Overview
| Uniprot ID | P0DOX7 |
|---|
| Protein Name | Immunoglobulin kappa light chain |
|---|
| Gene Name | - |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 145 |
NFYPREAKVQWKVDN |
| 149 |
REAKVQWKVDNALQS |
| 169 |
SVTEQDSKDSTYSLS |
| 183 |
SSTLTLSKADYEKHK |
| 190 |
KADYEKHKVYACEVT |
| 207 |
GLSSPVTKSFNRGEC |
Function
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)
Protein Sequence
10
DIQMTQSPST
20
LSASVGDRVT
30
ITCRASQSIN
40
TWLAWYQQKP
50
GKAPKLLMYK
60
ASSLESGVPS
70
RFIGSGSGTE
80
FTLTISSLQP
90
DDFATYYCQQ
100
YNSDSKMFGQ
110
GTKVEVKGTV
120
AAPSVFIFPP
130
SDEQLKSGTA
140
SVVCLLNNFY
150
PREAKVQWKV
160
DNALQSGNSQ
170
ESVTEQDSKD
180
STYSLSSTLT
190
LSKADYEKHK
200
VYACEVTHQG
210
LSSPVTKSFN
RGEC
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005576 |
extracellular region |
| Cellular Component |
GO:0019814 |
immunoglobulin complex |
| Cellular Component |
GO:0005886 |
plasma membrane |
| Biological Process |
GO:0002250 |
adaptive immune response |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.