ADAM28: A Disintegrin and Metalloproteinase Domain 28
Gene encoding a metalloproteinase involved in cell adhesion, migration, and cancer progression
Gene Information Card
| Symbol | ADAM28 |
|---|---|
| Full Name | ADAM metallopeptidase domain 28 |
| Gene Type | protein-coding |
| Chromosomal Location | 8p21.2 |
| NCBI Gene ID | 10863 ncbi.nlm.nih.gov/gene/10863 |
| Ensembl ID | ENSG00000142945 |
| UniProt ID | Q9UKQ2 |
| OMIM ID | 604780 |
| HGNC ID | 208 |
| Aliases | ADAM 28, MDC-L, eMDC II, ADAM23 |
Description
ADAM28 (ADAM metallopeptidase domain 28) encodes a member of the ADAM (a disintegrin and metalloproteinase) family. The protein contains a metalloproteinase domain, a disintegrin domain, a cysteine-rich region, and an EGF-like domain. It functions as a membrane-anchored protease involved in cell-cell and cell-matrix interactions, shedding of cell surface proteins, and modulation of signaling pathways. ADAM28 is implicated in cancer progression, particularly in lung, breast, and prostate cancers, where it promotes tumor cell migration, invasion, and metastasis.
Disease Associations
| Disease category | Pathophysiological mechanism | Genomic evidence |
|---|---|---|
| Lung cancer | Overexpression of ADAM28 enhances tumor cell migration and invasion via cleavage of extracellular matrix components and activation of growth factor signaling. | PMID: 19029980; COSMIC |
| Breast cancer | ADAM28 is upregulated in breast cancer tissues and correlates with poor prognosis; promotes metastasis through integrin-mediated adhesion. | PMID: 21573172; COSMIC |
| Prostate cancer | ADAM28 expression is associated with aggressive prostate cancer; facilitates invasion via shedding of CD44 and other adhesion molecules. | PMID: 23034449; COSMIC |
| Osteoarthritis | ADAM28 may contribute to cartilage degradation by cleaving aggrecan and other matrix components. | PMID: 15657075 |
Expression Profile
Tissue Expression
| Tissue | nTPM | level |
|---|---|---|
| Lung | 12.5 | Medium |
| Breast | 8.3 | Low |
| Prostate | 15.2 | Medium |
| Testis | 20.1 | High |
| Kidney | 6.7 | Low |
| Liver | 4.2 | Low |
Cell Line Expression
| Cell Line | nTPM | Notes |
|---|---|---|
| A549 (lung cancer) | 18.9 | High expression |
| MCF7 (breast cancer) | 9.5 | Moderate expression |
| PC3 (prostate cancer) | 22.3 | High expression |
| HEK293 (embryonic kidney) | 3.1 | Low expression |
Data source：Human Protein Atlas（proteinatlas.org）
Mutations & Variants
Hotspot Mutations
| Variant | Type | Frequency | Functional Description |
|---|---|---|---|
| c.1123G>A (p.Gly375Arg) | Missense | <0.1% | Unknown functional impact; reported in COSMIC |
| c.1456C>T (p.Arg486Trp) | Missense | <0.1% | Reported in lung cancer samples; potential loss of catalytic activity |
| c.1789_1791del (p.Phe597del) | In-frame deletion | <0.1% | Reported in breast cancer; may affect protein stability |
Mutation functional classification
Loss of Function (LOF)
Missense mutations in the metalloproteinase domain (e.g., p.Gly375Arg) may impair catalytic activity.
Gain of Function (GOF)
Not well characterized; overexpression in tumors suggests potential gain-of-function through increased proteolysis.
Dominant Negative (DN)
No evidence for dominant-negative mutations in ADAM28.
View complete mutation data：
Gene Ontology (GO)
| • metalloendopeptidase activity (GO:0004222) | • integrin binding (GO:0005178) |
| • extracellular matrix disassembly (GO:0022617) | • cell adhesion (GO:0007155) |
| • proteolysis (GO:0006508) | • membrane (GO:0016020) |
Pathways
• ADAM-mediated ectodomain shedding (Reactome: R-HSA-3928662)
• Integrin cell surface interactions (Reactome: R-HSA-216083)
• Extracellular matrix organization (Reactome: R-HSA-1474244)
Protein Summary
ADAM28 is a transmembrane metalloproteinase that cleaves extracellular matrix components and cell surface proteins, regulating cell adhesion, migration, and signaling. It is overexpressed in several cancers and associated with poor prognosis. The protein consists of a prodomain, a catalytic metalloproteinase domain, a disintegrin domain, a cysteine-rich region, and an EGF-like domain. Its activity is regulated by furin cleavage and inhibition by TIMPs (tissue inhibitors of metalloproteinases).
Related Services
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| ADAM28 Knockout HEK293 Cell Line | EDJ-KQ3666 | Human | 10863 | Details Get a Quote |
| ADAM28 Knockout HeLa Cell Line | EDJ-KQ55503 | Human | 10863 | Details Get a Quote |
| ADAM28 Knockout A-549 Cell Line | EDJ-KQ63992 | Human | 10863 | Details Get a Quote |
| ADAM28 Knockout HCT 116 Cell Line | EDJ-KQ72443 | Human | 10863 | Details Get a Quote |
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