ACVR2A

Activin A receptor, type IIA
PDB rendering based on 1bte.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1bte​, 1lx5​, 2goo​
Identifiers
Symbols	ACVR2A ; ACTRII; ACVR2
External IDs	Template:OMIM5 Template:MGI HomoloGene: 20391
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Template:Protbox Activin A receptor, type IIA, also known as ACVR2A, is a human gene. ACVR2A is an activin type 2 receptor. This gene encodes activin A type II receptor. Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally related signaling proteins. Activins signal through a heteromeric complex of receptor serine kinases which include at least two type I (I and IB) and two type II (II and IIB) receptors. These receptors are all transmembrane proteins, composed of a ligand-binding extracellular domain with cysteine-rich region, a transmembrane domain, and a cytoplasmic domain with predicted serine/threonine specificity. Type I receptors are essential for signaling; and type II receptors are required for binding ligands and for expression of type I receptors. Type I and II receptors form a stable complex after ligand binding, resulting in phosphorylation of type I receptors by type II receptors. Type II receptors are considered to be constitutively active kinases.

Further reading

• Welt CK (2002). "The physiology and pathophysiology of inhibin, activin and follistatin in female reproduction". Curr. Opin. Obstet. Gynecol. 14 (3): 317–23. PMID 12032389.
• Matzuk MM, Bradley A (1992). "Cloning of the human activin receptor cDNA reveals high evolutionary conservation". Biochim. Biophys. Acta. 1130 (1): 105–8. PMID 1311955.
• Donaldson CJ, Mathews LS, Vale WW (1992). "Molecular cloning and binding properties of the human type II activin receptor". Biochem. Biophys. Res. Commun. 184 (1): 310–6. PMID 1314589.CS1 maint: Multiple names: authors list (link)
• Mathews LS, Vale WW (1991). "Expression cloning of an activin receptor, a predicted transmembrane serine kinase". Cell. 65 (6): 973–82. PMID 1646080.
• Xu J, McKeehan K, Matsuzaki K, McKeehan WL (1995). "Inhibin antagonizes inhibition of liver cell growth by activin by a dominant-negative mechanism". J. Biol. Chem. 270 (11): 6308–13. PMID 7890768.CS1 maint: Multiple names: authors list (link)
• Attisano L, Cárcamo J, Ventura F; et al. (1993). "Identification of human activin and TGF beta type I receptors that form heteromeric kinase complexes with type II receptors". Cell. 75 (4): 671–80. PMID 8242742.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Peng C, Huang TH, Jeung EB; et al. (1994). "Expression of the type II activin receptor gene in the human placenta". Endocrinology. 133 (6): 3046–9. PMID 8243335.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• De Winter JP, De Vries CJ, Van Achterberg TA; et al. (1996). "Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. receptors". Exp. Cell Res. 224 (2): 323–34. PMID 8612709.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Attisano L, Wrana JL, Montalvo E, Massagué J (1996). "Activation of signalling by the activin receptor complex". Mol. Cell. Biol. 16 (3): 1066–73. PMID 8622651.CS1 maint: Multiple names: authors list (link)
• Liu QY, Niranjan B, Gomes P; et al. (1996). "Inhibitory effects of activin on the growth and morpholgenesis of primary and transformed mammary epithelial cells". Cancer Res. 56 (5): 1155–63. PMID 8640777.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Nishitoh H, Ichijo H, Kimura M; et al. (1996). "Identification of type I and type II serine/threonine kinase receptors for growth/differentiation factor-5". J. Biol. Chem. 271 (35): 21345–52. PMID 8702914.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Lebrun JJ, Vale WW (1997). "Activin and inhibin have antagonistic effects on ligand-dependent heteromerization of the type I and type II activin receptors and human erythroid differentiation". Mol. Cell. Biol. 17 (3): 1682–91. PMID 9032295.
• Macías-Silva M, Hoodless PA, Tang SJ; et al. (1998). "Specific activation of Smad1 signaling pathways by the BMP7 type I receptor, ALK2". J. Biol. Chem. 273 (40): 25628–36. PMID 9748228.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Barbara NP, Wrana JL, Letarte M (1999). "Endoglin is an accessory protein that interacts with the signaling receptor complex of multiple members of the transforming growth factor-beta superfamily". J. Biol. Chem. 274 (2): 584–94. PMID 9872992.CS1 maint: Multiple names: authors list (link)
• Lux A, Attisano L, Marchuk DA (1999). "Assignment of transforming growth factor beta1 and beta3 and a third new ligand to the type I receptor ALK-1". J. Biol. Chem. 274 (15): 9984–92. PMID 10187774.CS1 maint: Multiple names: authors list (link)
• D'Abronzo FH, Swearingen B, Klibanski A, Alexander JM (1999). "Mutational analysis of activin/transforming growth factor-beta type I and type II receptor kinases in human pituitary tumors". J. Clin. Endocrinol. Metab. 84 (5): 1716–21. PMID 10323406.CS1 maint: Multiple names: authors list (link)
• Ebisawa T, Tada K, Kitajima I; et al. (2000). "Characterization of bone morphogenetic protein-6 signaling pathways in osteoblast differentiation". J. Cell. Sci. 112 ( Pt 20): 3519–27. PMID 10504300.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• van Schaik RH, Wierikx CD, Timmerman MA; et al. (2000). "Variations in activin receptor, inhibin/activin subunit and follistatin mRNAs in human prostate tumour tissues". Br. J. Cancer. 82 (1): 112–7. doi:10.1054/bjoc.1999.0886. PMID 10638976.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Shoji H, Tsuchida K, Kishi H; et al. (2000). "Identification and characterization of a PDZ protein that interacts with activin type II receptors". J. Biol. Chem. 275 (8): 5485–92. PMID 10681527.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Bondestam J, Horelli-Kuitunen N, Hildén K; et al. (2000). "Assignment of ACVR2 and ACVR2B the human activin receptor type II and IIB genes to chromosome bands 2q22.2-->q23.3 and 3p22 and the human follistatin gene (FST) to chromosome 5q11.2 by FISH". Cytogenet. Cell Genet. 87 (3–4): 219–20. PMID 10702675.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)