A glycine-rich domain of hnRNP H/F promotes nucleocytoplasmic shuttling and nuclear import through an interaction with transportin 1.
Van Dusen
Courtney M
CM
Department of Microbiology and Molecular Genetics, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee, WI 53226, USA.
Yee
Lily
L
McNally
Lisa M
LM
McNally
Mark T
MT
D021581:Active Transport, Cell Nucleus / Q000502:physiology*; D017398:Alternative Splicing; D000595:Amino Acid Sequence; D002467:Cell Nucleus / Q000737:chemistry / Q000378:metabolism; D005998:Glycine / Q000378:metabolism*; D006367:HeLa Cells; D034541:Heterogeneous-Nuclear Ribonucleoprotein Group F-H / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D009154:Mutation; D019913:Nuclear Localization Signals / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D028961:beta Karyopherins / Q000235:genetics / Q000378:metabolism*
D034541:Heterogeneous-Nuclear Ribonucleoprotein Group F-H; D019913:Nuclear Localization Signals; D011993:Recombinant Fusion Proteins; C108121:TNPO1 protein, human; D028961:beta Karyopherins; D005998:Glycine