Sp100 nuclear antigen
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Two proteins, Sp100 and promyelocytic leukemia (PML) factor are localized to punctate domains in the nucleus (nuclear dots or nuclear bodies). These domains (few to 20) were found to form a donut-shaped structure when cells were starved of amino acids. In particular, deprivation of cystine results in most pronounced changes. Two other proteins, PIC1/SUMO-1, that also interact with nuclear pore complex factors also interact with these two proteins. In addition Sp100 interacts with a chromatin binding protein, HP1 alpha.
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Sp100 splicoforms
Some Sp100 variants contain a domain similar to two interferon-inducible nuclear phosphoproteins, suppressin and DEAF1. This defines a novel protein motif, the HNPP-box. Another class of variants has high mobility group 1 (HMG1) protein sequence as a domain. Both major classes of Sp100 splice variant proteins localize in part to nuclear dots/PML bodies and other nuclear domains.