| Name | immunoglobulin kappa joining cluster |
| Description | Immunoglobulins (Ig) are the antigen recognition molecules of B cells. An Ig molecule is made up of 2 identical heavy chains (see MIM 147100) and 2 identical light chains, either kappa or lambda (see MIM 147220), joined by disulfide bonds so that each heavy chain is linked to a light chain and the 2 heavy chains are linked together. The kappa and lambda light chains have no apparent functional differences. Each Ig kappa light chain has an N-terminal variable (V) region containing the antigen-binding site and a C-terminal constant (C) region, encoded by a C region gene (IGKC; MIM 147200), that provides signaling functions. The kappa light chain V region is encoded by 2 types of genes: V genes (see MIM 146980) and joining (J) genes. Random selection of just 1 gene of each type to assemble a V region accounts for the great diversity of V regions among Ig molecules. The kappa light chain locus on chromosome 2 contains approximately 40 functional V genes, followed by approximately 5 functional J genes. Due to polymorphism, the numbers of functional V and J genes differ among individuals (Janeway et al., 2005).[supplied by OMIM, Apr 2008] |
| Synonyms | IGKJ |
| NCBI Gene ID | 7842 |
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IGKJ@ has 0 functional associations with biological entities spanning 0 categories () extracted from 0 datasets.
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