Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Aryl hydrocarbon receptor nuclear translocator  

UniProtKB / Swiss-Prot ID :  ARNT_HUMAN

Gene Name (Synonyms) : 
ARNT, BHLHE2  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. 

Protein Function :  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 with HIF1A or EPAS1/HIF2A functions as a transcriptional regulator of the adaptive response to hypoxia. 

Protein Sequence MAATTANPEMTSDVPSLGPAIASGNSGPGIQGGGAIVQRAIKRRPGLDFDDDGEGNSKFLRCDDDQMSND...
Predicted Secondary Structure CCCCCCCCHHHCCCCCCCCCCCCCCCCCCCCCCCCEEECCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCC...
Protein Variant
LocationDescription
430R -> Q (in dbSNP:rs2229175). VAR_024280
435E -> K (in dbSNP:rs2229176). VAR_049537
511D -> N (in dbSNP:rs1805133). VAR_014819
517D -> E (in dbSNP:rs10305741). VAR_018906
706P -> L (in dbSNP:rs2275237). VAR_020189
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAATTA
---CCCCCC
17.32UniProtKB
Link-
68PhosphoserineDDQMSNDKE
CCCCCCCCC
35.92HPRD
Link-
68PhosphoserineDDQMSNDKE
CCCCCCCCC
35.92Phosphositeplus
Link-
77PhosphoserineRFARSDDEQ
CCCCCCCCC
46.08PhosphoELM
Link-
77PhosphoserineRFARSDDEQ
CCCCCCCCC
46.08Phosphositeplus
Link-
77PhosphoserineRFARSDDEQ
CCCCCCCCC
46.08SysPTM
Link-
77Phosphoserine (CSNK2A1)RFARSDDEQ
CCCCCCCCC
46.08HPRD
Link-
77Phosphoserine.RFARSDDEQ
CCCCCCCCC
46.08UniProtKB
Link-
82PhosphoserineDDEQSSADK
CCCCCCCCH
25.99SysPTM
Link-
83PhosphoserineDEQSSADKE
CCCCCCCHH
39.93SysPTM
Link-
245Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)TGTVKKEGQ
CCCCCCCCC
44.97HPRD
Link-
245Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)TGTVKKEGQ
CCCCCCCCC
44.97HPRD
Link-
348PhosphoserineQVTSSPNCT
CCCCCCCCC
15.69Phosphositeplus
Link-
561PhosphotyrosineFSEIYHNIN
CCCCCCCCC
5.69Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
AHR_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
EBI-80826
EBI-80850
EBI-36811
intact10395741
10395741
10395741
10395741
PML_HUMANin vitroHPRD:00524HPRD12354770
ARNT_HUMANin vitroHPRD:00524HPRD11502749
12354770
ARNT2_HUMANyeast 2-hybridHPRD:00524HPRD8927054
HEY1_HUMANyeast 2-hybridHPRD:00524HPRD10692439
HEY2_HUMANyeast 2-hybridHPRD:00524HPRD10692439
AHR_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:00524HPRD8384309
7488247
7628454
11768231
12024042
SIM2_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:00524HPRD9020169
9271372
11782478
EP300_HUMANin vivoHPRD:00524HPRD10999956
ESR1_HUMANin vitroHPRD:00524HPRD15837795
SMAD9_HUMANyeast 2-hybridHPRD:00524HPRD15231748
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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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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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures