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Experimental & Molecular Medicine ; : 828-838, 2007.
Article in English | WPRIM | ID: wpr-62080

ABSTRACT

KM-HN-1 is a C-terminal coiled-coil domain containing protein previously referred to as image clone MGC33607. This protein has been previously identified as a cancer/testis antigen and reported as nuclear and chromatin localizing protein. We raised polyclonal antisera with the GST fusion protein and identified them as a 105 kDa protein. Motif analysis showed that this protein harbors the leucine zipper motif in internal 1/3 region and the coiled-coil domain in the C-terminal region. Using the full length and various deletion mutants, we determined the motif that governs the subcellular localization of KM-HN-1. Immunofluorescence staining of the endogenous KM-HN-1 and various kinds of GFP-tagged KM-HN-1 revealed that KM-HN-1 localizes to the centrosomes as well as nucleus. The centrosomal localization-determining region of this protein is C-terminal coiled-coil domain in which the leucine zipper motif and the nuclear export signal (NES) harbor.


Subject(s)
Humans , Amino Acid Motifs/physiology , Amino Acid Sequence , Antigens, Neoplasm/chemistry , Cells, Cultured , Centrosome/metabolism , Fluorescent Antibody Technique , Leucine Zippers/physiology , Molecular Sequence Data , Mutation , Nuclear Proteins/chemistry , Protein Conformation , Protein Structure, Tertiary , Sequence Analysis, Protein
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