VGFR3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: VGFR3_MOUSE
• UniProt AC: P35917
• Protein Name: Vascular endothelial growth factor receptor 3
• Gene Name: Flt4
• Organism: Mus musculus (Mouse).
• Sequence Length: 1363
• Subcellular Localization: Cell membrane ; Single-pass type I membrane protein . Cytoplasm . Nucleus . Ligand-mediated autophosphorylation leads to rapid internalization.
• Protein Description: Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFC and VEGFD, and plays an essential role in adult lymphangiogenesis and in the development of the vascular network and the cardiovascular system during embryonic development. Promotes proliferation, survival and migration of endothelial cells, and regulates angiogenic sprouting. Signaling by activated FLT4 leads to enhanced production of VEGFC, and to a lesser degree VEGFA, thereby creating a positive feedback loop that enhances FLT4 signaling. Modulates KDR signaling by forming heterodimers. Mediates activation of the MAPK1/ERK2, MAPK3/ERK1 signaling pathway, of MAPK8 and the JUN signaling pathway, and of the AKT1 signaling pathway. Phosphorylates SHC1. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase. Promotes phosphorylation of MAPK8 at 'Thr-183' and 'Tyr-185', and of AKT1 at 'Ser-473'..
• Protein Sequence: MQPGAALNLRLWLCLGLLQGLANGYSMTPPTLNITEDSYVIDTGDSLSISCRGQHPLEWTWPGAQEVLTTGGKDSEDTRVVHDCEGTEARPYCKVLLLAQTHANNTGSYHCYYKYIKARIEGTTAASTYVFVRDFKHPFINKPDTLLVNRKDSMWVPCLVSIPGLNITLRSQSSALHPDGQEVLWDDRRGMRVPTQLLRDALYLQCETTWGDQNFLSNLFVVHITGNELYDIQLYPKKSMELLVGEKLVLNCTVWAEFDSGVTFDWDYPGKQAERAKWVPERRSQQTHTELSSILTIHNVSQNDLGPYVCEANNGIQRFRESTEVIVHEKPFISVEWLKGPVLEATAGDELVKLPVKLAAYPPPEFQWYKDRKAVTGRHNPHALVLKEVTEASAGVYTLALWNSAAGLRQNISLELVVNVPPHIHEKEASSPSIYSRHSRQTLTCTAYGVPQPLSVQWHWRPWTPCKTFAQRSLRRRQQRDGMPQCRDWKEVTTQDAVNPIESLDSWTEFVEGKNKTVSKLVIQDANVSAMYKCVVVNKVGQDERLIYFYVTTIPDGFSIESEPSEDPLEGQSVRLSCRADNYTYEHLRWYRLNLSTLHDAQGNPLLLDCKNVHLFATPLEANLEEAEPGARHATLSLNIPRVAPEDEGDYVCEVQDRRSQDKHCHKKYLSVQALEAPRLTQNLTDLLVNVSDSLEMRCPVAGAHVPSIVWYKDERLLEKESGIDLADSNQRLSIQRVREEDAGRYLCSVCNAKGCVNSSASVAVEGSEDKGSMEIVILIGTGVIAVFFWVLLLLIFCNMKRPAHADIKTGYLSIIMDPGEVPLEEQCEYLSYDASQWEFPRERLHLGRVLGHGAFGKVVEASAFGINKGSSCDTVAVKMLKEGATASEHRALMSELKILIHIGNHLNVVNLLGACTKPNGPLMVIVEFCKYGNLSNFLRVKRDTFNPYAEKSPEQRRRFRAMVEGAKADRRRPGSSDRALFTRFLMGKGSARRAPLVQEAEDLWLSPLTMEDLVCYSFQVARGMEFLASRKCIHRDLAARNILLSESDIVKICDFGLARDIYKDPDYVRKGSARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGVQINEEFCQRLKDGTRMRAPELATPAIRHIMQSCWSGDPKARPAFSDLVEILGDLLQGGGWQEEEEERMALHSSQSSEEDGFMQASTTALHITEADADDSPPSMHCHSLAARYYNCVSFPGRLARGTKTPGSSRMKTFEELPMTPTTYKASMDNQTDSGMVLASEEFEELESRHRPEGSFSCKGPGQHMDIPRGHPDPQGRRRRPTQGAQGGKVFYNNEYGEVSQPCTEGDCCPSAGSTFFADSSY

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
33	N-linked_Glycosylation	SMTPPTLNITEDSYV CCCCCCCCCCCCCEE	41.43	-
104	N-linked_Glycosylation	LLAQTHANNTGSYHC EEEECCCCCCCCEEE	38.70	-
128	Phosphorylation	EGTTAASTYVFVRDF CCCCCCEEEEEEECC	20.98	21454597
166	N-linked_Glycosylation	LVSIPGLNITLRSQS EEECCCCCEEECCCC	30.98	-
251	N-linked_Glycosylation	VGEKLVLNCTVWAEF CCCEEEEEEEEEEEC	16.37	-
299	N-linked_Glycosylation	SSILTIHNVSQNDLG HHHEEEEECCHHHCH	31.14	-
411	N-linked_Glycosylation	SAAGLRQNISLELVV CCCCCCCCEEEEEEE	21.27	-
515	N-linked_Glycosylation	TEFVEGKNKTVSKLV HHHCCCCCCEEEEEE	56.97	-
527	N-linked_Glycosylation	KLVIQDANVSAMYKC EEEEECCCHHCEEEE	36.24	-
582	N-linked_Glycosylation	RLSCRADNYTYEHLR EEEEECCCCHHHEEE	30.02	16944957
594	N-linked_Glycosylation	HLRWYRLNLSTLHDA EEEEEEECHHHCCCC	23.97	-
683	N-linked_Glycosylation	EAPRLTQNLTDLLVN HCHHHHCCHHHHHCH	39.41	-
690	N-linked_Glycosylation	NLTDLLVNVSDSLEM CHHHHHCHHHHHCHH	27.78	-
734	Phosphorylation	ADSNQRLSIQRVREE CCCCCCEEEEEECHH	20.90	25367039
758	N-linked_Glycosylation	CNAKGCVNSSASVAV HCCCCCCCCCCEEEE	34.03	-
830	Phosphorylation	PLEEQCEYLSYDASQ CHHHHHCEECCCHHH	14.47	-
833	Phosphorylation	EQCEYLSYDASQWEF HHHCEECCCHHHCCC	16.97	-
949	Phosphorylation	KRDTFNPYAEKSPEQ CCCCCCCCCCCCHHH	28.62	22871156
953	Phosphorylation	FNPYAEKSPEQRRRF CCCCCCCCHHHHHHH	25.77	26824392
1063	Phosphorylation	FGLARDIYKDPDYVR CCCCCHHHCCCCHHC	17.39	15673613
1064	Ubiquitination	GLARDIYKDPDYVRK CCCCHHHCCCCHHCC	64.22	-
1068	Phosphorylation	DIYKDPDYVRKGSAR HHHCCCCHHCCCCCC	13.93	25159016
1230	Phosphorylation	CHSLAARYYNCVSFP HHHHHHHHHCCCCCC	8.36	22817900
1231	Phosphorylation	HSLAARYYNCVSFPG HHHHHHHHCCCCCCC	9.13	22817900
1265	Phosphorylation	LPMTPTTYKASMDNQ CCCCCCEEECCCCCC	13.67	22817900
1268	Phosphorylation	TPTTYKASMDNQTDS CCCEEECCCCCCCCC	23.63	28059163
1298	Phosphorylation	HRPEGSFSCKGPGQH CCCCCCCCCCCCCCC	19.33	28059163
1333	Phosphorylation	AQGGKVFYNNEYGEV CCCCEEEECCCCCCC	21.77	22817900
1337	Phosphorylation	KVFYNNEYGEVSQPC EEEECCCCCCCCCCC	22.25	22817900
1363	Phosphorylation	TFFADSSY------- CEEECCCC-------	26.90	12881528

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
830	Y	Phosphorylation	Kinase	SRC	P05480	Uniprot
833	Y	Phosphorylation	Kinase	SRC	P05480	Uniprot
1063	Y	Phosphorylation	Kinase	SRC	P05480	Uniprot
1230	Y	Phosphorylation	Kinase	KDR	P35918	GPS
1231	Y	Phosphorylation	Kinase	KDR	P35918	GPS
1265	Y	Phosphorylation	Kinase	KDR	P35918	GPS
1333	Y	Phosphorylation	Kinase	SRC	P05480	Uniprot
1337	Y	Phosphorylation	Kinase	SRC	P05480	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of VGFR3_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 VGFR3_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of VGFR3_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

"Proteome-wide characterization of N-glycosylation events by diagonalchromatography.";
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,Gevaert K.;
J. Proteome Res. 5:2438-2447(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-582, AND MASSSPECTROMETRY.
PubMed: 16944957