMN
EECCHHHHHHHHHHH
35.8921906983
77GlutathionylationLRLSQQLCDVTLQVK
HHHHHHHCCEEEEEE
3.2522833525
84UbiquitinationCDVTLQVKYQDAPAA
CCEEEEEECCCCCHH
25.00-
97UbiquitinationAAQFMAHKVVLASSS
HHHHHEEEHHHHCCC
25.21-
102O-linked_GlycosylationAHKVVLASSSPVFKA
EEEHHHHCCCHHHHH
27.4728663241
103O-linked_GlycosylationHKVVLASSSPVFKAM
EEHHHHCCCHHHHHH
32.8128663241
104O-linked_GlycosylationKVVLASSSPVFKAMF
EHHHHCCCHHHHHHC
23.6928663241
108UbiquitinationASSSPVFKAMFTNGL
HCCCHHHHHHCCCCH
38.8921906983
108UbiquitinationASSSPVFKAMFTNGL
HCCCHHHHHHCCCCH
38.8921890473
108UbiquitinationASSSPVFKAMFTNGL
HCCCHHHHHHCCCCH
38.8921890473
112PhosphorylationPVFKAMFTNGLREQG
HHHHHHCCCCHHHCC
18.4523663014
131AcetylationSIEGIHPKVMERLIE
EEECCCHHHHHHHHH
39.8023954790
131MalonylationSIEGIHPKVMERLIE
EEECCCHHHHHHHHH
39.8026320211
151S-nitrosylationSISMGEKCVLHVMNG
CCCCCCCEEEEECCC
3.24-
151SuccinylationSISMGEKCVLHVMNG
CCCCCCCEEEEECCC
3.24-
151OtherSISMGEKCVLHVMNG
CCCCCCCEEEEECCC
3.2429590092
166O-linked_GlycosylationAVMYQIDSVVRACSD
CHHHCHHHHHHHHHH
24.9228663241
241SuccinylationRDDLNVRCESEVFHA
CCCCCCCCCHHHHHH
6.17-
257OtherINWVKYDCEQRRFYV
HHHHCCCHHHHHHHH
4.3329590092
273OtherALLRAVRCHSLTPNF
HHHHHHHHHCCCCCH
1.7429590092
273S-nitrosylationALLRAVRCHSLTPNF
HHHHHHHHHCCCCCH
1.7414585973
277PhosphorylationAVRCHSLTPNFLQMQ
HHHHHCCCCCHHHHH
21.14-
287UbiquitinationFLQMQLQKCEILQSD
HHHHHHHHCCHHCCC
42.2921906983
288SuccinylationLQMQLQKCEILQSDS
HHHHHHHCCHHCCCC
2.25-
288OtherLQMQLQKCEILQSDS
HHHHHHHCCHHCCCC
2.2529590092
288S-nitrosylationLQMQLQKCEILQSDS
HHHHHHHCCHHCCCC
2.2514585973
293PhosphorylationQKCEILQSDSRCKDY
HHCCHHCCCCCCHHH
33.8217192257
295PhosphorylationCEILQSDSRCKDYLV
CCHHCCCCCCHHHHH
44.8417192257
297GlutathionylationILQSDSRCKDYLVKI
HHCCCCCCHHHHHHH
4.5622833525
298UbiquitinationLQSDSRCKDYLVKIF
HCCCCCCHHHHHHHH
48.58-
312UbiquitinationFEELTLHKPTQVMPC
HHHHCCCCCCEEECC
53.5321906983
319SuccinylationKPTQVMPCRAPKVGR
CCCEEECCCCCCCCC
2.90-
319GlutathionylationKPTQVMPCRAPKVGR
CCCEEECCCCCCCCC
2.9022833525
334PhosphorylationLIYTAGGYFRQSLSY
EEEECCHHHHHHHHH
8.4820071362
345NitrationSLSYLEAYNPSDGTW
HHHHHHEECCCCCCE
20.45-
368GlutathionylationPRSGLAGCVVGGLLY
CCCCHHHHHHHHHHE
1.5422833525
388O-linked_GlycosylationNNSPDGNTDSSALDC
CCCCCCCCCCCHHHC
42.6728663241
390O-linked_GlycosylationSPDGNTDSSALDCYN
CCCCCCCCCHHHCCC
18.5728663241
391O-linked_GlycosylationPDGNTDSSALDCYNP
CCCCCCCCHHHCCCC
35.3428663241
400O-linked_GlycosylationLDCYNPMTNQWSPCA
HHCCCCCCCCCCCCC
26.0528663241
404O-linked_GlycosylationNPMTNQWSPCAPMSV
CCCCCCCCCCCCCCC
10.5928663241
410O-linked_GlycosylationWSPCAPMSVPRNRIG
CCCCCCCCCCCCCEE
