Search Results
Overview
| Uniprot ID | P01857 |
|---|---|
| Protein Name | Immunoglobulin heavy constant gamma 1 |
| Gene Name | IGHG1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 101 | VDKKVEPKSCDKTHT |
| 209 | YKCKVSNKALPAPIE |
| 217 | ALPAPIEKTISKAKG |
| 297 | YSKLTVDKSRWQQGN |
Function
Constant region of immunoglobulin (Ig) heavy chains. Igs are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound Igs serve as receptors, which upon binding to a specific antigen trigger the clonal expansion and differentiation of B lymphocytes into Ig-secreting plasma cells. Secreted Igs known as antibodies mediate the effector phase of humoral immunity by blocking the interaction of infectious antigens with cellular receptors (via the antigen-binding region) and eliciting effector mechanisms that lead to pathogen neutralization (via the constant region) (PubMed:17576170, PubMed:20176268, PubMed:22158414). The antigen-binding region is formed by the variable domain of one heavy chain paired with the variable domain of its associated light chain. Each Ig molecule has two antigen-binding sites with remarkable affinity for a particular antigen due to V-(D)-J rearrangement, somatic hypermutations and affinity maturation of the variable domains upon antigen exposure (PubMed:17576170, PubMed:20176268, PubMed:22158414). The constant region defines the Ig isotype that perform distinct sets of effector functions. B cells diversify and rearrange their Ig constant regions through class-switch recombination, a process by which the constant region is switched from one Ig isotype to another, namely from IgM and IgD to IgG, IgA and IgE (PubMed:17576170, PubMed:20176268, PubMed:22158414). The constant region of Ig gamma-1 (IgG1) isotype interacts (via the fragment crystallizable, Fc) with receptors on innate immune cells and the complement system to mediate humoral effector functions, including antibody-dependent cellular cytotoxicity or phagocytosis, complement-dependent cytotoxicity and inflammatory responses
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0072562 | blood microparticle |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005576 | extracellular region |
| Cellular Component | GO:0005615 | extracellular space |
| Cellular Component | GO:0042571 | immunoglobulin complex, circulating |
| Cellular Component | GO:0005886 | plasma membrane |
| Molecular Function | GO:0003823 | antigen binding |
| Molecular Function | GO:0034988 | Fc-gamma receptor I complex binding |
| Molecular Function | GO:0034987 | immunoglobulin receptor binding |
| Biological Process | GO:0002250 | adaptive immune response |
| Biological Process | GO:0019731 | antibacterial humoral response |
| Biological Process | GO:0001788 | antibody-dependent cellular cytotoxicity |
| Biological Process | GO:0050853 | B cell receptor signaling pathway |
| Biological Process | GO:0006958 | complement activation, classical pathway |
| Biological Process | GO:0097278 | complement-dependent cytotoxicity |
Reference
[1] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[2] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.