ACVR1 — Activin A receptor type 1
ACVR1 belongs to a gene co-expression module in 1 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.
ACVR1's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| Macrophages | Endolysosomal Trafficking Lysosomal & pahgocytosis | ATAD1, ATP6V1C1, CSNK2A1, CTNNB1, DDX6, EMILIN2, GNAI3, GTF2H1 +17 more | View in SCUBA |
About the gene
| Synonyms | ACVR1A, ACVRLK2, ALK2, SKR1 |
|---|---|
| Chromosome | 2: 157736251-157876330 |
| Predicted location | Intracellular, Membrane |
| Essential gene | No |
| Protein class | Cancer-related genes, Disease related genes, Enzymes, Human disease related genes, Potential drug targets, Predicted intracellular proteins, Predicted membrane proteins |
| Molecular function | Kinase, Receptor, Serine/threonine-protein kinase, Transferase |
Function
Bone morphogenetic protein (BMP) type I receptor that is involved in a wide variety of biological processes, including bone, heart, cartilage, nervous, and reproductive system development and regulation. As a type I receptor, forms heterotetrameric receptor complexes with the type II receptors AMHR2, ACVR2A or ACVR2B. Upon binding of ligands such as BMP7 or GDF2/BMP9 to the heteromeric complexes, type II receptors transphosphorylate ACVR1 intracellular domain. In turn, ACVR1 kinase domain is activated and subsequently phosphorylates SMAD1/5/8 proteins that transduce the signal. In addition to its role in mediating BMP pathway-specific signaling, suppresses TGFbeta/activin pathway signaling by interfering with the binding of activin to its type II receptor. Besides canonical SMAD signaling, can activate non-canonical pathways such as p38 mitogen-activated protein kinases/MAPKs (By similarity). May promote the expression of HAMP, potentially via its interaction with BMP6 (By similarity).
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.