BACKGROUND: Glycoprotein 210 (GP210) is a transmembrane component of the nuclear 
pore complex of metazoans, with a short carboxyterminus protruding towards the 
cytoplasm. Its function is unknown, but it is considered to be a major 
structural component of metazoan nuclear pores. Yet, our previous findings 
showed pronounced differences in expression levels in embryonic mouse tissues 
and cell lines. In order to identify factors regulating GP210, the genomic 
organization of human GP210 was analyzed in silico.
RESULTS: The human gene was mapped to chromosome 3 and consists of 40 exons 
spread over 102 kb. The deduced 1887 amino acid showed a high degree of 
alignment homology to previously reported orthologues. Experimentally we defined 
two transcription initiation sites, 18 and 29 bp upstream of the ATG start 
codon. The promoter region is characterized by a CpG island and several 
consensus binding motifs for gene regulatory transcription factors, including 
clustered sites associated with Sp1 and the Wilms' tumor suppressor gene zinc 
finger protein (WT1). In addition, distal to the translation start we found a 
(GT)n repetitive sequence, an element known for its ability to bind WT1. 
Homologies for these motifs could be identified in the corresponding mouse 
genomic region. However, experimental tetracycline dependent induction of WT1 in 
SAOS osteosarcoma cells did not influence GP210 transcription.
CONCLUSION: Although mouse GP210 was identified as an early response gene during 
induced metanephric kidney development, and WT1 binding sites were identified in 
the promoter region of the human GP210 gene, experimental modulation of WT1 
expression did not influence expression of GP210. Therefore, WT1 is probably not 
regulating GP210 expression. Instead, we suggest that the identified Sp binding 
sites are involved.