SCUBA

SIGLEC1 — Sialic acid binding Ig like lectin 1

SIGLEC1 belongs to a gene co-expression module in 1 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.

SIGLEC1's module in each cell type

Cell typeModuleShares the module with
MonocytesMonocyte Lipid Handling
Lysosomal & pahgocytosis
AKR1A1, CD81, FUOM, ISOC2, LAIR1, NPC2, RGL1, SPATS2L +1 moreView in SCUBA

About the gene

SynonymsCD169, dJ1009E24.1, FLJ00051, FLJ00055, FLJ00073, FLJ32150, sialoadhesin, SIGLEC-1, SN
Chromosome20: 3686970-3712600
Predicted locationIntracellular, Membrane
Essential geneNo
Protein classCD markers, Predicted intracellular proteins, Predicted membrane proteins
Biological processCell adhesion, Endocytosis

Function

Macrophage-restricted adhesion molecule that mediates sialic- acid dependent binding to lymphocytes, including granulocytes, monocytes, natural killer cells, B-cells and CD8 T-cells. Plays a crucial role in limiting bacterial dissemination by engaging sialylated bacteria to promote effective phagocytosis and antigen presentation for the adaptive immune response. Mediates the uptake of various enveloped viruses via sialic acid recognition and subsequently induces the formation of intracellular compartments filled with virions (VCCs). In turn, enhances macrophage-to-T-cell transmission of several viruses including HIV-1 or SARS-CoV-2. Acts as an endocytic receptor mediating clathrin dependent endocytosis. Preferentially binds to alpha-2,3-linked sialic acid. Binds to SPN/CD43 on T-cells (By similarity). May play a role in hemopoiesis. Plays a role in the inhibition of antiviral innate immune by promoting TBK1 degradation via TYROBP and TRIM27-mediated ubiquitination. (Microbial infection) Facilitates viral cytoplasmic entry into activated dendritic cells via recognition of sialylated gangliosides pesent on viral membrane

Human Protein Atlas · Open Targets · UniProt

Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.