HRG report

I. Expression across cell types

II. Expression across tissues

sc-RNAseq data

Insufficient scRNA-seq data for expression of HRG at tissue level.

III. Associated gene sets

GO_0001525Biological processangiogenesis
GO_0010468Biological processregulation of gene expression
GO_0008285Biological processnegative regulation of cell population proliferation
GO_0050832Biological processdefense response to fungus
GO_2001027Biological processnegative regulation of endothelial cell chemotaxis
GO_0010951Biological processnegative regulation of endopeptidase activity
GO_0010543Biological processregulation of platelet activation
GO_0002839Biological processpositive regulation of immune response to tumor cell
GO_0051918Biological processnegative regulation of fibrinolysis
GO_0007162Biological processnegative regulation of cell adhesion
GO_0006935Biological processchemotaxis
GO_0033629Biological processnegative regulation of cell adhesion mediated by integrin
GO_0051838Biological processcytolysis by host of symbiont cells
GO_0042730Biological processfibrinolysis
GO_0043537Biological processnegative regulation of blood vessel endothelial cell migration
GO_0030168Biological processplatelet activation
GO_0016525Biological processnegative regulation of angiogenesis
GO_0010593Biological processnegative regulation of lamellipodium assembly
GO_0030193Biological processregulation of blood coagulation
GO_0050730Biological processregulation of peptidyl-tyrosine phosphorylation
GO_0051894Biological processpositive regulation of focal adhesion assembly
GO_1900747Biological processnegative regulation of vascular endothelial growth factor signaling pathway
GO_0043254Biological processregulation of protein-containing complex assembly
GO_0061844Biological processantimicrobial humoral immune response mediated by antimicrobial peptide
GO_2000504Biological processpositive regulation of blood vessel remodeling
GO_0043065Biological processpositive regulation of apoptotic process
GO_0032956Biological processregulation of actin cytoskeleton organization
GO_0030308Biological processnegative regulation of cell growth
GO_0005576Cellular componentextracellular region
GO_0005886Cellular componentplasma membrane
GO_0070062Cellular componentextracellular exosome
GO_0062023Cellular componentcollagen-containing extracellular matrix
GO_0072562Cellular componentblood microparticle
GO_0009986Cellular componentcell surface
GO_0031093Cellular componentplatelet alpha granule lumen
GO_0004869Molecular functioncysteine-type endopeptidase inhibitor activity
GO_0008201Molecular functionheparin binding
GO_0019865Molecular functionimmunoglobulin binding
GO_0004867Molecular functionserine-type endopeptidase inhibitor activity
GO_0005102Molecular functionsignaling receptor binding
GO_0020037Molecular functionheme binding
GO_0008270Molecular functionzinc ion binding
GO_0046872Molecular functionmetal ion binding
GO_0043395Molecular functionheparan sulfate proteoglycan binding
GO_0005515Molecular functionprotein binding

IV. Literature review

[source]
Gene nameHRG
Protein nameHistidine-rich glycoprotein (Histidine-proline-rich glycoprotein) (HPRG)
Synonyms
DescriptionFUNCTION: Plasma glycoprotein that binds a number of ligands such as heme, heparin, heparan sulfate, thrombospondin, plasminogen, and divalent metal ions. Binds heparin and heparin/glycosaminoglycans in a zinc-dependent manner. Binds heparan sulfate on the surface of liver, lung, kidney and heart endothelial cells. Binds to N-sulfated polysaccharide chains on the surface of liver endothelial cells. Inhibits rosette formation. Acts as an adapter protein and is implicated in regulating many processes such as immune complex and pathogen clearance, cell chemotaxis, cell adhesion, angiogenesis, coagulation and fibrinolysis. Mediates clearance of necrotic cells through enhancing the phagocytosis of necrotic cells in a heparan sulfate-dependent pathway. This process can be regulated by the presence of certain HRG ligands such as heparin and zinc ions. Binds to IgG subclasses of immunoglobins containing kappa and lambda light chains with different affinities regulating their clearance and inhibiting the formation of insoluble immune complexes. Tethers plasminogen to the cell surface. Binds T-cells and alters the cell morphology. Modulates angiogenesis by blocking the CD6-mediated antiangiongenic effect of thrombospondins, THBS1 and THBS2. Acts as a regulator of the vascular endothelial growth factor (VEGF) signaling pathway; inhibits endothelial cell motility by reducing VEGF-induced complex formation between PXN/paxillin and ILK/integrin-linked protein kinase and by promoting inhibition of VEGF-induced tyrosine phosphorylation of focal adhesion kinases and alpha-actinins in endothelial cells. Also plays a role in the regulation of tumor angiogenesis and tumor immune surveillance. Normalizes tumor vessels and promotes antitumor immunity by polarizing tumor-associated macrophages, leading to decreased tumor growth and metastasis. .

AccessionsP04196
ENST00000232003.5