IGKC

Immunoglobulin kappa constant
Identifiers
Symbols	IGKC ; HCAK1; IGKCD; Km
External IDs	OMIM: 147200 GeneCards: IGKC Gene
Gene ontology Molecular function • antigen binding Cellular component • extracellular region • extracellular space • plasma membrane • extracellular exosome • blood microparticle Biological process • retina homeostasis • receptor-mediated endocytosis • immune response • complement activation • complement activation, classical pathway • Fc-epsilon receptor signaling pathway • Fc-gamma receptor signaling pathway involved in phagocytosis • innate immune response • regulation of immune response Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	3514	n/a
Ensembl	n/a	n/a
UniProt	P01601	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search		n/a

Immunoglobulin kappa constant, also known as IGKC, is a human gene that encodes the constant domain of kappa-type light chains for antibodies.^[1] It is found on chromosome 2, in humans, within the Immunoglobulin kappa locus, IGK@.

References

1. "Entrez Gene: IGKC immunoglobulin kappa constant".

Further reading

• Brady RL, Edwards DJ, Hubbard RE, et al. (1992). "Crystal structure of a chimeric Fab' fragment of an antibody binding tumour cells". J. Mol. Biol. 227 (1): 253–64. doi:10.1016/0022-2836(92)90695-G. PMID 1522589.
• Titani K, Shinoda T, Putnam FW (1969). "The amino acid sequence of a kappa type Bence-Jones protein. 3. The complete sequence and the location of the disulfide bridges". J. Biol. Chem. 244 (13): 3550–60. PMID 4893682.
• Gall WE, Edelman GM (1971). "The covalent structure of a human gamma G-immunoglobulin. X. Intrachain disulfide bonds". Biochemistry 9 (16): 3188–96. doi:10.1021/bi00818a011. PMID 4923144.
• Suter L, Barnikol HU, Watanabe S, Hilschmann N (1972). "[Rule of antibody structure. The primary structure of a monoclonal immunoglobulin L-chain of kappa-type, subgroup 3 (Bence-Jones protein Ti). IV. The complete amino acid sequence and its significance for the mechanism of antibody production]". Hoppe-Seyler's Z. Physiol. Chem. 353 (2): 189–208. PMID 5027703.
• Kohler H, Shimizu A, Paul C, Putnam FW (1970). "Macroglobulin structure: variable sequence of light and heavy chains". Science 169 (3940): 56–9. doi:10.1126/science.169.3940.56. PMID 5447531.
• Gottlieb PD, Cunningham BA, Rutishauser U, Edelman GM (1971). "The covalent structure of a human gamma G-immunoglobulin. VI. Amino acid sequence of the light chain". Biochemistry 9 (16): 3155–61. doi:10.1021/bi00818a007. PMID 5489770.
• Hilschmann N (1968). "[The complete amino acid sequence of Bence Jones protein Cum (kappa-type)]". Hoppe-Seyler's Z. Physiol. Chem. 348 (12): 1718–22. PMID 5586923.
• Klobeck HG, Combriato G, Zachau HG (1984). "Immunoglobulin genes of the kappa light chain type from two human lymphoid cell lines are closely related". Nucleic Acids Res. 12 (18): 6995–7006. doi:10.1093/nar/12.18.6995. PMC 320138. PMID 6091049.
• Hieter PA, Maizel JV, Leder P (1982). "Evolution of human immunoglobulin kappa J region genes". J. Biol. Chem. 257 (3): 1516–22. PMID 6276389.
• Emorine L, Kuehl M, Weir L, et al. (1983). "A conserved sequence in the immunoglobulin J kappa-C kappa intron: possible enhancer element". Nature 304 (5925): 447–9. doi:10.1038/304447a0. PMID 6308460.
• Bentley DL, Rabbitts TH (1983). "Evolution of immunoglobulin V genes: evidence indicating that recently duplicated human V kappa sequences have diverged by gene conversion". Cell 32 (1): 181–9. doi:10.1016/0092-8674(83)90508-1. PMID 6402305.
• Hieter PA, Max EE, Seidman JG, et al. (1981). "Cloned human and mouse kappa immunoglobulin constant and J region genes conserve homology in functional segments". Cell 22 (1 Pt 1): 197–207. doi:10.1016/0092-8674(80)90168-3. PMID 6775818.
• Bentley DL, Rabbits TH (1981). "Human immunoglobulin variable region genes--DNA sequences of two V kappa genes and a pseudogene". Nature 288 (5792): 730–3. doi:10.1038/288730a0. PMID 6779204.
• Huber C, Schäble KF, Huber E, et al. (1993). "The V kappa genes of the L regions and the repertoire of V kappa gene sequences in the human germ line". Eur. J. Immunol. 23 (11): 2868–75. doi:10.1002/eji.1830231121. PMID 8223863.
• Olsen KE, Sletten K, Westermark P (1998). "Extended analysis of AL-amyloid protein from abdominal wall subcutaneous fat biopsy: kappa IV immunoglobulin light chain". Biochem. Biophys. Res. Commun. 245 (3): 713–6. doi:10.1006/bbrc.1998.8515. PMID 9588180.
• Wally J, Kica G, Zhang Y, et al. (1999). "Identification of a novel substitution in the constant region of a gene coding for an amyloidogenic kappa1 light chain". Biochim. Biophys. Acta 1454 (1): 49–56. doi:10.1016/s0925-4439(99)00019-8. PMID 10354514.
• Hotta K, Lange H, Tantillo DJ, et al. (2000). "Catalysis of decarboxylation by a preorganized heterogeneous microenvironment: crystal structures of abzyme 21D8". J. Mol. Biol. 302 (5): 1213–25. doi:10.1006/jmbi.2000.4503. PMID 11183784.
• Karpusas M, Lucci J, Ferrant J, et al. (2001). "Structure of CD40 ligand in complex with the Fab fragment of a neutralizing humanized antibody". Structure 9 (4): 321–9. doi:10.1016/S0969-2126(01)00590-1. PMID 11525169.
• Davis DP, Gallo G, Vogen SM, et al. (2001). "Both the environment and somatic mutations govern the aggregation pathway of pathogenic immunoglobulin light chain". J. Mol. Biol. 313 (5): 1021–34. doi:10.1006/jmbi.2001.5092. PMID 11700059.
• Pandey JP, Frederick M, (2002). "TNF-alpha, IL1-beta, and immunoglobulin (GM and KM) gene polymorphisms in sarcoidosis". Hum. Immunol. 63 (6): 485–91. doi:10.1016/S0198-8859(02)00399-3. PMID 12039524.