AHR_HUMAN - dbPTM
AHR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AHR_HUMAN
UniProt AC P35869
Protein Name Aryl hydrocarbon receptor
Gene Name AHR
Organism Homo sapiens (Human).
Sequence Length 848
Subcellular Localization Cytoplasm . Nucleus . Initially cytoplasmic
upon binding with ligand and interaction with a HSP90, it translocates to the nucleus.
Protein Description Ligand-activated transcriptional activator. Binds to the XRE promoter region of genes it activates. Activates the expression of multiple phase I and II xenobiotic chemical metabolizing enzyme genes (such as the CYP1A1 gene). Mediates biochemical and toxic effects of halogenated aromatic hydrocarbons. Involved in cell-cycle regulation. Likely to play an important role in the development and maturation of many tissues. Regulates the circadian clock by inhibiting the basal and circadian expression of the core circadian component PER1. Inhibits PER1 by repressing the CLOCK-ARNTL/BMAL1 heterodimer mediated transcriptional activation of PER1. The heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription. [PubMed: 28602820]
Protein Sequence MNSSSANITYASRKRRKPVQKTVKPIPAEGIKSNPSKRHRDRLNTELDRLASLLPFPQDVINKLDKLSVLRLSVSYLRAKSFFDVALKSSPTERNGGQDNCRAANFREGLNLQEGEFLLQALNGFVLVVTTDALVFYASSTIQDYLGFQQSDVIHQSVYELIHTEDRAEFQRQLHWALNPSQCTESGQGIEEATGLPQTVVCYNPDQIPPENSPLMERCFICRLRCLLDNSSGFLAMNFQGKLKYLHGQKKKGKDGSILPPQLALFAIATPLQPPSILEIRTKNFIFRTKHKLDFTPIGCDAKGRIVLGYTEAELCTRGSGYQFIHAADMLYCAESHIRMIKTGESGMIVFRLLTKNNRWTWVQSNARLLYKNGRPDYIIVTQRPLTDEEGTEHLRKRNTKLPFMFTTGEAVLYEATNPFPAIMDPLPLRTKNGTSGKDSATTSTLSKDSLNPSSLLAAMMQQDESIYLYPASSTSSTAPFENNFFNESMNECRNWQDNTAPMGNDTILKHEQIDQPQDVNSFAGGHPGLFQDSKNSDLYSIMKNLGIDFEDIRHMQNEKFFRNDFSGEVDFRDIDLTDEILTYVQDSLSKSPFIPSDYQQQQSLALNSSCMVQEHLHLEQQQQHHQKQVVVEPQQQLCQKMKHMQVNGMFENWNSNQFVPFNCPQQDPQQYNVFTDLHGISQEFPYKSEMDSMPYTQNFISCNQPVLPQHSKCTELDYPMGSFEPSPYPTTSSLEDFVTCLQLPENQKHGLNPQSAIITPQTCYAGAVSMYQCQPEPQHTHVGQMQYNPVLPGQQAFLNKFQNGVLNETYPAELNNINNTQTTTHLQPLHHPSEARPFPDLTSSGFL
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
1Acetylation-------MNSSSANI
-------CCCCCCCC
11.2222814378
10PhosphorylationSSSANITYASRKRRK
CCCCCCCCCCCCCCC
9.9729759185
12PhosphorylationSANITYASRKRRKPV
CCCCCCCCCCCCCCC
28.1115063792
24AcetylationKPVQKTVKPIPAEGI
CCCCCCCCCCCCCHH
42.3226051181
24SumoylationKPVQKTVKPIPAEGI
CCCCCCCCCCCCCHH
42.32-
24SumoylationKPVQKTVKPIPAEGI
CCCCCCCCCCCCCHH
42.32-
24UbiquitinationKPVQKTVKPIPAEGI
CCCCCCCCCCCCCHH
42.3221906983
32UbiquitinationPIPAEGIKSNPSKRH
CCCCCHHCCCCCHHH
55.8521906983
36PhosphorylationEGIKSNPSKRHRDRL
CHHCCCCCHHHHHHH
46.7215063792
45PhosphorylationRHRDRLNTELDRLAS
HHHHHHHHHHHHHHH
42.3828857561
