UniProtKB/Swiss-Prot PTM Description

Constant region of immunoglobulin heavy chains. 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:22158414, PubMed:20176268). 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)

Compositional data available: 74 compositions reported:

Asn180 [Hex]5 [HexNAc]2 [Hex]3 [HexNAc]3 [Hex]3 [HexNAc]4 [dHex]2 [Hex]3 [HexNAc]4 [NeuAc]1 [Hex]3 [HexNAc]4 [NeuAc]1 [dHex]2 [Hex]3 [HexNAc]5 [Hex]5 [HexNAc]3 [NeuAc]1 [dHex]1 [Hex]5 [HexNAc]4 [Hex]5 [HexNAc]4 [dHex]1 [Hex]5 [HexNAc]4 [dHex]2 [Hex]5 [HexNAc]4 [NeuAc]1 [Hex]5 [HexNAc]4 [NeuAc]1 [dHex]1 [Hex]5 [HexNAc]4 [NeuAc]2 [Hex]5 [HexNAc]5 [Hex]5 [HexNAc]5 [dHex]1 [Hex]5 [HexNAc]5 [NeuAc]1 [Hex]6 [HexNAc]4 [Hex]6 [HexNAc]4 [dHex]1 [Hex]6 [HexNAc]4 [NeuAc]2 [Hex]3 [HexNAc]6 [Hex]4 [HexNAc]3 [NeuAc]1 [Hex]4 [HexNAc]3 [Hex]4 [HexNAc]3 [dHex]1 [Hex]4 [HexNAc]3 [NeuAc]1 [dHex]1 [Hex]3 [HexNAc]3 [dHex]1 [Hex]3 [HexNAc]4 [Hex]3 [HexNAc]4 [dHex]1 [Hex]4 [HexNAc]4 [dHex]1 [Hex]4 [HexNAc]4 [dHex]2 [Hex]4 [HexNAc]4 [NeuAc]1 [Hex]4 [HexNAc]4 [NeuAc]1 [dHex]1 [Hex]4 [HexNAc]4 [NeuAc]2 [Hex]4 [HexNAc]5 [Hex]4 [HexNAc]5 [dHex]1 [Hex]4 [HexNAc]6 [Hex]4 [HexNAc]7 [NeuAc]1 [Hex]3 [HexNAc]5 [dHex]1 [Hex]4 [HexNAc]4

180 [Hex]5 [HexNAc]4 [dHex]1 [NeuAc]1

Asn176 [Hex]6 [HexNAc]3 [NeuAc]1 [dHex]1 [Hex]6 [HexNAc]4 [Hex]6 [HexNAc]4 [NeuAc]1 [Hex]6 [HexNAc]5 [Hex]3 [HexNAc]2 [dHex]1 [Hex]3 [HexNAc]3 [Hex]3 [HexNAc]3 [dHex]1 [Hex]3 [HexNAc]4 [Hex]3 [HexNAc]5 [dHex]1 [Hex]3 [HexNAc]6 [Hex]4 [HexNAc]2 [dHex]1 [Hex]4 [HexNAc]3 [Hex]4 [HexNAc]3 [dHex]1 [Hex]4 [HexNAc]4 [Hex]4 [HexNAc]4 [NeuAc]1 [Hex]4 [HexNAc]4 [NeuAc]1 [dHex]1 [Hex]4 [HexNAc]4 [NeuAc]2 [Hex]4 [HexNAc]5 [Hex]4 [HexNAc]5 [dHex]1 [Hex]5 [HexNAc]5 [NeuAc]1 [dHex]1 [Hex]4 [HexNAc]6 [Hex]5 [HexNAc]2 [Hex]5 [HexNAc]3 [NeuAc]1 [dHex]1 [Hex]5 [HexNAc]4 [Hex]5 [HexNAc]4 [dHex]1 [Hex]5 [HexNAc]4 [dHex]2 [Hex]5 [HexNAc]4 [NeuAc]1 [Hex]5 [HexNAc]4 [NeuAc]1 [dHex]1 [Hex]5 [HexNAc]4 [NeuAc]2 [Hex]5 [HexNAc]5 [Hex]6 [HexNAc]5 [NeuAc]2 [Hex]5 [HexNAc]5 [NeuAc]1 [Hex]3 [HexNAc]4 [dHex]1 [Hex]3 [HexNAc]5 [Hex]4 [HexNAc]3 [NeuAc]1 [dHex]1

Glycan Structures

Notes

Accompanying information

Structure Format

CFG/Essentials Text Oxford

Sequence

ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK

References 2

  1. Comparison of sialylated N-glycopeptide levels in serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls

    Kontro H, Joenväärä S, Haglund C, Renkonen R

    PubMed: 24841998 Year: 2014

  2. Efficient and accurate glycopeptide identification pipeline for high-throughput site-specific N-glycosylation analysis

    Liu M, Zhang Y, Chen Y, Yan G, Shen C, Cao J, Zhou X, Liu X, Zhang L, Shen H, Lu H, He F, Yang P

    PubMed: 24766575 Year: 2014