28.1028663241
434OtherAVGGSHGCIHHNSVE
EECCCCCCCCCCCCC
1.93-
434GlutathionylationAVGGSHGCIHHNSVE
EECCCCCCCCCCCCC
1.9322833525
473NitrationAVLNRLLYAVGGFDG
HHHHHHHHHCCCCCC
12.11-
486PhosphorylationDGTNRLNSAECYYPE
CCCCCCCCCEEECCC
30.0030257219
490PhosphorylationRLNSAECYYPERNEW
CCCCCEEECCCCCCE
17.3530257219
491NitrationLNSAECYYPERNEWR
CCCCEEECCCCCCEE
15.41-
491PhosphorylationLNSAECYYPERNEWR
CCCCEEECCCCCCEE
15.4130257219
533O-linked_GlycosylationDGQDQLNSVERYDVE
CCHHHCCCEEEEECC
33.6728663241
537PhosphorylationQLNSVERYDVETETW
HCCCEEEEECCCCEE
15.7225262027
537NitrationQLNSVERYDVETETW
HCCCEEEEECCCCEE
15.72-
541PhosphorylationVERYDVETETWTFVA
EEEEECCCCEEEEEE
38.2725262027
543PhosphorylationRYDVETETWTFVAPM
EEECCCCEEEEEEEC
36.9125262027
545PhosphorylationDVETETWTFVAPMKH
ECCCCEEEEEEECCC
18.6925262027
599PhosphorylationSEVTRMTSGRSGVGV
HHHHHHCCCCCCCEE
23.90-
602PhosphorylationTRMTSGRSGVGVAVT
HHHCCCCCCCEEEEE
41.16-
609PhosphorylationSGVGVAVTMEPCRKQ
CCCEEEEEEHHHHHH
13.1820860994
613SuccinylationVAVTMEPCRKQIDQQ
EEEEEHHHHHHCHHC
5.60-
615UbiquitinationVTMEPCRKQIDQQNC
EEEHHHHHHCHHCCC
59.3221890473

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
599SPhosphorylationKinasePRKCEQ02156
GPS
602SPhosphorylationKinasePRKCEQ02156
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KEAP1_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NF2L2_HUMANNFE2L2physical
14517290
NF2L2_HUMANNFE2L2physical
18757741
NF2L2_HUMANNFE2L2physical
18417180
CUL3_HUMANCUL3physical
18417180
NF2L2_HUMANNFE2L2physical
17822677
CUL3_HUMANCUL3physical
17822677
COPD_HUMANARCN1physical
19615732
BBS1_HUMANBBS1physical
19615732
ERF1_HUMANETF1physical
19615732
NIPS2_HUMANGBASphysical
19615732
MD2L1_HUMANMAD2L1physical
19615732
MAZ_HUMANMAZphysical
19615732
PUR4_HUMANPFASphysical
19615732
SQSTM_HUMANSQSTM1physical
19615732
SLK_HUMANSLKphysical
19615732
COPG1_HUMANCOPG1physical
19615732
VWA8_HUMANVWA8physical
19615732
GET4_HUMANGET4physical
19615732
TM160_HUMANTMEM160physical
19615732
NIBL1_HUMANFAM129Bphysical
19615732
MCMBP_HUMANMCMBPphysical
19615732
T22D4_HUMANTSC22D4physical
19615732
RBM45_HUMANRBM45physical
19615732
SAS6_HUMANSASS6physical
19615732
PGAM5_HUMANPGAM5physical
19615732
NF2L2_HUMANNFE2L2physical
17462537
UBP11_HUMANUSP11physical
19615732
CUL3_HUMANCUL3physical
17439941
GABPA_HUMANGABPAphysical
17439941
PGAM5_HUMANPGAM5physical
17046835
NF2L2_HUMANNFE2L2physical
15985429
CUL3_HUMANCUL3physical
15983046
RBX1_HUMANRBX1physical
15983046
CUL3_HUMANCUL3physical
15601839
NF2L2_HUMANNFE2L2physical
15601839
CUL2_HUMANCUL2physical
15572695
CUL3_HUMANCUL3physical
