AHRR_HUMAN - dbPTM
AHRR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AHRR_HUMAN
UniProt AC A9YTQ3
Protein Name Aryl hydrocarbon receptor repressor
Gene Name AHRR
Organism Homo sapiens (Human).
Sequence Length 701
Subcellular Localization Cytoplasm . Nucleus . Predominantly in the nuclear compartment. First cytoplasmic, translocates into the nuclear compartment upon interaction with ARNT in the cytoplasmic compartment.
Protein Description Mediates dioxin toxicity and is involved in regulation of cell growth and differentiation. Represses the transcription activity of AHR by competing with this transcription factor for heterodimer formation with the ARNT and subsequently binding to the xenobiotic response element (XRE) sequence present in the promoter regulatory region of variety of genes. Represses CYP1A1 by binding the XRE sequence and recruiting ANKRA2, HDAC4 and/or HDAC5. Autoregulates its expression by associating with its own XRE site..
Protein Sequence MPRTMIPPGECTYAGRKRRRPLQKQRPAVGAEKSNPSKRHRDRLNAELDHLASLLPFPPDIISKLDKLSVLRLSVSYLRVKSFFQVVQEQSSRQPAAGAPSPGDSCPLAGSAVLEGRLLLESLNGFALVVSAEGTIFYASATIVDYLGFHQTDVMHQNIYDYIHVDDRQDFCRQLHWAMDPPQVVFGQPPPLETGDDAILGRLLRAQEWGTGTPTEYSAFLTRCFICRVRCLLDSTSGFLTMQFQGKLKFLFGQKKKAPSGAMLPPRLSLFCIAAPVLLPSAAEMKMRSALLRAKPRADTAATADAKVKATTSLCESELHGKPNYSAGRSSRESGVLVLREQTDAGRWAQVPARAPCLCLRGGPDLVLDPKGGSGDREEEQHRMLSRASGVTGRRETPGPTKPLPWTAGKHSEDGARPRLQPSKNDPPSLRPMPRGSCLPCPCVQGTFRNSPISHPPSPSPSAYSSRTSRPMRDVGEDQVHPPLCHFPQRSLQHQLPQPGAQRFATRGYPMEDMKLQGVPMPPGDLCGPTLLLDVSIKMEKDSGCEGAADGCVPSQVWLGASDRSHPATFPTRMHLKTEPDSRQQVYISHLGHGVRGAQPHGRATAGRSRELTPFHPAHCACLEPTDGLPQSEPPHQLCARGRGEQSCTCRAAEAAPVVKREPLDSPQWATHSQGMVPGMLPKSALATLVPPQASGCTFLP
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
4Phosphorylation----MPRTMIPPGEC
----CCCCCCCCCCC		17.3750564199
12PhosphorylationMIPPGECTYAGRKRR
CCCCCCCCCCCCCCC		16.4729759185
13PhosphorylationIPPGECTYAGRKRRR
CCCCCCCCCCCCCCC		20.7929759185
24UbiquitinationKRRRPLQKQRPAVGA
CCCCCCCCCCCCCCC		56.8329967540
69PhosphorylationISKLDKLSVLRLSVS
HHHHHHHHHHHHHHH		25.5024719451
76PhosphorylationSVLRLSVSYLRVKSF
HHHHHHHHHHHHHHH		18.31-
77PhosphorylationVLRLSVSYLRVKSFF
HHHHHHHHHHHHHHH		9.07-
101PhosphorylationQPAAGAPSPGDSCPL
CCCCCCCCCCCCCCC		40.7725850435
105PhosphorylationGAPSPGDSCPLAGSA
CCCCCCCCCCCCCHH		24.4525850435
260PhosphorylationGQKKKAPSGAMLPPR
CCCCCCCCCCCCCCH		44.0029396449
281PhosphorylationAAPVLLPSAAEMKMR
HHCCCCCCHHHHHHH		39.8350564207
322UbiquitinationCESELHGKPNYSAGR
