VGFR2_HUMAN - dbPTM
VGFR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VGFR2_HUMAN
UniProt AC P35968
Protein Name Vascular endothelial growth factor receptor 2
Gene Name KDR
Organism Homo sapiens (Human).
Sequence Length 1356
Subcellular Localization Cell junction. Endoplasmic reticulum . Localized with RAP1A at cell-cell junctions (By similarity). Colocalizes with ERN1 and XBP1 in the endoplasmic reticulum in endothelial cells in a vascular endothelial growth factor (VEGF)-dependent manner (PubM
Protein Description Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFC and VEGFD. Plays an essential role in the regulation of angiogenesis, vascular development, vascular permeability, and embryonic hematopoiesis. Promotes proliferation, survival, migration and differentiation of endothelial cells. Promotes reorganization of the actin cytoskeleton. Isoforms lacking a transmembrane domain, such as isoform 2 and isoform 3, may function as decoy receptors for VEGFA, VEGFC and/or VEGFD. Isoform 2 plays an important role as negative regulator of VEGFA- and VEGFC-mediated lymphangiogenesis by limiting the amount of free VEGFA and/or VEGFC and preventing their binding to FLT4. Modulates FLT1 and FLT4 signaling by forming heterodimers. Binding of vascular growth factors to isoform 1 leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, reorganization of the actin cytoskeleton and activation of PTK2/FAK1. Required for VEGFA-mediated induction of NOS2 and NOS3, leading to the production of the signaling molecule nitric oxide (NO) by endothelial cells. Phosphorylates PLCG1. Promotes phosphorylation of FYN, NCK1, NOS3, PIK3R1, PTK2/FAK1 and SRC..
Protein Sequence MQSKVLLAVALWLCVETRAASVGLPSVSLDLPRLSIQKDILTIKANTTLQITCRGQRDLDWLWPNNQSGSEQRVEVTECSDGLFCKTLTIPKVIGNDTGAYKCFYRETDLASVIYVYVQDYRSPFIASVSDQHGVVYITENKNKTVVIPCLGSISNLNVSLCARYPEKRFVPDGNRISWDSKKGFTIPSYMISYAGMVFCEAKINDESYQSIMYIVVVVGYRIYDVVLSPSHGIELSVGEKLVLNCTARTELNVGIDFNWEYPSSKHQHKKLVNRDLKTQSGSEMKKFLSTLTIDGVTRSDQGLYTCAASSGLMTKKNSTFVRVHEKPFVAFGSGMESLVEATVGERVRIPAKYLGYPPPEIKWYKNGIPLESNHTIKAGHVLTIMEVSERDTGNYTVILTNPISKEKQSHVVSLVVYVPPQIGEKSLISPVDSYQYGTTQTLTCTVYAIPPPHHIHWYWQLEEECANEPSQAVSVTNPYPCEEWRSVEDFQGGNKIEVNKNQFALIEGKNKTVSTLVIQAANVSALYKCEAVNKVGRGERVISFHVTRGPEITLQPDMQPTEQESVSLWCTADRSTFENLTWYKLGPQPLPIHVGELPTPVCKNLDTLWKLNATMFSNSTNDILIMELKNASLQDQGDYVCLAQDRKTKKRHCVVRQLTVLERVAPTITGNLENQTTSIGESIEVSCTASGNPPPQIMWFKDNETLVEDSGIVLKDGNRNLTIRRVRKEDEGLYTCQACSVLGCAKVEAFFIIEGAQEKTNLEIIILVGTAVIAMFFWLLLVIILRTVKRANGGELKTGYLSIVMDPDELPLDEHCERLPYDASKWEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATCRTVAVKMLKEGATHSEHRALMSELKILIHIGHHLNVVNLLGACTKPGGPLMVIVEFCKFGNLSTYLRSKRNEFVPYKTKGARFRQGKDYVGAIPVDLKRRLDSITSSQSSASSGFVEEKSLSDVEEEEAPEDLYKDFLTLEHLICYSFQVAKGMEFLASRKCIHRDLAARNILLSEKNVVKICDFGLARDIYKDPDYVRKGDARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKIDEEFCRRLKEGTRMRAPDYTTPEMYQTMLDCWHGEPSQRPTFSELVEHLGNLLQANAQQDGKDYIVLPISETLSMEEDSGLSLPTSPVSCMEEEEVCDPKFHYDNTAGISQYLQNSKRKSRPVSVKTFEDIPLEEPEVKVIPDDNQTDSGMVLASEELKTLEDRTKLSPSFGGMVPSKSRESVASEGSNQTSGYQSGYHSDDTDTTVYSSEEAELLKLIEIGVQTGSTAQILQPDSGTTLSSPPV