15572695
CUL3_HUMANCUL3physical
15367669
CUL3_HUMANCUL3physical
15282312
NF2L2_HUMANNFE2L2physical
14585973
KEAP1_HUMANKEAP1physical
16790436
CUL3_HUMANCUL3physical
16790436
NF2L2_HUMANNFE2L2physical
16790436
NF2L2_HUMANNFE2L2physical
20027226
IKKB_HUMANIKBKBphysical
19818716
NF2L2_HUMANNFE2L2physical
19920073
NF2L2_HUMANNFE2L2physical
20486933
NF2L2_HUMANNFE2L2physical
20599909
CUL3_HUMANCUL3physical
20599909
KEAP1_HUMANKEAP1physical
20599909
NF2L1_HUMANNFE2L1physical
21262351
NF2L2_HUMANNFE2L2physical
21262351
TF65_HUMANRELAphysical
21262351
SQSTM_HUMANSQSTM1physical
20421418
NF2L2_HUMANNFE2L2physical
20421418
CUL3_HUMANCUL3physical
20421418
RBX1_HUMANRBX1physical
20421418
AMER1_HUMANAMER1physical
22215675
CUL3_HUMANCUL3physical
20534351
NF2L2_HUMANNFE2L2physical
21383067
IMA7_HUMANKPNA6physical
21383067
IPO11_HUMANIPO11physical
21383067
NF2L2_HUMANNFE2L2physical
15475350
ENC1_HUMANENC1physical
19424503
GABPA_HUMANGABPAphysical
19424503
MLP3A_HUMANMAP1LC3Aphysical
20495340
SQSTM_HUMANSQSTM1physical
20495340
PGAM5_HUMANPGAM5physical
18387606
NF2L2_HUMANNFE2L2physical
20484052
NF2L2_HUMANNFE2L2physical
22245129
CUL3_HUMANCUL3physical
22245129
NF2L2_HUMANNFE2L2physical
22558124
CUL3_HUMANCUL3physical
22558124
RBX1_HUMANRBX1physical
22558124
IKKB_HUMANIKBKBphysical
20600852
NF2L2_HUMANNFE2L2physical
16888629
NF2L2_HUMANNFE2L2physical
16006525
KEAP1_HUMANKEAP1physical
12145307
NF2L2_HUMANNFE2L2physical
11909699
CUL3_HUMANCUL3physical
21357422
SQSTM_HUMANSQSTM1physical
20378532
NF2L1_HUMANNFE2L1physical
16687406
DPP3_HUMANDPP3physical
23382044
F117B_HUMANFAM117Bphysical
23382044
MCM3_HUMANMCM3physical
23382044
T22D4_HUMANTSC22D4physical
23382044
WDR1_HUMANWDR1physical
23382044
MD2L1_HUMANMAD2L1physical
23382044
NF2L2_HUMANNFE2L2physical
23382044
SLK_HUMANSLKphysical
23382044
SQSTM_HUMANSQSTM1physical
23242280
BPTF_HUMANBPTFphysical
15379550
NF2L2_HUMANNFE2L2physical
23722832
NF2L2_HUMANNFE2L2physical
23645672
TF65_HUMANRELAphysical
21988832
NF2L1_HUMANNFE2L1physical
21988832
NF2L2_HUMANNFE2L2physical
21988832
RSMN_HUMANSNRPNphysical
21988832
PDC6I_HUMANPDCD6IPphysical
21988832
PIDD1_HUMANPIDD1physical
21988832
T22D4_HUMANTSC22D4physical
21988832
SQSTM_HUMANSQSTM1physical
24011591
NF2L2_HUMANNFE2L2physical
24011591
NF2L2_HUMANNFE2L2physical
23986495
NF2L2_HUMANNFE2L2physical
24130096
NF2L1_HUMANNFE2L1physical
24127568
CUL3_HUMANCUL3physical
24127568
RBX1_HUMANRBX1physical
24127568
HS90A_HUMANHSP90AA1physical
24127568
PGAM5_HUMANPGAM5physical
24127568
IKKB_HUMANIKBKBphysical
24127568
BCL2_HUMANBCL2physical
