The MIG-6 gene is composed of 4 exons, and its coding region spans from exon 2 to within exon 4.

MIG-6 transcription can be rapidly up-regulated by many stress stimuli such as mechanical forces, injury and hypoxia, and by serum as well as various growth factors including EGF and HGF/SF. It is regulated during cell cycle progression, and peaks at the mid-G1 phase. The transcription results in a 3.1-kb mRNA.

MIG-6 is a 58-kDa non-kinase scaffolding adaptor protein consisting of 462 amino-acids. Several conserved protein-protein interaction motifs/domains are present in this protein: a CRIB domain is in the N-terminus, and has been shown to interact with CDC42 and IκBα ; multiple proline-rich motifs are present in the middle of the molecule, and can bind to SH3 domain containing proteins like GRB2; and a 14-3-3 protein binding motif and two PEST sequences are also present. A large portion of its C-terminus (AH domain) shares a high homology with ACK1 kinase, and an EGFR-binding domain is mapped within this region.

MIG-6 is highly expressed in the liver and kidney. Moderate to low expression is observed in the brain, lung, placenta, heart, thymus, and some other tissues.

It is mainly localized in the cytoplasm.

MIG-6 is a negative feedback regulator of EGFR and Met receptor tyrosine kinase signaling. MIG-6 inhibits EGFR-mediated cell transformation and cell cycle progression in NIH3T3 cells. It can physically interact with EGFR, causing inhibition of EGFR phosphorylation and downstream activation. This inhibition is likely due to a blockage of EGFR dimer formation by MIG-6, as a crystal structure reveals binding of MIG-6 to the EGFR kinase domain interface. MIG-6 inhibits Met-mediated cell migration, likely through blocking HGF/SF-induced CDC42 activation (although it does not physically interact with Met). Expression of MIG-6 has also been shown to activate NFκB by sequestering IκBα. The involvement of other MIG-6-interacting molecules in regulating the signaling output remains to be determined.
MIG-6 may function as a tumor suppressor gene, and is likely to play an important role in skin morphogenesis, tissue homeostasis and stress response. Disruption of Mig-6 results in hyperproliferation of the cells in the tissues like joint, gallbladder and skin. Mice with Mig-6 deficiency are prone to the formation of lung, gallbladder, bile duct, and skin cancers, and they develop early onset degenerative joint disease in heavily used joints. Reduced expression of MIG-6 has been observed in several human cancers including breast, ovarian, and skin cancers. While rare, mutations in MIG-6 have also been identified in human lung cancer.

A heterozygous germline mutation at MIG-6 codon 373 (Ala → Val) has been identified in a primary lung cancer patient with squamous cell carcinoma.

Two somatic mutations have been identified in non-small cell lung cancer cell lines: a nonsense mutation at codon 83 (Glu → stop codon) in the NCI-H322 adenocarcinoma cell line; and a missense mutation at codon 109 (Asp → Asn) in the NCI-H226 squamous cell carcinoma cell line.