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0EWS_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionRna-binding protein ews (ews oncogene) (ewing sarcoma breakpoint region 1 protein).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0003723 RNA binding (TAS)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Many eukaryotic proteins that are known or supposed to bind single-stranded RNA contain one or more copies of a putative RNA-binding domain of about 90 amino acids. This is known as the eukaryotic putative RNA-binding region RNP-1 signature or RNA recognition motif (RRM). RRMs are found in a variety of RNA binding proteins.ncluding heterogeneous nuclear ribonucleoproteins (hnRNPs).roteins implicated in regulation of alternative splicing.nd protein components of small nuclear ribonucleoproteins (snRNPs). The RRM in heterodimeric splicing factor U2 snRNP auxiliary factor (U2AF) appears to have two RRM-like domains with specialized features for protein recognition . The motif also appears in a few single stranded DNA binding proteins. The RRM structure consists of four strands and two helices arranged in an alpha/beta sandwich.ith a third helix present during RNA binding in some cases .
  IPR000504:RNA-binding region RNP-1 (RNA recognition motif)
Ran is an evolutionary conserved member of the Ras superfamily that regulates all receptor-mediated transport between the nucleus and the cytoplasm. Ran binding protein 2 (RanBP2) is a 358-kDa nucleoporin located on the cytoplasmic side of the nuclear pore complex which plays a role in nuclear protein import . RanBP2 contains multiple zinc fingers which mediate binding to RanGDP .
  IPR001876:Zinc finger, RanBP2-type
High mobility group (HMG) proteins are a family of relatively low molecular weight non-histone componentsin chromatin. HMG-I and HMG-Y are proteins of about 100 amino acid residues which are produced by thealternative splicing of a single gene. HMG-I proteins bind preferentially to the minor groove of AT-richregions in double-stranded DNA . It is suggested that these proteins could functionin nucleosome phasing and in the 3 end processing of mRNA transcripts. They are also involved in thetranscription regulation of genes containing.r in close proximity to.T-rich regions. DNA-binding of these.nd several related.roteins is effected by an 11-residue domain known as an AT-hook. Within known HMG-Iproteins are found three highly conserved regions.losely related to the consensus sequence TPKRPRGRPKK. Asynthetic oligopeptide with this sequence specifically binds to substrate DNA in a manner reminiscent ofintact HMG-I proteins. Structure predictions suggest that the peptide has a secondary structure similar tothe anti-tumour and anti-viral drugs netropsin and distamycin.nd to the dye Hoechst 33258. These ligands.hich also preferentially bind to AT-rich DNA.ffectively compete with both the synthetic peptide and theHMG-I proteins for DNA binding. The peptide also contains novel structural features such as a predicted Asxbend.r hook.t its N-terminus.nd laterally-projecting cationic Arg/Lys bristles.hich may play arole in the binding of HMG-I proteins. The predicted peptide structure.he AT-hook.s a previouslyundescribed DNA-binding motif .
  IPR000637:HMG-I and HMG-Y, DNA-binding
This group represents a predicted RNA-binding protein.WS type.
  IPR011368:Predicted RNA-binding protein, EWS
This entry represents nucleotide-binding domains with an alpha-beta plait structure.hich consists of either a ferredoxin-like (beta-alpha-beta)2 fold.uch as that found in RNA-binding domains of various ribonucleoproteins or in viral DNA-binding domains . or a beta-(alpha)-beta-alpha-beta(2) fold.uch as that found in the ribosomal protein L23 .
  IPR012677:Nucleotide-binding, alpha-beta plait
SequencesProtein: EWS_HUMAN (656 aa)
mRNA: NM_005243
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
activation of protein kinase C
sdb:0206 activation of protein kinase C  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 19 residues, 27994282-27994338Exon2: 14 residues, 27998204-27998241Exon3: 19 residues, 27998368-27998420Exon4: 43 residues, 27999729-27999853Exon5: 64 residues, 28004018-28004205Exon6: 58 residues, 28008378-28008546Exon7: 72 residues, 28012911-28013123Exon8: 62 residues, 28014594-28014775Exon9: 14 residues, 28017550-28017588Exon10: 13 residues, 28018125-28018158Exon11: 41 residues, 28018476-28018595Exon12: 45 residues, 28022228-28022358Exon13: 43 residues, 28023816-28023939Exon14: 56 residues, 28024722-28024885Exon15: 34 residues, 28025223-28025321Exon16: 86 residues, 28025588-28025841Exon17: 133 residues, 28026111-28026505Exon18: 2 residues, -Jump to EWS_HUMAN  
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Loci Cluster (Details)Loci: 4562 28053670-28114569 ~-61K 24460(AP1B1)(-)Loci: 3306 28196906-28217275 ~-20K 24467(NEFH)(+)Loci: 3305 27994282-28026505 ~-32K 24453(EWSR1)(+)Link out to UCSC