Phospho-CD79A (Tyr182)

CD79A (CD79a Molecule) is a Protein Coding gene. Diseases associated with CD79A include Agammaglobulinemia 3, Autosomal Recessive and Agammaglobulinemia, Non-Bruton Type. Among its related pathways are Hematopoietic Stem Cell Differentiation Pathways and Lineage-specific Markers and Innate Immune System. Gene Ontology (GO) annotations related to this gene include transmembrane signaling receptor activity.

CD79a Molecule

Required in cooperation with CD79B for initiation of the signal transduction cascade activated by binding of antigen to the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Also required for BCR surface expression and for efficient differentiation of pro- and pre-B-cells. Stimulates SYK autophosphorylation and activation. Binds to BLNK, bringing BLNK into proximity with SYK and allowing SYK to phosphorylate BLNK. Also interacts with and increases activity of some Src-family tyrosine kinases. Represses BCR signaling during development of immature B-cells.

Adaptive immune response Source: UniProtKB-KW
B cell activation Source: UniProtKB
B cell differentiation Source: UniProtKB
B cell proliferation Source: UniProtKB
B cell receptor signaling pathway Source: UniProtKB

Cell membrane. Following antigen binding, the BCR has been shown to translocate from detergent-soluble regions of the cell membrane to lipid rafts although signal transduction through the complex can also occur outside lipid rafts.

Agammaglobulinemia 3, autosomal recessive (AGM3): The disease is caused by variants affecting the gene represented in this entry. Two different mutations, one at the splice donor site of intron 2 and the other at the splice acceptor site for exon 3, have been identified. Both mutations give rise to a truncated protein. A primary immunodeficiency characterized by profoundly low or absent serum antibodies and low or absent circulating B-cells due to an early block of B-cell development. Affected individuals develop severe infections in the first years of life.

Extracellular: 33-143
Helical: 144-165
Cytoplasmic: 166-226

Phosphorylated on tyrosine, serine and threonine residues upon B-cell activation. Phosphorylation of tyrosine residues by Src-family kinases is an early and essential feature of the BCR signaling cascade. The phosphorylated tyrosines serve as docking sites for SH2-domain containing kinases, leading to their activation which in turn leads to phosphorylation of downstream targets. Phosphorylated by LYN. Phosphorylation of serine and threonine residues may prevent subsequent tyrosine phosphorylation.
Arginine methylation in the ITAM domain may interfere with the binding of SYK. It promotes signals leading to B-cell differentiation (By similarity).