Immunoglobulins (Ig) are the antigen recognition molecules of B cells. An Ig molecule is made up of 2 identical heavy chains and 2 identical light chains (see MIM 147200) joined by disulfide bonds so that each heavy chain is linked to a light chain and the 2 heavy chains are linked together. Each Ig heavy chain has an N-terminal variable (V) region containing the antigen-binding site and a C-terminal constant (C) region, encoded by an individual C region gene, that determines the isotype of the antibody and provides effector or signaling functions. The heavy chain V region is encoded by 1 each of 3 types of genes: V genes (see MIM 147070), joining (J) genes (see MIM 147010), and diversity (D) genes (see MIM 146910). The C region genes are clustered downstream of the V region genes within the heavy chain locus on chromosome 14. IGHM (Immunoglobulin Heavy Constant Mu) is a Protein Coding gene. Diseases associated with IGHM include Agammaglobulinemia 1 and Agammaglobulinemia, Non-Bruton Type. Among its related pathways are Development Angiotensin activation of ERK and Immune response Lectin induced complement pathway. GO annotations related to this gene include single-stranded DNA binding and phosphatidylcholine binding. An important paralog of this gene is IGHG1.