ARNT_HUMAN - dbPTM
ARNT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARNT_HUMAN
UniProt AC P27540
Protein Name Aryl hydrocarbon receptor nuclear translocator
Gene Name ARNT
Organism Homo sapiens (Human).
Sequence Length 789
Subcellular Localization Nucleus.
Protein Description Required for activity of the Ah (dioxin) receptor. This protein is required for the ligand-binding subunit to translocate from the cytosol to the nucleus after ligand binding. The complex then initiates transcription of genes involved in the activation of PAH procarcinogens. The heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters and functions as a transcriptional regulator of the adaptive response to hypoxia (By similarity). 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: 28396409]
Protein Sequence MAATTANPEMTSDVPSLGPAIASGNSGPGIQGGGAIVQRAIKRRPGLDFDDDGEGNSKFLRCDDDQMSNDKERFARSDDEQSSADKERLARENHSEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVSHMKSLRGTGNTSTDGSYKPSFLTDQELKHLILEAADGFLFIVSCETGRVVYVSDSVTPVLNQPQSEWFGSTLYDQVHPDDVDKLREQLSTSENALTGRILDLKTGTVKKEGQQSSMRMCMGSRRSFICRMRCGSSSVDPVSVNRLSFVRNRCRNGLGSVKDGEPHFVVVHCTGYIKAWPPAGVSLPDDDPEAGQGSKFCLVAIGRLQVTSSPNCTDMSNVCQPTEFISRHNIEGIFTFVDHRCVATVGYQPQELLGKNIVEFCHPEDQQLLRDSFQQVVKLKGQVLSVMFRFRSKNQEWLWMRTSSFTFQNPYSDEIEYIICTNTNVKNSSQEPRPTLSNTIQRPQLGPTANLPLEMGSGQLAPRQQQQQTELDMVPGRDGLASYNHSQVVQPVTTTGPEHSKPLEKSDGLFAQDRDPRFSEIYHNINADQSKGISSSTVPATQQLFSQGNTFPPTPRPAENFRNSGLAPPVTIVQPSASAGQMLAQISRHSNPTQGATPTWTPTTRSGFSAQQVATQATAKTRTSQFGVGSFQTPSSFSSMSLPGAPTASPGAAAYPSLTNRGSNFAPETGQTAGQFQTRTAEGVGVWPQWQGQQPHHRSSSSEQHVQQPPAQQPGQPEVFQEMLSMLGDQSNSYNNEEFPDLTMFPPFSE
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
2Acetylation------MAATTANPE
------CCCCCCCHH		17.3222814378
11PhosphorylationTTANPEMTSDVPSLG
CCCCHHHCCCCCCCC		21.80-
58AcetylationDDGEGNSKFLRCDDD
CCCCCCCCEEECCCH		53.0325953088
58UbiquitinationDDGEGNSKFLRCDDD
CCCCCCCCEEECCCH		53.03-
58SumoylationDDGEGNSKFLRCDDD
CCCCCCCCEEECCCH		53.0328112733
68PhosphorylationRCDDDQMSNDKERFA
ECCCHHCCCCHHHHH		35.9219664994
77PhosphorylationDKERFARSDDEQSSA
CHHHHHCCHHHCCHH		46.0829255136
82PhosphorylationARSDDEQSSADKERL
HCCHHHCCHHHHHHH		25.9921712546
83PhosphorylationRSDDEQSSADKERLA
CCHHHCCHHHHHHHH		39.9321712546
95PhosphorylationRLARENHSEIERRRR
HHHHHCHHHHHHHHH		52.4229083192
120PhosphorylationSDMVPTCSALARKPD
HHHHCHHHHHCCCCC		28.88-
125AcetylationTCSALARKPDKLTIL
HHHHHCCCCCHHHHH		52.5425953088
128AcetylationALARKPDKLTILRMA
HHCCCCCHHHHHHHH		56.9325953088
143MethylationVSHMKSLRGTGNTST
HHHHHHHCCCCCCCC		47.95-
149PhosphorylationLRGTGNTSTDGSYKP
HCCCCCCCCCCCCCC		28.6228555341
155UbiquitinationTSTDGSYKPSFLTDQ
CCCCCCCCCCCCCHH		35.56-
240UbiquitinationTGRILDLKTGTVKKE
HHCEEECCCCCCCCC		44.57-
245SumoylationDLKTGTVKKEGQQSS
ECCCCCCCCCCCHHH		44.97-
245SumoylationDLKTGTVKKEGQQSS
ECCCCCCCCCCCHHH		44.9712354770
251PhosphorylationVKKEGQQSSMRMCMG
CCCCCCHHHHCHHHC		20.4323403867
252PhosphorylationKKEGQQSSMRMCMGS
CCCCCHHHHCHHHCC		13.1822210691
259PhosphorylationSMRMCMGSRRSFICR
HHCHHHCCCCCEEEE		9.5323403867
262PhosphorylationMCMGSRRSFICRMRC
HHHCCCCCEEEECCC		20.1824719451
278PhosphorylationSSSVDPVSVNRLSFV
CCCCCCCCHHHHHHH		21.0429449344
283PhosphorylationPVSVNRLSFVRNRCR
CCCHHHHHHHHHHHH		20.6124719451
346PhosphorylationAIGRLQVTSSPNCTD
EEECEEEECCCCCCC		15.5529978859
347PhosphorylationIGRLQVTSSPNCTDM
EECEEEECCCCCCCC		44.9628348404
348PhosphorylationGRLQVTSSPNCTDMS
ECEEEECCCCCCCCC		15.6929978859
352PhosphorylationVTSSPNCTDMSNVCQ
EECCCCCCCCCCCCC		41.1829978859
355PhosphorylationSPNCTDMSNVCQPTE
CCCCCCCCCCCCCHH		28.9929978859