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
46N-linked_GlycosylationDILTIKANTTLQITC
CEEEEECCCEEEEEE		28.70UniProtKB CARBOHYD
66N-linked_GlycosylationLDWLWPNNQSGSEQR
CCCCCCCCCCCCCEE		33.06UniProtKB CARBOHYD
96N-linked_GlycosylationTIPKVIGNDTGAYKC
ECCEEECCCCCCHHE		32.33UniProtKB CARBOHYD
143N-linked_GlycosylationVYITENKNKTVVIPC
EEEECCCCEEEEEEC		57.7320145116
158N-linked_GlycosylationLGSISNLNVSLCARY
CCHHHCCCHHHHHCC		26.11UniProtKB CARBOHYD
160PhosphorylationSISNLNVSLCARYPE
HHHCCCHHHHHCCCC		19.3624719451
224PhosphorylationVVVGYRIYDVVLSPS
EEECCCEEEEEECCC		8.1623879269
229PhosphorylationRIYDVVLSPSHGIEL
CEEEEEECCCCCEEE		16.8523879269
237PhosphorylationPSHGIELSVGEKLVL
CCCCEEEECCCEEEE		18.4523879269
245N-linked_GlycosylationVGEKLVLNCTARTEL
CCCEEEEECEECCEE		17.3920145116
250PhosphorylationVLNCTARTELNVGID
EEECEECCEEEECCC		42.2223879269
290PhosphorylationSEMKKFLSTLTIDGV
HHHHHHHHCCEECCC		25.2230108239
291PhosphorylationEMKKFLSTLTIDGVT
HHHHHHHCCEECCCC		30.0230108239
293PhosphorylationKKFLSTLTIDGVTRS
HHHHHCCEECCCCCC		19.6730108239
298PhosphorylationTLTIDGVTRSDQGLY
CCEECCCCCCCCCCE		29.9530108239
318N-linked_GlycosylationSGLMTKKNSTFVRVH
CCCCCCCCCCEEEEE		48.0820145116
374N-linked_GlycosylationNGIPLESNHTIKAGH
CCCCCCCCCEEECCC		27.26UniProtKB CARBOHYD
395N-linked_GlycosylationVSERDTGNYTVILTN
EEECCCCCEEEEECC		31.25UniProtKB CARBOHYD
477O-linked_GlycosylationPSQAVSVTNPYPCEE
CCCCCEECCCCCCHH		23.99OGP
511N-linked_GlycosylationFALIEGKNKTVSTLV
EEEEECCCCEEEEEE		56.97UniProtKB CARBOHYD
515PhosphorylationEGKNKTVSTLVIQAA
ECCCCEEEEEEEEEC		22.6626074081
516PhosphorylationGKNKTVSTLVIQAAN
CCCCEEEEEEEEECC		22.2526074081
523N-linked_GlycosylationTLVIQAANVSALYKC
EEEEEECCHHHHEEE		31.15UniProtKB CARBOHYD
525PhosphorylationVIQAANVSALYKCEA
EEEECCHHHHEEEEE		16.6226437602
580N-linked_GlycosylationADRSTFENLTWYKLG
CCCCCCCCCCEEECC		38.28UniProtKB CARBOHYD
613N-linked_GlycosylationLDTLWKLNATMFSNS
HHHHHHHCCEEECCC		29.64UniProtKB CARBOHYD
619N-linked_GlycosylationLNATMFSNSTNDILI
HCCEEECCCCCCEEE		41.40UniProtKB CARBOHYD
631N-linked_GlycosylationILIMELKNASLQDQG
EEEEEECCCCCCCCC		47.59UniProtKB CARBOHYD
660 (in isoform 2)Phosphorylation-18.0829523821
675N-linked_GlycosylationTITGNLENQTTSIGE
CCCCCCCCCCCCCCC		47.90UniProtKB CARBOHYD
704N-linked_GlycosylationQIMWFKDNETLVEDS
CEEEEECCCCEEECC		44.75UniProtKB CARBOHYD
711PhosphorylationNETLVEDSGIVLKDG
CCCEEECCCEEEECC		19.53-
721N-linked_GlycosylationVLKDGNRNLTIRRVR
EEECCCCCEEEEEEE		45.60UniProtKB CARBOHYD
723PhosphorylationKDGNRNLTIRRVRKE
ECCCCCEEEEEEECC		18.9124719451
799PhosphorylationANGGELKTGYLSIVM
HCCCCCCEEEEEEEE		43.6227251275
801PhosphorylationGGELKTGYLSIVMDP
CCCCCEEEEEEEECC		11.5118936167
803PhosphorylationELKTGYLSIVMDPDE
CCCEEEEEEEECCCC		12.4927251275
822PhosphorylationEHCERLPYDASKWEF
HHHHCCCCCHHHCCC		28.8227251275
825PhosphorylationERLPYDASKWEFPRD
HCCCCCHHHCCCCHH		35.0927251275
