HRG
entrez
3273
canonical
uniprot
P04196
canonical
ensembl
ENSG00000113905
resolver
ensp
ENSP00000232003
resolver
ensp
ENSP00000557916
resolver
enst
ENST00000232003
resolver
genesymbol
HRG
resolver
hgnc
HGNC:5181
resolver
uniprot
B9EK35
resolver
uniprot
D3DNU7
resolver
uniprot_entry
HRG_HUMAN
resolver
uniprot_sec
B9EK35
resolver
uniprot_sec
D3DNU7
resolver
amino_acid_sequence
MKALIAALLLITLQYSCAVSPTDCSAVEPEAEKALDLINKRRRDGYLFQLLRIADAHLDRVENTTVYYLVLDVQESDCSVLSRKYWNDCEPPDSRRPSEIVIGQCKVIATRHSHESQDLRVIDFNCTTSSVSSALANTKDSPVLIDFFEDTERYRKQANKALEKYKEENDDFASFRVDRIERVARVRGGEGTGYFVDFSVRNCPRHHFPRHPNVFGFCRADLFYDVEALDLESPKNLVINCEVFDPQEHENINGVPPHLGHPFHWGGHERSSTTKPPFKPHGSRDHHHPHKPHEHGPPPPPDERDHSHGPPLPQGPPPLLPMSCSSCQHATFGTNGAQRHSHNNNSSDLHPHKHHSHEQHPHGHHPHAHHPHEHDTHRQHPHGHHPHGHHPHGHHPHGHHPHGHHPHCHDFQDYGPCDPPPHNQGHCCHGHGPPPGHLRRRGPGKGPRPFHCRQIGSVYRLPPLRKGEVLPLPEANFPSFPLPHHKHPLKPDNQPFPQSVSESCPGKFKSGFPQVSMFFTHTFPK
uniprot
proteins
disease_involvement
DISEASE: Thrombophilia due to histidine-rich glycoprotein deficiency (THPH11) [MIM:613116]: A hemostatic disorder characterized by a tendency to thrombosis. {ECO:0000269|PubMed:11057869, ECO:0000269|PubMed:9414276}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: 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. {ECO:0000269|PubMed:11134179, ECO:0000269|PubMed:12235005, ECO:0000269|PubMed:14744774, ECO:0000269|PubMed:15220341, ECO:0000269|PubMed:15313924, ECO:0000269|PubMed:16436387, ECO:0000269|PubMed:16489009, ECO:0000269|PubMed:19285951, ECO:0000269|PubMed:19535045, ECO:0000269|PubMed:19712047, ECO:0000269|PubMed:19903770, ECO:0000269|PubMed:20573803, ECO:0000269|PubMed:21215706, ECO:0000269|PubMed:21304106}.
uniprot
proteins
mass_dalton
59578
uniprot
proteins
post_translational_modification
PTM: Proteolytic cleavage produces several HRG fragments which are mostly disulfide-linked and, therefore, not released. Cleavage by plasmin is inhibited in the presence of heparin, zinc ions or in an acidic environment. Cleavage reduces binding of HRG to heparan sulfate, but enhances the ability of HRG to bind and tether plasminogen to the cell surface. On platelet activation, releases a 33 kDa antiangiogenic peptide which encompasses the HRR. Also cleaved in the C-terminal by plasmin. {ECO:0000269|PubMed:14744774, ECO:0000269|PubMed:19712047, ECO:0000269|PubMed:19903770}.; PTM: N-glycosylated. {ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19285951}.
uniprot
proteins
pubmed
10514432
uniprot
proteins
pubmed
11057869
uniprot
proteins
pubmed
11134179
uniprot
proteins
pubmed
12235005
uniprot
proteins
pubmed
1459097
uniprot
proteins
pubmed
14744774
uniprot
proteins
pubmed
15138272
uniprot
proteins
pubmed
15220341
uniprot
proteins
pubmed
15313924
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
16436387
uniprot
proteins
pubmed
16489009
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19285951
uniprot
proteins
pubmed
19535045
uniprot
proteins
pubmed
19712047
uniprot
proteins
pubmed
19786305
uniprot
proteins
pubmed
19903770
uniprot
proteins
pubmed
20561914
uniprot
proteins
pubmed
20573803
uniprot
proteins
pubmed
21215706
uniprot
proteins
pubmed
21304106
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
3011081
uniprot
proteins
pubmed
678554
uniprot
proteins
pubmed
8188234
uniprot
proteins
pubmed
9414276
uniprot
proteins
sequence_length
525
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21215706}.
uniprot
proteins