63UbiquitinationFPQDVINKLDKLSVL
CCHHHHHHHHHHHHH
47.1121906983
68PhosphorylationINKLDKLSVLRLSVS
HHHHHHHHHHHHHHH
25.5014985336
75PhosphorylationSVLRLSVSYLRAKSF
HHHHHHHHHHHHHHH
18.31-
76PhosphorylationVLRLSVSYLRAKSFF
HHHHHHHHHHHHHHH
9.69-
81PhosphorylationVSYLRAKSFFDVALK
HHHHHHHHHHHHHHC
30.1154886401
88UbiquitinationSFFDVALKSSPTERN
HHHHHHHCCCCCCCC
38.8721906983
89PhosphorylationFFDVALKSSPTERNG
HHHHHHCCCCCCCCC
42.2629214152
90PhosphorylationFDVALKSSPTERNGG
HHHHHCCCCCCCCCC
33.9628857561
92PhosphorylationVALKSSPTERNGGQD
HHHCCCCCCCCCCCC
49.9126270265
232PhosphorylationRCLLDNSSGFLAMNF
HHHHCCCCCEEEEEE
39.5650564191
244UbiquitinationMNFQGKLKYLHGQKK
EEEHHHHHHHCCCCC
49.61-
254SumoylationHGQKKKGKDGSILPP
CCCCCCCCCCCCCCH
68.73-
254SumoylationHGQKKKGKDGSILPP
CCCCCCCCCCCCCCH
68.73-
292UbiquitinationFIFRTKHKLDFTPIG
EEEEECCCCCCEECC
51.84-
322PhosphorylationLCTRGSGYQFIHAAD
HCCCCCCCCEEEHHH
11.2721703235
346PhosphorylationRMIKTGESGMIVFRL
EEEECCCCCEEEEEE
34.7023401153
355PhosphorylationMIVFRLLTKNNRWTW
EEEEEEEECCCCEEE
36.0068735857
361PhosphorylationLTKNNRWTWVQSNAR
EECCCCEEEHHHCCE
16.7227067055
372UbiquitinationSNARLLYKNGRPDYI
HCCEEEEECCCCCEE
53.55-
378PhosphorylationYKNGRPDYIIVTQRP
EECCCCCEEEEECCC
8.6711032419
382PhosphorylationRPDYIIVTQRPLTDE
CCCEEEEECCCCCCC
14.4124719451
438AcetylationTKNGTSGKDSATTST
CCCCCCCCCCCCCCC
48.5626051181
438UbiquitinationTKNGTSGKDSATTST
CCCCCCCCCCCCCCC
48.5621906983
507PhosphorylationTAPMGNDTILKHEQI
CCCCCCCCCCCHHHC
32.0128555341
510UbiquitinationMGNDTILKHEQIDQP
CCCCCCCCHHHCCCC
41.0421906983
535UbiquitinationPGLFQDSKNSDLYSI
CCCCCCCCCCCHHHH
69.6221906983
540PhosphorylationDSKNSDLYSIMKNLG
CCCCCCHHHHHHHCC
10.9225159151
544UbiquitinationSDLYSIMKNLGIDFE
CCHHHHHHHCCCCHH
47.56-
560UbiquitinationIRHMQNEKFFRNDFS
HHHHHCCHHHCCCCC
58.3021906983
641UbiquitinationPQQQLCQKMKHMQVN
HHHHHHHHCCCCHHC
49.25-
689PhosphorylationSQEFPYKSEMDSMPY
CCCCCCCCCCCCCCC
32.1021945579
693PhosphorylationPYKSEMDSMPYTQNF
CCCCCCCCCCCCCCC
21.9821945579
696PhosphorylationSEMDSMPYTQNFISC
CCCCCCCCCCCCCCC
16.5921945579
697PhosphorylationEMDSMPYTQNFISCN
CCCCCCCCCCCCCCC
15.9221945579
702PhosphorylationPYTQNFISCNQPVLP
CCCCCCCCCCCCCCC
11.6821945579
712PhosphorylationQPVLPQHSKCTELDY
CCCCCCCCCCCCCCC
24.9521945579
723PhosphorylationELDYPMGSFEPSPYP
CCCCCCCCCCCCCCC
21.8628348404
729PhosphorylationGSFEPSPYPTTSSLE
CCCCCCCCCCCCCHH
19.9728348404
731PhosphorylationFEPSPYPTTSSLEDF
CCCCCCCCCCCHHHH
33.2028348404
732PhosphorylationEPSPYPTTSSLEDFV
CCCCCCCCCCHHHHH
16.2928348404
733PhosphorylationPSPYPTTSSLEDFVT
CCCCCCCCCHHHHHH
35.0928348404
734PhosphorylationSPYPTTSSLEDFVTC
CCCCCCCCHHHHHHH
33.4128348404
740PhosphorylationSSLEDFVTCLQLPEN
CCHHHHHHHHCCCCH
13.9028348404