826AcetylationRLPYDASKWEFPRDR
CCCCCHHHCCCCHHH		53.0826210075
875PhosphorylationKMLKEGATHSEHRAL
HHHHCCCCHHHHHHH		36.4729514088
877PhosphorylationLKEGATHSEHRALMS
HHCCCCHHHHHHHHH		30.6429514088
884PhosphorylationSEHRALMSELKILIH
HHHHHHHHHHHHHHH		40.4029514088
951PhosphorylationRFRQGKDYVGAIPVD
HHCCCCCCCCCEECC		12.3110102632
960AcetylationGAIPVDLKRRLDSIT
CCEECCHHHHHHHCC		30.8919816163
982PhosphorylationSGFVEEKSLSDVEEE
CCCCCCCCCCCCCHH		36.0623403867
984PhosphorylationFVEEKSLSDVEEEEA
CCCCCCCCCCCHHHC		46.8623403867
996PhosphorylationEEAPEDLYKDFLTLE
HHCCHHHHHHHHCHH		22.3410102632
1037PhosphorylationAARNILLSEKNVVKI
HHHHHHHCCCCEEEE		42.9824719451
1054PhosphorylationFGLARDIYKDPDYVR
CCCCCHHHCCCCHHC		17.3916286478
1055UbiquitinationGLARDIYKDPDYVRK
CCCCHHHCCCCHHCC		64.22-
1059PhosphorylationDIYKDPDYVRKGDAR
HHHCCCCHHCCCCCC		13.9316286478
1175PhosphorylationAQQDGKDYIVLPISE
HHCCCCCEEEEEEEC		9.0916286478
1214PhosphorylationVCDPKFHYDNTAGIS
CCCCCCCCCCHHHHH		17.6415962004
1217PhosphorylationPKFHYDNTAGISQYL
CCCCCCCHHHHHHHH		24.3022817900
1223PhosphorylationNTAGISQYLQNSKRK
CHHHHHHHHHHCCCC		11.94-
1227PhosphorylationISQYLQNSKRKSRPV
HHHHHHHCCCCCCCC		22.3723403867
1231PhosphorylationLQNSKRKSRPVSVKT
HHHCCCCCCCCEEEE		45.9423403867
1235PhosphorylationKRKSRPVSVKTFEDI
CCCCCCCEEEEECCC		22.1523403867
1238PhosphorylationSRPVSVKTFEDIPLE
CCCCEEEEECCCCCC		30.0519664994
1258PhosphorylationVIPDDNQTDSGMVLA
ECCCCCCCCCCEEEE		38.0923403867
1260PhosphorylationPDDNQTDSGMVLASE
CCCCCCCCCEEEECH		31.9823403867
1279PhosphorylationLEDRTKLSPSFGGMV
HHHHHCCCCCCCCCC		21.7623403867
1281PhosphorylationDRTKLSPSFGGMVPS
HHHCCCCCCCCCCCC		32.90-
1288PhosphorylationSFGGMVPSKSRESVA
CCCCCCCCCCCHHHH		31.67-
1290PhosphorylationGGMVPSKSRESVASE
CCCCCCCCCHHHHCC		45.69-
1305PhosphorylationGSNQTSGYQSGYHSD
CCCCCCCCCCCCCCC		10.1615962004
1309PhosphorylationTSGYQSGYHSDDTDT
CCCCCCCCCCCCCCC		11.9115962004
1319PhosphorylationDDTDTTVYSSEEAEL
CCCCCEEECHHHHHH		12.3721827946
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
229SPhosphorylationKinaseCDK5Q00535
PSP
951YPhosphorylationKinaseKDRP35968
GPS
996YPhosphorylationKinaseKDRP35968
GPS
1054YPhosphorylationKinaseKDRP35968
GPS
1059YPhosphorylationKinaseKDRP35968
GPS
1175YPhosphorylationKinaseSRCP12931
PSP
1175YPhosphorylationKinaseKDRP35968
GPS
1214YPhosphorylationKinaseKDRP35968
GPS
1305YPhosphorylationKinaseKDRP35968
GPS
1309YPhosphorylationKinaseKDRP35968
GPS
1319YPhosphorylationKinaseKDRP35968
GPS
-KUbiquitinationE3 ubiquitin ligaseBTRCQ9Y297
PMID:22711876
-KUbiquitinationE3 ubiquitin ligaseCBLP22681
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseNEDD4P46934
PMID:15060076
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VGFR2_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 VGFR2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANXA5_HUMANANXA5physical
10329451
SHC2_HUMANSHC2physical
10749680
PLXA1_HUMANPLXNA1physical
14977921
CADH5_HUMANCDH5physical
11950700
PPAC_HUMANACP1physical
