|S-adenosylmethionine Decarboxylase||OKDB#: 2634|
|Synonyms:||AMD, SAM, SAMDC||Locus:||6q21-q22 in Homo sapiens|
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R-L INTERACTIONS MGI
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The biosynthesis of polyamines, which are universally essential for cellular functions, takes place from arginine and methionine and involves 4 distinct enzymes: spermidine synthase (EC 184.108.40.206), ornithine decarboxylase (165640), S-adenosyl-L-methionine decarboxylase (180980), and spermine synthase (300105).
NCBI Summary: The product of this gene is an important intermediate enzyme in polyamine biosynthesis. The polyamines spermine, spermidine, and putrescine are low-molecular-weight aliphatic amines essential for cellular proliferation and tumor promotion. This gene spans 22 kb comprised of 9 exons and 8 introns and encoding two species of mRNA of 2.1 and 3.4-3.6 kb originating from the use of two different polyadenylation signals. The pro-protein is an approximate 38.3 kDa which is known to undergo processing at amino acid 68 to yield two fragments of 32- and 6-kDa.
|Expression regulated by|
|Comment||FOund in an ovarian cDNA library.|
|Genomic Region||show genomic region|
|Phenotypes and GWAS||show phenotypes and GWAS|
|created:||Oct. 24, 2004, 9:55 a.m.||by:||
|last update:||March 4, 2009, 2:43 p.m.||by:||hsueh email:|
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