VEGFC_HUMAN - dbPTM
VEGFC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
101PhosphorylationREQANLNSRTEETIK
HHHHCCCCCCHHHHH
43.6918491316
106PhosphorylationLNSRTEETIKFAAAH
CCCCCHHHHHHHHHH
24.2018491316
175N-linked_GlycosylationSEGLQCMNTSTSYLS
CCCCCCCCCCHHHHC
38.2020145116
205N-linked_GlycosylationPVTISFANHTSCRCM
CEEEEECCCCCCCHH
36.6420145116
223PhosphorylationDVYRQVHSIIRRSLP
HHHHHHHHHHHHHCC
22.3624719451
240N-linked_GlycosylationLPQCQAANKTCPTNY
CHHHHHCCCCCCCHH
43.09UniProtKB CARBOHYD

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

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VEGFC_HUMANVEGFCphysical
9233800

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615907Lymphedema, hereditary, 1D (LMPH1D)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VEGFC_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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.

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