10608891
GRB2_HUMANGRB2physical
10319320
SHC1_HUMANSHC1physical
10319320
RASA1_HUMANRASA1physical
10319320
PLCG1_HUMANPLCG1physical
9398617
FBW1A_HUMANBTRCphysical
21402774
CUL1_HUMANCUL1physical
22711876
FBW1A_HUMANBTRCphysical
22711876
FBW1B_HUMANFBXW11physical
22711876
EPN1_HUMANEPN1physical
23187125
MYO1C_HUMANMYO1Cphysical
23262137
CAV1_HUMANCAV1physical
23262137
1433G_HUMANYWHAGphysical
26496610
ZSC21_HUMANZSCAN21physical
26496610
NCOA4_HUMANNCOA4physical
26496610
PALLD_HUMANPALLDphysical
26496610
AAR2_HUMANAAR2physical
26496610
NNRD_HUMANCARKDphysical
26496610
TUT7_HUMANZCCHC6physical
26496610
GATC_HUMANGATCphysical
26496610
SH22A_HUMANSH2D2Aphysical
22689825
SRC_HUMANSRCphysical
22689825
SHC2_HUMANSHC2physical
12214271
NCK1_HUMANNCK1physical
12214271
SHC2_HUMANSHC2physical
9790910
VEGFA_HUMANVEGFAphysical
19818105
A4_HUMANAPPphysical
19818105
PTN6_HUMANPTPN6physical
28065597
PTN11_HUMANPTPN11physical
28065597
PTN12_HUMANPTPN12physical
28065597
PTPRR_HUMANPTPRRphysical
28065597
PPM1A_HUMANPPM1Aphysical
28065597
PPM1B_HUMANPPM1Bphysical
28065597
ILKAP_HUMANILKAPphysical
28065597
DUS19_HUMANDUSP19physical
28065597
STYX_HUMANSTYXphysical
28065597
VGFR2_HUMANKDRphysical
20190562
MK01_HUMANMAPK1physical
20190562
P53_HUMANTP53genetic
27438146
PTN11_HUMANPTPN11physical
16339483
IL3RB_HUMANCSF2RBphysical
16007196
VGFR2_HUMANKDRphysical
16007196
DYN2_HUMANDNM2physical
16049137
VGFR2_HUMANKDRphysical
10102632
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
602089Hemangioma, capillary infantile (HCI)
Kegg Drug
D03218 Axitinib (JAN/USAN); Inlyta (TN)
D05029 Midostaurin (USAN/INN)
D05380 Pazopanib hydrochloride (JAN/USAN); Votrient (TN)
D05819 Semaxanib (USAN/INN)
D06272 Sorafenib tosilate (JAN); Sorafenib tosylate (USAN); Nexavar (TN)
D06285 Vatalanib (USAN/INN)
D06402 Sunitinib malate (JAN/USAN); Sutent (TN)
D06407 Vandetanib (JAN/USAN/INN); Caprelsa (TN)
D06678 Motesanib; AMG 706
D08503 Toceranib (USAN)
D08524 Sorafenib (USAN/INN)
D08544 Toceranib phosphate (USAN)
D08552 Sunitinib (INN)
D08878 Brivanib alaninate (JAN/USAN/INN)
D08881 Cediranib (USAN/INN)
D08883 Cediranib maleate (JAN/USAN)
D08907 Dovitinib lactate (USAN)
D08947 Motesanib phosphate (JAN); Motesanib diphosphate (USAN)
D09371 Ramucirumab (USAN)
D09589 Brivanib (USAN)
D09618 Foretinib (USAN/INN)
D09635 Linifanib (USAN/INN)
D09683 Tivozanib (USAN/INN)
D09945 Pegdinetanib (USAN/INN)
D10062 Cabozantinib (USAN)
D10095 Cabozantinib s-malate (USAN); Cometriq (TN)
D10190 Tivozanib hydrochloride (USAN); Tivozanib hydrochloride monohydrate
D10224 Golvatinib (USAN)
D10396 Nintedanib esylate (USAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VGFR2_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"The structural basis for the function of two anti-VEGF receptor 2antibodies.";
Franklin M.C., Navarro E.C., Wang Y., Patel S., Singh P., Zhang Y.,Persaud K., Bari A., Griffith H., Shen L., Balderes P., Kussie P.;
Structure 19:1097-1107(2011).
