UniProt ID | VEGFC_HUMAN | |
---|---|---|
UniProt AC | P49767 | |
Protein Name | Vascular endothelial growth factor C | |
Gene Name | VEGFC | |
Organism | Homo sapiens (Human). | |
Sequence Length | 419 | |
Subcellular Localization | Secreted. | |
Protein Description | Growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. May function in angiogenesis of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentiated lymphatic endothelium in adults. Binds and activates KDR/VEGFR2 and FLT4/VEGFR3 receptors.. | |
Protein Sequence | MHLLGFFSVACSLLAAALLPGPREAPAAAAAFESGLDLSDAEPDAGEATAYASKDLEEQLRSVSSVDELMTVLYPEYWKMYKCQLRKGGWQHNREQANLNSRTEETIKFAAAHYNTEILKSIDNEWRKTQCMPREVCIDVGKEFGVATNTFFKPPCVSVYRCGGCCNSEGLQCMNTSTSYLSKTLFEITVPLSQGPKPVTISFANHTSCRCMSKLDVYRQVHSIIRRSLPATLPQCQAANKTCPTNYMWNNHICRCLAQEDFMFSSDAGDDSTDGFHDICGPNKELDEETCQCVCRAGLRPASCGPHKELDRNSCQCVCKNKLFPSQCGANREFDENTCQCVCKRTCPRNQPLNPGKCACECTESPQKCLLKGKKFHHQTCSCYRRPCTNRQKACEPGFSYSEEVCRCVPSYWKRPQMS | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
101 | Phosphorylation | REQANLNSRTEETIK HHHHCCCCCCHHHHH | 43.69 | 18491316 | |
106 | Phosphorylation | LNSRTEETIKFAAAH CCCCCHHHHHHHHHH | 24.20 | 18491316 | |
175 | N-linked_Glycosylation | SEGLQCMNTSTSYLS CCCCCCCCCCHHHHC | 38.20 | 20145116 | |
205 | N-linked_Glycosylation | PVTISFANHTSCRCM CEEEEECCCCCCCHH | 36.64 | 20145116 | |
223 | Phosphorylation | DVYRQVHSIIRRSLP HHHHHHHHHHHHHCC | 22.36 | 24719451 | |
240 | N-linked_Glycosylation | LPQCQAANKTCPTNY CHHHHHCCCCCCCHH | 43.09 | UniProtKB CARBOHYD |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of VEGFC_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of VEGFC_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of VEGFC_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
VEGFC_HUMAN | VEGFC | physical | 9233800 |
Kegg Disease | ||||||
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There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
615907 | Lymphedema, hereditary, 1D (LMPH1D) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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N-linked Glycosylation | |
Reference | PubMed |
"Structural determinants of growth factor binding and specificity byVEGF receptor 2."; Leppanen V.M., Prota A.E., Jeltsch M., Anisimov A., Kalkkinen N.,Strandin T., Lankinen H., Goldman A., Ballmer-Hofer K., Alitalo K.; Proc. Natl. Acad. Sci. U.S.A. 107:2425-2430(2010). Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 112-215 IN COMPLEX WITH KDR,FUNCTION, DISULFIDE BONDS, GLYCOSYLATION AT ASN-175 AND ASN-205, ANDSUBUNIT. |