Details of the Target
General Information of Target
Target ID | LDTP16373 | |||||
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Target Name | Probable non-functional immunoglobulinn kappa variable 1-37 (IGKV1-37) | |||||
Gene Name | IGKV1-37 | |||||
Synonyms |
Probable non-functional immunoglobulinn kappa variable 1-37 |
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3D Structure | ||||||
Sequence |
MRLPAQLLGLLMLWVPGSSGDVVMTQSPLSLPVTLGQPASISCRSSQSLVYSDGNTYLNW
FQQRPGQSPRRLIYKVSNWDSGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCMQGTHWP |
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Target Bioclass |
Immunoglobulin
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Subcellular location |
Secreted
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Function |
Probable non-functional open reading frame (ORF) of V region of the variable domain of immunoglobulin light chains. Non-functional ORF generally cannot participate in the synthesis of a productive immunoglobulin chain due to altered V-(D)-J or switch recombination and/or splicing site (at mRNA level) and/or conserved amino acid change (protein level). 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. 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.
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Uniprot ID | ||||||
Ensemble ID | ||||||
HGNC ID |
Probe(s) Labeling This Target
ABPP Probe
Probe name | Structure | Binding Site(Ratio) | Interaction ID | Ref | |
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NAIA_4 Probe Info |
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N.A. | LDD2226 | [1] |