24127568
NF2L2_HUMANNFE2L2physical
24512214
KEAP1_HUMANKEAP1physical
24322982
CUL3_HUMANCUL3physical
24322982
NF2L2_HUMANNFE2L2physical
24322982
SLK_HUMANSLKphysical
24322982
AMER1_HUMANAMER1physical
24322982
MCM3_HUMANMCM3physical
24322982
DPP3_HUMANDPP3physical
24322982
IKKB_HUMANIKBKBphysical
24322982
SQSTM_HUMANSQSTM1physical
24322982
NF2L2_HUMANNFE2L2physical
23066931
XPO1_HUMANXPO1physical
22448038
CUL3_HUMANCUL3physical
22448038
NF2L2_HUMANNFE2L2physical
22448038
RBX1_HUMANRBX1physical
22448038
NF2L2_HUMANNFE2L2physical
22215675
DPP3_HUMANDPP3physical
25416956
NUDT4_HUMANNUDT4physical
25416956
MABP1_HUMANMAPKBP1physical
25416956
KLHL3_HUMANKLHL3physical
25416956
LSM3_HUMANLSM3physical
25416956
ZSC32_HUMANZSCAN32physical
25416956
OXR1_HUMANOXR1physical
25416956
CIP1_HUMANCCNB1IP1physical
25416956
WDR83_HUMANWDR83physical
25416956
F117B_HUMANFAM117Bphysical
25416956
RBX1_HUMANRBX1physical
15572695
NF2L2_HUMANNFE2L2physical
15572695
KEAP1_HUMANKEAP1physical
15983046
SQSTM_HUMANSQSTM1physical
25505069
UBC_HUMANUBCphysical
25505069
CUL3_HUMANCUL3physical
25742418
KEAP1_HUMANKEAP1physical
25742418
UBC_HUMANUBCphysical
25742418
NF2L2_HUMANNFE2L2physical
25582950
PTMA_HUMANPTMAphysical
25582950
IKKB_HUMANIKBKBphysical
25926686
EGFR_HUMANEGFRphysical
25628777
CUL3_HUMANCUL3physical
25628777
RBM45_HUMANRBM45physical
25939382
SQSTM_HUMANSQSTM1physical
25939382
PALB2_HUMANPALB2physical
26649820
NF2L2_HUMANNFE2L2physical
26078718
CUL3_HUMANCUL3physical
16449638
NF2L2_HUMANNFE2L2physical
16449638
RBX1_HUMANRBX1physical
16449638
KEAP1_HUMANKEAP1physical
17254749
CADH1_HUMANCDH1physical
22302998
NF2L2_HUMANNFE2L2physical
22302998
NF2L2_HUMANNFE2L2physical
27212020
PAQR3_HUMANPAQR3physical
27212020
IKKB_HUMANIKBKBphysical
27387502
CUL3_HUMANCUL3physical
28186440
NF2L2_HUMANNFE2L2physical
28186440
CUL3_HUMANCUL3physical
23727018
NF2L2_HUMANNFE2L2physical
23727018
CUL3_HUMANCUL3physical
26757824
PALB2_HUMANPALB2physical
22331464
BRCA2_HUMANBRCA2physical
22331464
BRCA1_HUMANBRCA1physical
22331464
RAD51_HUMANRAD51physical
22331464
NF2L2_HUMANNFE2L2physical
22331464
SQSTM_HUMANSQSTM1physical
29033244
NF2L2_HUMANNFE2L2physical
29033244
IASPP_HUMANPPP1R13Lphysical
29033244
NF2L2_HUMANNFE2L2physical
28638054
NF2L2_HUMANNFE2L2physical
28534518
SRC8_HUMANCTTNphysical
26602019
NF2L2_HUMANNFE2L2physical
27091842
PSD10_HUMANPSMD10physical
27091842

Drug and Disease Associations
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
DB08908Dimethyl fumarate
Regulatory Network of KEAP1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

TOP