ULBP2

ULBP2 is ligand for the NKG2D receptor, together with at least ULBP1 and ULBP3. ULBPs activate multiple signaling pathways in primary NK cells, resulting in the production of cytokines and chemokines. ULBP2 binds of ULBPs ligands to NKG2D induces calcium mobilization and activation of the JAK2, STAT5, ERK and PI3K kinase/Akt signal transduction pathway. In CMV infected cells, ULBP2 interacts with soluble CMV glycoprotein UL16. The interaction with UL16 blocked the interaction with the NKG2D receptor, providing a mechanism by which CMV infected cells might escape the immune system. UL16 also causes ULBP2 to be retained in the ER and cis-Golgi apparatus so that it does not reach the cell surface.

ULBP2 Related Areas

Immunology>>Innate Immunity>>Natural Killer Cell (NK Cell)>>ULBP2

ULBP2 Alternative Names

ULBP2, UNQ463/PRO791, N2DL2, RAET1H [Homo sapiens]

Summaries for ULBP2

Wikipedia summary for ULBP2:

NKG2D ligand 2 is a protein that in humans is encoded by the ULBP2 gene. It is a stress induced ligand for the NK cell activating receptor NKG2D.

Human ULBP2 Protein General Information

 

• Protein names: UL16-binding protein 2
  Short name=ULBP2
• Sequence length: 246 AA.
• Domain: Signal
• Sequence similarities: Belongs to the MHC class I family.
• Miscellaneous: The ULBPs are unusual members of the extended MHC class I superfamily, because they do not contain the alpha 3 domain and they lack a transmembrane domain. They are unlikely to present peptides.
• Subunit structure: Interacts with the CMV glycoprotein UL16. Does not bind to beta2-microglobulin.
• Subcellular location: Cell membrane; Lipid-anchor › GPI-anchor. Secreted .
• Tissue specificity: Expressed in various types of cancer cell lines and in the fetus, but not in normal tissues.

General information above from UniProt

Function for ULBP2 Protein

UniProtKB:

ULBP2 is ligand for the NKG2D receptor, together with at least ULBP1 and ULBP3. ULBPs activate multiple signaling pathways in primary NK cells, resulting in the production of cytokines and chemokines. ULBP2 binds of ULBPs ligands to NKG2D induces calcium mobilization and activation of the JAK2, STAT5, ERK and PI3K kinase/Akt signal transduction pathway. In CMV infected cells, ULBP2 interacts with soluble CMV glycoprotein UL16. The interaction with UL16 blocked the interaction with the NKG2D receptor, providing a mechanism by which CMV infected cells might escape the immune system. UL16 also causes ULBP2 to be retained in the ER and cis-Golgi apparatus so that it does not reach the cell surface.