HRG_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HRG_MOUSE
• UniProt AC: Q9ESB3
• Protein Name: Histidine-rich glycoprotein
• Gene Name: Hrg
• Organism: Mus musculus (Mouse).
• Sequence Length: 525
• Subcellular Localization: Secreted.
• Protein Description: 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. 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 (By similarity). Modulates angiogenesis by blocking the CD6-mediated antiangiongenic effect of thrombospondins, THBS1 and THBS2..
• Protein Sequence: MKVLTTALLLVTLQCSHALSPTNCDASEPLAEKVLDLINKGRRSGYVFELLRVSDAHLDRAGTATVYYLALDVIESDCWVLSTKAQDDCLPSRWQSEIVIGQCKVIATRYSNESQDLSVNGYNCTTSSVSSALRNTKDSPVLLDFFEDSELYRKQARKALDKYKTDNGDFASFRVERAERVIRARGGERTNYYVEFSMRNCSTQHFPRSPLVFGFCRALLSYSIETSDLETPDSIDINCEVFNIEDHKDTSDMKPHWGHERPLCDKHLCKLSGSRDHHHTHKTDKLGCPPPPEGKDNSDRPRLQEGALPQLPPGYPPHSGANRTHRPSYNHSCNEHPCHGHRPHGHHPHSHHPPGHHSHGHHPHGHHPHSHHSHGHHPPGHHPHGHHPHGHHPHGHHPHGHHPHGHDFLDYGPCDPPSNSQELKGQYHRGYGPPHGHSRKRGPGKGLFPFHHQQIGYVYRLPPLNIGEVLTLPEANFPSFSLPNCNRSLQPEIQPFPQTASRSCPGKFESEFPQISKFFGYTPPK

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
24	S-palmitoylation	HALSPTNCDASEPLA CCCCCCCCCCCHHHH	5.21	26165157
89	S-palmitoylation	STKAQDDCLPSRWQS ECCCCCCCCCCHHCC	8.95	26165157
112	N-linked_Glycosylation	VIATRYSNESQDLSV EEEEECCCCCCCEEE	43.96	-
123	N-linked_Glycosylation	DLSVNGYNCTTSSVS CEEECCEECCHHHHH	20.32	-
200	N-linked_Glycosylation	YVEFSMRNCSTQHFP EEEEECCCCCCCCCC	18.56	17330941
288	S-palmitoylation	HKTDKLGCPPPPEGK CCCCCCCCCCCCCCC	7.10	26165157
322	N-linked_Glycosylation	YPPHSGANRTHRPSY CCCCCCCCCCCCCCC	53.56	-
330	N-linked_Glycosylation	RTHRPSYNHSCNEHP CCCCCCCCCCCCCCC	25.57	-
438	Phosphorylation	YGPPHGHSRKRGPGK CCCCCCCCCCCCCCC	44.05	-
449	Phosphorylation	GPGKGLFPFHHQQIG CCCCCCCCCCCCCCE	32.48	24719451
485	S-palmitoylation	PSFSLPNCNRSLQPE CCCCCCCCCCCCCCC	4.17	26165157
504	S-palmitoylation	PQTASRSCPGKFESE CCCCCCCCCCCCHHC	5.11	26165157

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of HRG_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HRG_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of HRG_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of HRG_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides.";
Bernhard O.K., Kapp E.A., Simpson R.J.;
J. Proteome Res. 6:987-995(2007).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-200, AND MASSSPECTROMETRY.
PubMed: 17330941