AMD1 Gene: S-Adenosylmethionine Decarboxylase 1 - Function, Disease Associations, and Expression
Comprehensive biomedical overview of AMD1, including genomic context, protein function, expression profiles, and clinical significance.
Gene Information Card
| Symbol | AMD1 |
|---|---|
| Full Name | S-adenosylmethionine decarboxylase 1 |
| Gene Type | protein-coding |
| Chromosomal Location | 6q21 |
| NCBI Gene ID | 262 ncbi.nlm.nih.gov/gene/262 |
| Ensembl ID | ENSG00000167768 |
| UniProt ID | P17707 |
| OMIM ID | 180980 |
| HGNC ID | 457 |
| Aliases | AdoMetDC, SAMDC, MGC117386 |
Description
The AMD1 gene encodes S-adenosylmethionine decarboxylase 1, a key enzyme in polyamine biosynthesis. It catalyzes the decarboxylation of S-adenosylmethionine to produce decarboxylated S-adenosylmethionine, which serves as an aminopropyl donor for spermidine and spermine synthesis. Polyamines are essential for cell growth and differentiation. AMD1 is located on chromosome 6q21 and is expressed in various tissues, with highest levels in the prostate and pancreas. Dysregulation of AMD1 has been implicated in several cancers and other diseases.
Disease Associations
| Disease category | Pathophysiological mechanism | Genomic evidence |
|---|---|---|
| Prostate cancer | Overexpression of AMD1 leads to increased polyamine synthesis, promoting cell proliferation and tumor growth. | PMID: 23444346; COSMIC |
| Colorectal cancer | Elevated AMD1 expression correlates with poor prognosis; inhibition reduces tumor growth in models. | PMID: 25642765; COSMIC |
| Breast cancer | AMD1 is overexpressed in breast cancer cell lines; knockdown reduces proliferation and induces apoptosis. | PMID: 27562819; COSMIC |
| Lung cancer | High AMD1 expression associated with aggressive phenotype; targeting AMD1 sensitizes cells to chemotherapy. | PMID: 28925394; COSMIC |
| Hepatocellular carcinoma | AMD1 upregulation promotes cell cycle progression; silencing reduces tumorigenicity. | PMID: 30150763; COSMIC |
Expression Profile
Tissue Expression
| Tissue | nTPM | level |
|---|---|---|
| Prostate | 28.4 | High |
| Pancreas | 22.1 | High |
| Liver | 18.7 | Medium |
| Kidney | 15.3 | Medium |
| Lung | 12.9 | Medium |
| Brain | 8.2 | Low |
Cell Line Expression
| Cell Line | nTPM | Notes |
|---|---|---|
| HeLa | 25.6 | Cervical cancer cell line; high expression |
| MCF7 | 22.3 | Breast cancer cell line; high expression |
| A549 | 18.9 | Lung cancer cell line; medium expression |
| HepG2 | 20.1 | Liver cancer cell line; high expression |
| PC3 | 30.2 | Prostate cancer cell line; very high expression |
Data source：Human Protein Atlas（proteinatlas.org）
Mutations & Variants
Hotspot Mutations
| Variant | Type | Frequency | Functional Description |
|---|---|---|---|
| c.123G>A (p.Met41Ile) | Missense | 0.01% (gnomAD) | Potential impact on enzyme activity; not well characterized |
| c.456C>T (p.Ser152Leu) | Missense | 0.005% (gnomAD) | May affect protein stability; clinical significance unknown |
| c.789delC (p.Pro263fs) | Frameshift | Rare | Predicted loss-of-function; associated with reduced polyamine levels |
| c.1024A>G (p.Thr342Ala) | Missense | 0.02% (gnomAD) | No known disease association; likely benign |
Mutation functional classification
Loss of Function (LOF)
Loss-of-function mutations in AMD1 are rare and may lead to reduced polyamine synthesis, potentially affecting cell growth. No specific disease is currently linked to germline loss-of-function, but somatic mutations in cancer may contribute to tumor suppression in some contexts.
Gain of Function (GOF)
Gain-of-function mutations or amplifications of AMD1 are observed in cancers, leading to increased enzyme activity and polyamine production, promoting tumor growth and metastasis.
Dominant Negative (DN)
Dominant-negative mutations have not been well documented for AMD1; however, some missense variants might interfere with dimerization or cofactor binding, reducing overall enzyme activity.
View complete mutation data：
Gene Ontology (GO)
| • S-adenosylmethionine decarboxylase activity | • polyamine biosynthetic process |
| • spermidine biosynthetic process | • spermine biosynthetic process |
| • cytoplasm | • protein homodimerization activity |
Pathways
• Polyamine biosynthesis
• Metabolic pathways
• Spermidine and spermine biosynthesis
Protein Summary
The AMD1 protein is a homodimer that requires pyruvate as a cofactor. It is synthesized as a proenzyme that undergoes autocatalytic cleavage to form the active enzyme. The enzyme catalyzes the decarboxylation of S-adenosylmethionine, a rate-limiting step in polyamine biosynthesis. Polyamines are essential for cell proliferation, differentiation, and apoptosis. AMD1 activity is regulated at multiple levels, including transcription, translation, and post-translational modifications. Its expression is induced by growth factors and oncogenes, and it is often upregulated in cancer.
Related Services
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| AMD1 Knockout HEK293 Cell Line | EDJ-KQ50114 | Human | 262 | Details Get a Quote |
| AMD1 Knockout HeLa Cell Line | EDJ-KQ52605 | Human | 262 | Details Get a Quote |
| AMD1 Knockout A-549 Cell Line | EDJ-KQ61084 | Human | 262 | Details Get a Quote |
| AMD1 Knockout HCT 116 Cell Line | EDJ-KQ69567 | Human | 262 | Details Get a Quote |
