RelevanceMIIP has 3 SEG (segments of low compositional complexity) domains, an RGD motif, and several potential phosphorylation sites. The C-terminal region of IGFBP2 interacts with a central 44-amino acid sequence of MIIP. MIIP inhibits glioma cells invasion and down-regulates adhesion- and motility-associated genes such as NFKB2 and ICAM1. It exhibits opposing effects to IGFBP2 on cell invasion. There are 2 named isoforms due to alternative splicing. Isoform 1 is expressed in brain but underexpressed in glioma tissues, at protein level. Isoform 2 is not detected in normal organs, but is expressed in gliomas with increasing levels with glioma progression. On the contrary, at protein level, isoform 2 is not detected in gliomas, suggesting that this isoform is unstable in glioma cells. Isoform 2 is degraded by the ubiquitin-proteasome pathway.