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0EPAS1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionEndothelial pas domain protein 1 (epas-1) (member of pas protein 2) (mop2) (hypoxia-inducible factor 2 alpha) (hif-2 alpha) (hif2 alpha) (hif-1 alpha-like factor) (hlf).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0035035 histone acetyltransferase binding (IPI)
0005515 protein binding (IPI)
0003705 RNA polymerase II transcription factor acti... (TAS)
0003713 transcription coactivator activity (TAS)
0007165 signal transduction (TAS)
0006366 transcription from RNA polymerase II promoter (TAS)

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Domain Architecture (Details)
InterPro domains unassigned to SynO:
The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs . The PAS fold appears in archaea.ubacteria and eukarya. The PAS domain contains a sensory box.r S-box domain that occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL .AD in the redox potential sensor NifL .nd a 4-hydroxycinnamyl chromophore in photoactive yellow protein . Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. This domain has been found in the gene product of the madA gene of the filamentous zygomycete fungus Phycomyces blakesleeanus. It has been shown that MadA encodes a blue-light photoreceptor for phototropism and other light responses. The gene is involved in the phototropic responses associated with sporangiophore growth; they exhibit phototropism by bending toward near-UV and blue wavelengths and away from far-UV wavelengths in a manner that is physiologically similar to plant phototropic responses .
  IPR013655:PAS fold-3
PAS domains are involved in many signalling proteins where theyare used as a signal sensor domain. PAS domains appear in archaea.acteria and eukaryotes. Several PAS-domain proteins are known todetect their signal by way of an associated cofactor. Haeme.lavin.nd a 4-hydroxycinnamyl chromophore are used in differentproteins. The PAS domain was named after three proteins that itoccurs in: Per- period circadian proteinArnt- Ah receptor nuclear translocator proteinSim- single-minded protein.PAS domains are often associated withPAC domains . It appears that these domains are directly linked.nd that together they form the conserved 3D PAS fold. The division between the PAS and PAC domains is caused by major differences in sequences in the region connecting these two motifs . In human PAS kinase.his region has been shown to be very flexible.nd adopts different conformations depending on the bound ligand .Probably the most surprising identification of a PAS domain was that inEAG-like K+-channels .
PAC motifs occur C-terminal to a subset of all known PAS motifs (see ). It is proposed to contribute to the PAS domain fold .
  IPR001610:PAC motif
Basic helix-loop-helix proteins (bHLH) are a group of eukaryotic transcription factors that exert a determinative influence in a variety of developmental pathways. These transcription factors are characterised by a highly evolutionary conserved bHLH domain that mediates specific dimerisation . They facilitate the conversion of inactive monomers to trans-activating dimers at appropriate stages of development . The bHLH proteins can be classified into discrete categories. One such subdivision according to dimerisation.NA binding and expression characteristics defines seven groups . Class I proteins form dimers within the group or with class II proteins. Class II can only form heterodimers with class I factors. Class III factors are characterised by the presence of a leucine zipper () adjacent to the bHLH domain. Class IV factors may form homodimers or teterodimers with class III proteins. Class V and class VI proteins act as regulators of class I and class II factors and class VII proteins have a PAS domain ().
  IPR001092:Basic helix-loop-helix dimerisation region bHLH
The Ah (dioxin) receptor nuclear translocator protein (Arnt) belongs to the basichelix-loop-helix (bHLH) family of transcription factors and is required forAh receptor function. The Ah receptor binds.nd mediates the carcinogeniceffects of a variety of environmental pollutants.ncluding 2...-tetrachlorodibenzo-p-dioxin and polycyclic aromatic hydrocarbons. Arnt is a structural component of theXRE-binding form of the Ah receptor. These proteins are class VII members of the basic helix-loop-helix (bHLH) family. The bHLH domain may be responsible for interacting with both the XRE and the ligand-bindingsubunit .The activated Ah receptor and Arnt protein bind DNA as a heterodimer. Both proteins contain PAS homology regions.hich in Drosophila PER and SIM proteins function as dimerisation domains .
  IPR001067:Nuclear translocator
The helix-loop-helix (HLH) DNA-binding domain consists of a closed bundleof four helices in a left-handed twist with two crossover connections. TheHLH domain directs dimerisation.nd is juxtaposed to basic regions tocreate a DNA interaction interface surface that recognises specific DNAsequences. Basic region/HLH (bHLH) proteins regulate diverse biologicalpathways . bHLH proteins include MyoD .REBPs (sterol regulatory element binding proteins).nd yeast Pho4 (phosphatase system) .In certain proteins the bHLH domain contains a leucine-zipper motif. ThebHLH/leucine zipper (bHLHZip) domain specifies dimerisation within a networkof proteins and determines sequence-specific DNA binding . bHLHZip domains occur in the transcription factors and Usf . This entry is bHLHZip.hich covers the bHLH domain and the leucine zipper motif.hen present.
  IPR011598:Helix-loop-helix DNA-binding
SequencesProtein: EPAS1_HUMAN (870 aa)
mRNA: NM_001430
Local Annotation
Synapse Ontology
calcium-regulated transcription factor
sdb:0215 calcium-regulated transcription factor  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 172 residues, 46378066-46378580Exon2: 65 residues, 46427515-46427706Exon3: 52 residues, 46436793-46436945Exon4: 30 residues, 46437366-46437451Exon5: 41 residues, 46441280-46441399Exon6: 70 residues, 46441527-46441733Exon7: 37 residues, 46450469-46450576Exon8: 51 residues, 46456332-46456480Exon9: 73 residues, 46457181-46457396Exon10: 66 residues, 46458536-46458730Exon11: 39 residues, 46459299-46459410Exon12: 165 residues, 46460869-46461360Exon13: 44 residues, 46462238-46462365Exon14: 40 residues, 46462617-46462732Exon15: 60 residues, 46463067-46463241Exon16: 731 residues, 46465151-46467339Exon17: 2 residues, -Jump to EPAS1_HUMAN  
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Loci Cluster (Details)Loci: 3162 46697811-46705687 ~-8K 20390(+)Loci: 3161 46378066-46467339 ~-89K 20384(EPAS1)(+)Link out to UCSC