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MARCH6 encodes a member of a family of membrane-associated E3 ubiquitin ligases containing RING-CH-type zinc finger motifs. Additionally we are shipping MARCH6 Antibodies (57) and many more products for this protein.
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Data suggest that human MARCH6 and Saccharomyces cerevisiae Doa10 ubiquitin ligases are functionally similar.
Loss of MARCH6 increases expression of SREBP-regulated genes involved in cholesterol biosynthesis and lipoprotein uptake.
Data suggest that unsaturated fatty acids (oleate; oleoyl-CoA) stabilize SM/SQLE (squalene monooxygenase (show SQLE Proteins); catalyzes 1st oxygenation step in cholesterol synthesis) most likely via inhibition of poly-ubiquitination by MARCH6.
MARCH6 and squalene monooxygenase (SM) physically interact, and consistent with MARCH6 acting as an E3 ligase, its overexpression reduces SM abundance in a RING-dependent manner.
analysis of yeast endoplasmic reticulum-localized ubiquitin ligase Doa10 and comparison with its human ortholog TEB4
TEB4 interacts with and mediates loss of type 2 iodothyronine deiodinase (show DIO2 Proteins) (D2)activity, indicating that D2 ubiquitination and degradation can be tissue specific, depending on WSB-1 (show WSB1 Proteins) and TEB4 expression levels.
This gene encodes a member of a family of membrane-associated E3 ubiquitin ligases containing RING-CH-type zinc finger motifs. Ubiquitination of type II deiodinase by the encoded protein is an important regulatory step in thyroid hormone signalling. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
E3 ubiquitin-protein ligase MARCH6
, membrane-associated RING finger protein 6
, membrane-associated RING-CH protein VI
, RING finger protein 176
, doa10 homolog
, membrane-associated RING-CH finger protein 6