HHHHHCCCCCCCCCC		21.2429967540
322AcetylationCESELHGKPNYSAGR
HHHHHCCCCCCCCCC		21.2426051181
334PhosphorylationAGRSSRESGVLVLRE
CCCCCCCCCEEEEEE		32.8422985185
340UbiquitinationESGVLVLREQTDAGR
CCCEEEEEECCCCCC		26.8829967540
371UbiquitinationPDLVLDPKGGSGDRE
CCEEECCCCCCCCHH		75.4729967540
389UbiquitinationHRMLSRASGVTGRRE
HHHHHHHCCCCCCCC		32.4629967540
397PhosphorylationGVTGRRETPGPTKPL
CCCCCCCCCCCCCCC		31.5626852163
401PhosphorylationRRETPGPTKPLPWTA
CCCCCCCCCCCCCCC		51.7326852163
402UbiquitinationRETPGPTKPLPWTAG
CCCCCCCCCCCCCCC		47.9229967540
420UbiquitinationEDGARPRLQPSKNDP
CCCCCCCCCCCCCCC		11.0029967540
451PhosphorylationVQGTFRNSPISHPPS
CEEECCCCCCCCCCC		21.2526425664
454PhosphorylationTFRNSPISHPPSPSP
ECCCCCCCCCCCCCC		33.0723312004
458PhosphorylationSPISHPPSPSPSAYS
CCCCCCCCCCCCCCC		42.3229116813
460PhosphorylationISHPPSPSPSAYSSR
CCCCCCCCCCCCCCC		35.5123312004
462PhosphorylationHPPSPSPSAYSSRTS
CCCCCCCCCCCCCCC		44.1523312004
464PhosphorylationPSPSPSAYSSRTSRP
CCCCCCCCCCCCCCC		16.1223312004
465PhosphorylationSPSPSAYSSRTSRPM
CCCCCCCCCCCCCCC		17.0423312004
466PhosphorylationPSPSAYSSRTSRPMR
CCCCCCCCCCCCCCC		27.2323312004
491PhosphorylationLCHFPQRSLQHQLPQ
CCCCCHHHHHHCCCC		27.4328555341
577SumoylationFPTRMHLKTEPDSRQ
CCCEECEECCCCCCC		35.84-
577SumoylationFPTRMHLKTEPDSRQ
CCCEECEECCCCCCC		35.8428112733
595SumoylationISHLGHGVRGAQPHG
EEECCCCCCCCCCCC		4.18-
605PhosphorylationAQPHGRATAGRSREL
CCCCCCCCCCCCCCC		28.4324719451
623PhosphorylationHPAHCACLEPTDGLP
CCCCEEEECCCCCCC		4.7424719451
660SumoylationAEAAPVVKREPLDSP
HHHCCCCCCCCCCCC		51.8028112733
660UbiquitinationAEAAPVVKREPLDSP
HHHCCCCCCCCCCCC		51.8029967540
660SumoylationAEAAPVVKREPLDSP
HHHCCCCCCCCCCCC		51.80-
678SumoylationTHSQGMVPGMLPKSA
HCCCCCCCCCCCHHH		17.37-
678UbiquitinationTHSQGMVPGMLPKSA
HCCCCCCCCCCCHHH		17.3729967540
684PhosphorylationVPGMLPKSALATLVP
CCCCCCHHHHHHCCC		26.9522210691
688PhosphorylationLPKSALATLVPPQAS
CCHHHHHHCCCCCCC		29.1922210691
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

Oops, there are no upstream regulatory protein records of AHRR_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AHRR_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 AHRR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ESR1_HUMANESR1physical
18565642
HDAC4_HUMANHDAC4physical
17949687
HDAC5_HUMANHDAC5physical
17949687
ANRA2_HUMANANKRA2physical
17949687
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AHRR_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory