VEGFD_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: VEGFD_HUMAN
• UniProt AC: O43915
• Protein Name: Vascular endothelial growth factor D {ECO:0000312|HGNC:HGNC:3708}
• Gene Name: VEGFD {ECO:0000312|HGNC:HGNC:3708}
• Organism: Homo sapiens (Human).
• Sequence Length: 354
• Subcellular Localization: Secreted.
• Protein Description: Growth factor active in angiogenesis, lymphangiogenesis and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. May function in the formation of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentiated lymphatic endothelium in adults. Binds and activates VEGFR-2 (KDR/FLK1) and VEGFR-3 (FLT4) receptors..
• Protein Sequence: MYREWVVVNVFMMLYVQLVQGSSNEHGPVKRSSQSTLERSEQQIRAASSLEELLRITHSEDWKLWRCRLRLKSFTSMDSRSASHRSTRFAATFYDIETLKVIDEEWQRTQCSPRETCVEVASELGKSTNTFFKPPCVNVFRCGGCCNEESLICMNTSTSYISKQLFEISVPLTSVPELVPVKVANHTGCKCLPTAPRHPYSIIRRSIQIPEEDRCSHSKKLCPIDMLWDSNKCKCVLQEENPLAGTEDHSHLQEPALCGPHMMFDEDRCECVCKTPCPKDLIQHPKNCSCFECKESLETCCQKHKLFHPDTCSCEDRCPFHTRPCASGKTACAKHCRFPKEKRAAQGPHSRKNP

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
155	N-linked_Glycosylation	EESLICMNTSTSYIS CCCEEEEECCCHHHH	26.85	21148085
185	N-linked_Glycosylation	LVPVKVANHTGCKCL CEEEEECCCCCCCCC	35.92	21148085
187	Phosphorylation	PVKVANHTGCKCLPT EEEECCCCCCCCCCC	44.04	30266825
287	N-linked_Glycosylation	DLIQHPKNCSCFECK HHHCCCCCCCCHHCH	27.64	UniProtKB CARBOHYD

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

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

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
VGFR2_HUMAN	KDR	physical	9435229
UBR4_HUMAN	UBR4	physical	26186194
ZER1_HUMAN	ZER1	physical	26186194
ADAM9_HUMAN	ADAM9	physical	26186194
BIRC6_HUMAN	BIRC6	physical	26186194
KCMF1_HUMAN	KCMF1	physical	26186194
TBB8_HUMAN	TUBB8	physical	26186194
MOCS3_HUMAN	MOCS3	physical	26186194
OAF_HUMAN	OAF	physical	26186194
ADAM9_HUMAN	ADAM9	physical	28514442
UBR4_HUMAN	UBR4	physical	28514442
BIRC6_HUMAN	BIRC6	physical	28514442
KCMF1_HUMAN	KCMF1	physical	28514442

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Structural determinants of vascular endothelial growth factor-D -receptor binding and specificity.";
Leppanen V.M., Jeltsch M., Anisimov A., Tvorogov D., Aho K.,Kalkkinen N., Toivanen P., Yla-Herttuala S., Ballmer-Hofer K.,Alitalo K.;
Blood 117:1507-1515(2011).
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 92-195 OF MUTANT ALA-117,FUNCTION, SUBUNIT, GLYCOSYLATION AT ASN-155 AND ASN-185, AND DISULFIDEBONDS.
PubMed: 21148085