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http://purl.uniprot.org/SHA-384/4B317185A2DEFB333C7091D4A10C14FDF39C7D5F9773BF2F7EBFF0330479F0E05BD973C81805D75C35DFB34265300B7Fhttp://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/4B317185A2DEFB333C7091D4A10C14FDF39C7D5F9773BF2F7EBFF0330479F0E05BD973C81805D75C35DFB34265300B7Fhttp://www.w3.org/2000/01/rdf-schema#comment"Study reports the 2.0-A resolution crystal structure of the human ELL2 C-terminal domain bound to its 50-residue binding site on AFF4 the ELLBow. The ELLBow consists of an N-terminal helix followed by an extended hairpin and occupies most of the concave surface of ELL2. This surface is important for the ability of ELL2 to promote HIV-1 Tat-mediated proviral transcription."xsd:string
http://purl.uniprot.org/uniprot/#_633E42A5D7366A950FFCACE5CFE0BF9B8BB9827B5E30F3F3497C3D04CDFD31F2C437AFED5151E7E689ABDDFDE5D01466http://www.w3.org/1999/02/22-rdf-syntax-ns#subjecthttp://purl.uniprot.org/SHA-384/4B317185A2DEFB333C7091D4A10C14FDF39C7D5F9773BF2F7EBFF0330479F0E05BD973C81805D75C35DFB34265300B7F
http://purl.uniprot.org/uniprot/Q7Z656http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/4B317185A2DEFB333C7091D4A10C14FDF39C7D5F9773BF2F7EBFF0330479F0E05BD973C81805D75C35DFB34265300B7F
http://purl.uniprot.org/uniprot/#_Q7Z656-mappedCitation-28134250http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/4B317185A2DEFB333C7091D4A10C14FDF39C7D5F9773BF2F7EBFF0330479F0E05BD973C81805D75C35DFB34265300B7F