417UbiquitinationDSFQQVVKLKGQVLS
HHHHHHHHHHCCEEE		45.70-
417UbiquitinationDSFQQVVKLKGQVLS
HHHHHHHHHHCCEEE		45.70-
419UbiquitinationFQQVVKLKGQVLSVM
HHHHHHHHCCEEEEE		41.39-
419UbiquitinationFQQVVKLKGQVLSVM
HHHHHHHHCCEEEEE		41.39-
487PhosphorylationQRPQLGPTANLPLEM
CCCCCCCCCCCCCCC		26.7829978859
496PhosphorylationNLPLEMGSGQLAPRQ
CCCCCCCCCCCCCHH		23.2729978859
508PhosphorylationPRQQQQQTELDMVPG
CHHHHCCCHHCCCCC		33.8929978859
539PhosphorylationTTTGPEHSKPLEKSD
ECCCCCCCCCCCCCC		34.0224719451
540AcetylationTTGPEHSKPLEKSDG
CCCCCCCCCCCCCCC		56.3726051181
544UbiquitinationEHSKPLEKSDGLFAQ
CCCCCCCCCCCCCCC		62.62-
558PhosphorylationQDRDPRFSEIYHNIN
CCCCCCHHHHHHCCC		25.1021945579
561PhosphorylationDPRFSEIYHNINADQ
CCCHHHHHHCCCCCC		5.6921945579
593PhosphorylationQGNTFPPTPRPAENF
CCCCCCCCCCCHHHC		31.97-
626O-linked_GlycosylationGQMLAQISRHSNPTQ
HHHHHHHHHCCCCCC		16.3230059200
629O-linked_GlycosylationLAQISRHSNPTQGAT
HHHHHHCCCCCCCCC		43.3130059200
636PhosphorylationSNPTQGATPTWTPTT
CCCCCCCCCCCCCCC		28.24-
638PhosphorylationPTQGATPTWTPTTRS
CCCCCCCCCCCCCCC		37.30-
640PhosphorylationQGATPTWTPTTRSGF
CCCCCCCCCCCCCCC		17.15-
642O-linked_GlycosylationATPTWTPTTRSGFSA
CCCCCCCCCCCCCCH		27.7130059200
643O-linked_GlycosylationTPTWTPTTRSGFSAQ
CCCCCCCCCCCCCHH		24.8430059200
645O-linked_GlycosylationTWTPTTRSGFSAQQV
CCCCCCCCCCCHHHH		41.9430059200
648PhosphorylationPTTRSGFSAQQVATQ
CCCCCCCCHHHHHHH		28.7928555341
654PhosphorylationFSAQQVATQATAKTR
CCHHHHHHHHCCCCC		21.6323401153
657PhosphorylationQQVATQATAKTRTSQ
HHHHHHHCCCCCCCC		20.9028555341
669PhosphorylationTSQFGVGSFQTPSSF
CCCCCCCCCCCCCCC		16.27-
686PhosphorylationMSLPGAPTASPGAAA
CCCCCCCCCCCCCCC		38.9528348404
688PhosphorylationLPGAPTASPGAAAYP
CCCCCCCCCCCCCCC		26.7528348404
788PhosphorylationLTMFPPFSE------
CCCCCCCCC------		48.44-
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
77SPhosphorylationKinaseCSNK2A1P68400
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARNT_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 ARNT_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AHR_HUMANAHRphysical
7628454
NCOA2_HUMANNCOA2physical
12024042
SIM1_HUMANSIM1physical
9020169
SIM2_HUMANSIM2physical
9020169
TEBP_HUMANPTGES3physical
11259606
AIP_HUMANAIPphysical
11259606
SIM1_HUMANSIM1physical
11782478
SIM2_HUMANSIM2physical
11782478
HIF1A_HUMANHIF1Aphysical
11782478
T2FA_HUMANGTF2F1physical
8794892
T2FB_HUMANGTF2F2physical
8794892
AHR_HUMANAHRphysical
9887096
AHRR_HUMANAHRRphysical
9887096
HIF1A_HUMANHIF1Aphysical
9079689
EPAS1_HUMANEPAS1physical
9079689
BRCA1_HUMANBRCA1physical
16567799
HIF1A_HUMANHIF1Aphysical
20049704
CUL2_HUMANCUL2physical
20049704
ELOB_HUMANTCEB2physical
20049704
AHR_HUMANAHRphysical
19390533
NCOA7_HUMANNCOA7physical
10395741
NCOR2_HUMANNCOR2physical
10395741
HEY2_HUMANHEY2physical
10692439
HEY1_HUMANHEY1physical
10692439
CLOCK_MOUSEClockphysical
9704006
MTA3_HUMANMTA3physical
21988832
DBLOH_HUMANDIABLOphysical
21988832
BACD2_HUMANTNFAIP1physical
21988832
GEMI_HUMANGMNNphysical
21988832
IRAK4_HUMANIRAK4physical
21988832
LSM8_HUMANLSM8physical
21988832
STRBP_HUMANSTRBPphysical
21988832
NCOA1_HUMANNCOA1physical
12024042
TBB2A_HUMANTUBB2Aphysical
20006590
JUN_HUMANJUNphysical
19203995
ESR1_HUMANESR1physical
15837795
AHR_HUMANAHRphysical
28514442
HSP7C_HUMANHSPA8physical
28514442
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
There are no disease associations of PTM sites.
Regulatory Network of ARNT_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND MASSSPECTROMETRY.

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