Browse our AMN Proteins (AMN)

Human Amnionless (AMN) interaction partners

1. Data indicate the crystal structure of amnionless (AMN) in complex with the amino-terminal region of intrinsic factor-cobalamin receptor (cubilin).

2. Study shows that cubilin mutations (novel and some previously reported) and all previously reported amnionless missense mutations resulted in endoplasmic reticulum retention and completely inhibited amnionless-dependent plasma membrane expression of cubilin.

3. heterozygous mutations in AMN in a family from the United Kingdom with clinical features of Imerslund-Grasbeck Syndrome

4. Our genetic screening of 154 families of patients with inherited cobalamin malabsorption revealed population-specific mutations, mutational hotspots, and functionally distinct regions in the three causal genes: CUBN, AMN, and GIF.

5. We present evidence that this founder mutation causes over 50% of the Imerslund-Grasbeck syndrome (IGS) cases among Arabic, Turkish, and Sephardic Jewish families, and the mutation is as old as human civvlization.

6. amnionless is essential for the correct luminal expression of cubilin in humans.

7. homozygous mutations affecting exons 1-4 of human AMN lead to megaloblastic anemia 1

8. cubilin and amnionless are subunits of a novel cubilin/amnionless (cubam) complex

9. Recurrent spontaneous abortions may be caused by mutations in the Amnionless gene.

10. This review summarizes recent data on the biological function of amnionless and focuses on its implication in embryonic nutrition and central nervous system malformations.

Mouse (Murine) Amnionless (AMN) interaction partners

1. AMN may participate in meiosis in early spermatocytes and in functional differentiation of adult Leydig cells through the mediation of vitamin B(12) transport in the mouse testes

2. Amn is an essential component of the Cubn receptor complex