MAGI1

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Protein-coding gene in the species Homo sapiens

title: "MAGI1" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public description: "Protein-coding gene in the species Homo sapiens" topic_path: "uncategorized" source: "https://en.wikipedia.org/wiki/MAGI1" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0

::summary Protein-coding gene in the species Homo sapiens ::

Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1 is an enzyme that in humans is encoded by the MAGI1 gene.

Function

The protein encoded by this gene is a member of the membrane-associated guanylate kinase homologue (MAGUK) family. MAGUK proteins participate in the assembly of multiprotein complexes on the inner surface of the plasma membrane at regions of cell–cell contact. The product of this gene may play a role as scaffolding protein at cell–cell junctions. Alternatively spliced transcript variants encoding different isoforms have been identified.

Interactions

MAGI1 has been shown to interact with:

ACCN3,
ATN1,
Actinin alpha 4,
Beta-catenin,
Brain-specific angiogenesis inhibitor 1,
Calcium-activated potassium channel subunit alpha-1,
FCHSD2,
LRP2, and
SYNPO.

References

(Jun 1998). "Cloning and characterization of BAI-associated protein 1: a PDZ domain-containing protein that interacts with BAI1". Biochemical and Biophysical Research Communications.
(Jul 1997). "cDNAs with long CAG trinucleotide repeats from human brain". Human Genetics.
"Entrez Gene: MAGI1 membrane associated guanylate kinase, WW and PDZ domain containing 1".
(Nov 2004). "PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have opposite effects on H+- gated current". The Journal of Biological Chemistry.
(Jun 1998). "Atrophin-1, the DRPLA gene product, interacts with two families of WW domain-containing proteins". Molecular and Cellular Neurosciences.
(Aug 2002). "Interaction of two actin-binding proteins, synaptopodin and alpha-actinin-4, with the tight junction protein MAGI-1". The Journal of Biological Chemistry.
(Apr 2000). "MAGI-1 interacts with beta-catenin and is associated with cell-cell adhesion structures". Biochemical and Biophysical Research Communications.
(Jul 2009). "MAGI-1 interacts with Slo1 channel proteins and suppresses Slo1 expression on the cell surface". American Journal of Physiology. Cell Physiology.
(Nov 2003). "Carom: a novel membrane-associated guanylate kinase-interacting protein with two SH3 domains". Oncogene.
(Apr 2001). "The membrane-associated guanylate kinase protein MAGI-1 binds megalin and is present in glomerular podocytes". Journal of the American Society of Nephrology.

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