CD22 — CD22 molecule
CD22 belongs to a gene co-expression module in 2 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.
CD22's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| CD19⁺ B cells | BCR signaling/maturation B cell maturation | ATP6V0A1, BCL11A, CAMK2D, CLEC2D, DDHD1, DGKD, IL4R, ITPR1 +9 more | View in SCUBA |
| Hematopoietic progenitor cells | Lymphoid-Primed Progenitor Lymphcyte development | ARHGAP27, COBLL1, LILRB2, LTB, PACSIN1, S100Z, SH3TC1, SLC2A5 +4 more |
About the gene
| Synonyms | SIGLEC-2, SIGLEC2 |
|---|---|
| Chromosome | 19: 35319261-35347361 |
| Predicted location | Intracellular, Membrane |
| Essential gene | No |
| Protein class | CD markers, FDA approved drug targets, Plasma proteins, Predicted intracellular proteins, Predicted membrane proteins |
| Biological process | Cell adhesion |
Function
Most highly expressed siglec (sialic acid-binding immunoglobulin-like lectin) on B-cells that plays a role in various aspects of B-cell biology including differentiation, antigen presentation, and trafficking to bone marrow. Binds to alpha 2,6-linked sialic acid residues of surface molecules such as CD22 itself, CD45 and IgM in a cis configuration. Can also bind to ligands on other cells as an adhesion molecule in a trans configuration. Acts as an inhibitory coreceptor on the surface of B-cells and inhibits B-cell receptor induced signaling, characterized by inhibition of the calcium mobilization and cellular activation. Mechanistically, the immunoreceptor tyrosine-based inhibitory motif domain is phosphorylated by the Src kinase LYN, which in turn leads to the recruitment of the protein tyrosine phosphatase 1/PTPN6, leading to the negative regulation of BCR signaling. If this negative signaling from is of sufficient strength, apoptosis of the B-cell can be induced.
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.