IGKC

Chr 2p11.2

immunoglobulin kappa constant

Aliases:: HCAK1

OMIM: 147200 ↗NCBI: 3514 ↗Ensembl ↗

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Predicted protein structure

AlphaFold predicted structure

IGKC · P01834

v62025-08-01

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

Mean pLDDT

97.0/ 100

Very high

107 residues

Confidence breakdown

Very high(≥ 90)96%
Confident(70–90)3%
Low(50–70)1%
Very low(< 50)0%

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)

cutaneous leishmaniasis
0.59
recurrent infections associated with rare immunoglobulin isotypes deficiency
0.57
Barrett esophagus
0.07
neoplasm
0.06
squamous cell carcinoma
0.06
sebaceous of Jadassohn nevus
0.06
breast carcinoma
0.05
breast cancer
0.05
esophageal adenocarcinoma
0.05
rheumatoid arthritis
0.04

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

Protein function (UniProt)

Immunoglobulin kappa constant

Constant region of immunoglobulin light 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)