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
12SPhosphorylationKinasePRKCAP17252
GPS
36SPhosphorylationKinasePRKCAP17252
GPS
-KUbiquitinationE3 ubiquitin ligaseSTUB1Q9UNE7
PMID:17209571

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AHR_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 AHR_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CCNT1_HUMANCCNT1physical
12917420
ESR1_HUMANESR1physical
12612060
SMCA4_HUMANSMARCA4physical
11805098
NEDD8_HUMANNEDD8physical
12215427
AIP_HUMANAIPphysical
9111057
NCOA2_HUMANNCOA2physical
12024042
ARNT_HUMANARNTphysical
8384309
ARNT_HUMANARNTphysical
7488247
NRIP1_HUMANNRIP1physical
10428779
AIP_HUMANAIPphysical
9837941
TBP_HUMANTBPphysical
8794892
T2FB_HUMANGTF2F2physical
8794892
T2FA_HUMANGTF2F1physical
8794892
TF65_HUMANRELAphysical
12181450
RB_HUMANRB1physical
9712901
ESR1_HUMANESR1physical
10620335
COT1_HUMANNR2F1physical
10620335
HS90A_HUMANHSP90AA1physical
9083006
AIP_HUMANAIPphysical
9083006
CTNB1_HUMANCTNNB1physical
19651607
FOXA1_HUMANFOXA1physical
22596188
CHIP_HUMANSTUB1physical
12837759
AHR_HUMANAHRphysical
18358233
NS1BP_HUMANIVNS1ABPphysical
16582008
AIP_HUMANAIPphysical
16582008
BRCA1_HUMANBRCA1physical
18259752
NCOA7_HUMANNCOA7physical
10395741
NCOR2_HUMANNCOR2physical
10395741
RB_HUMANRB1physical
10644764
TBP_HUMANTBPphysical
15641800
TAF9_HUMANTAF9physical
15641800
TAF6_HUMANTAF6physical
15641800
TAF4_HUMANTAF4physical
15641800
NCOA1_HUMANNCOA1physical
15641800
NCOA2_HUMANNCOA2physical
15641800
RB_HUMANRB1physical
11259609
ARNT_HUMANARNTphysical
11259609
MAF_HUMANMAFphysical
20676092
EP300_HUMANEP300physical
21988832
GNA13_HUMANGNA13physical
19390533
NCOA1_HUMANNCOA1physical
12024042
XPO1_HUMANXPO1physical
12065584
AIP_HUMANAIPphysical
12065584
AIP_HUMANAIPphysical
11013261
ARNT_HUMANARNTphysical
22138065
ARNT_HUMANARNTphysical
20006590
ARNT_HUMANARNTphysical
18096572
ARNT2_HUMANARNT2physical
18096572
CTNB1_HUMANCTNNB1physical
23174221
ESR1_HUMANESR1physical
15837795
VIME_HUMANVIMphysical
27752740
CSN5_HUMANCOPS5physical
27060206
SMAD4_HUMANSMAD4physical
27060206

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
DB01076Atorvastatin
DB00499Flutamide
DB01404Ginseng
DB01097Leflunomide
DB00379Mexiletine
DB00393Nimodipine
Regulatory Network of AHR_HUMAN

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Related Literatures of Post-Translational Modification

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