IGHM

Chr 14q32.33

immunoglobulin heavy constant mu

OMIM: 147020 ↗NCBI: 3507 ↗Ensembl ↗

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Predicted protein structure

AlphaFold predicted structure

IGHM · P01871

v62025-08-01

Predicted Aligned Error matrix for IGHM — diagonal shows residue index, colour shows pairwise prediction confidence (lower is better) — Predicted Aligned Error

Mean pLDDT

85.4/ 100

Confident

474 residues

Confidence breakdown

Very high(≥ 90)53%
Confident(70–90)35%
Low(50–70)8%
Very low(< 50)4%

Open interactive 3D viewer

AlphaFold (Jumper et al., 2021) · CC BY 4.0

Clinical relevance (Genomics England PanelApp)

Diagnostic Grade (Green)

COVID-19 research
BIALLELIC, autosomal or pseudoautosomal
Primary immunodeficiency or monogenic inflammatory bowel disease
BIALLELIC, autosomal or pseudoautosomal

Disease associations (Open Targets)

isolated agammaglobulinemia
0.55
agammaglobulinemia
0.46
autosomal agammaglobulinemia
0.37
BENTA disease
0.09
activated PI3K-delta syndrome
0.07
common variable immunodeficiency
0.06
Autosomal recessive systemic lupus erythematosus
0.06
autosomal systemic lupus erythematosus type 16
0.06
Barrett esophagus
0.06
C1Q deficiency 1
0.06

Score is the Open Targets composite evidence score (0-1). Higher = stronger gene-disease association.

Protein function (UniProt)

Immunoglobulin heavy constant mu

Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268)