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 220-338 IN COMPLEX WITHANTIBODY FRAGMENT, DISULFIDE BOND, AND GLYCOSYLATION AT ASN-245 ANDASN-318.
"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 (2.70 ANGSTROMS) OF 120-326 IN COMPLEX WITHVEGFC, INTERACTION WITH VEGFC, DOMAIN, DISULFIDE BONDS, ANDGLYCOSYLATION AT ASN-143; ASN-245 AND ASN-318.
Phosphorylation
ReferencePubMed
"Crystal structure of the kinase domain of human vascular endothelialgrowth factor receptor 2: a key enzyme in angiogenesis.";
McTigue M.A., Wickersham J.A., Pinko C., Showalter R.E., Parast C.V.,Tempczyk-Russell A., Gehring M.R., Mroczkowski B., Kan C.-C.,Villafranca J.E., Appelt K.;
Structure 7:319-330(1999).
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 806-1171, FUNCTION,PHOSPHORYLATION AT TYR-1059, AND MASS SPECTROMETRY.
"New role for the protein tyrosine phosphatase DEP-1 in Akt activationand endothelial cell survival.";
Chabot C., Spring K., Gratton J.P., Elchebly M., Royal I.;
Mol. Cell. Biol. 29:241-253(2009).
Cited for: PHOSPHORYLATION AT TYR-801; TYR-951; TYR-996; TYR-1054; TYR-1059;TYR-1175 AND TYR-1214; DEPHOSPHORYLATION BY PTPRJ AT TYR-951; TYR-996;TYR-1054; TYR-1059; TYR-1175 AND TYR-1214.
"Transcriptional profiling reveals a critical role for tyrosinephosphatase VE-PTP in regulation of VEGFR2 activity and endothelialcell morphogenesis.";
Mellberg S., Dimberg A., Bahram F., Hayashi M., Rennel E., Ameur A.,Westholm J.O., Larsson E., Lindahl P., Cross M.J., Claesson-Welsh L.;
FASEB J. 23:1490-1502(2009).
Cited for: PHOSPHORYLATION AT TYR-951; TYR-1175 AND TYR-1214, ANDDEPHOSPHORYLATION BY PTPRB.
"Phosphorylation of tyrosine 801 of vascular endothelial growth factorreceptor-2 is necessary for Akt-dependent endothelial nitric-oxidesynthase activation and nitric oxide release from endothelial cells.";
Blanes M.G., Oubaha M., Rautureau Y., Gratton J.P.;
J. Biol. Chem. 282:10660-10669(2007).
Cited for: FUNCTION IN ACTIVATION OF AKT1; PHOSPHORYLATION OF PLCG1 AND NOS3 ANDREGULATION OF NITRIC OXIDE PRODUCTION, PHOSPHORYLATION AT TYR-801, ANDMUTAGENESIS OF TYR-801.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1054 AND TYR-1059, ANDMASS SPECTROMETRY.
"VEGF receptor-2 Y951 signaling and a role for the adapter moleculeTSAd in tumor angiogenesis.";
Matsumoto T., Bohman S., Dixelius J., Berge T., Dimberg A.,Magnusson P., Wang L., Wikner C., Qi J.H., Wernstedt C., Wu J.,Bruheim S., Mugishima H., Mukhopadhyay D., Spurkland A.,Claesson-Welsh L.;
EMBO J. 24:2342-2353(2005).
Cited for: FUNCTION IN CELL MIGRATION; PHOSPHORYLATION OF PLCG1; ACTIVATION OFMAPK1/ERK2; MAPK3/ERK1 AND THE MAP KINASES AND IN REGULATION OF ACTINCYTOSKELETON REORGANIZATION, INTERACTION WITH SH2D2A/TSAD,PHOSPHORYLATION AT TYR-951; TYR-1054; TYR-1059; TYR-1214; TYR-1305;TYR-1309 AND TYR-1319, AND MUTAGENESIS OF TYR-951.
"Vascular endothelial growth factor (VEGF)-D and VEGF-A differentiallyregulate KDR-mediated signaling and biological function in vascularendothelial cells.";
Jia H., Bagherzadeh A., Bicknell R., Duchen M.R., Liu D., Zachary I.;
J. Biol. Chem. 279:36148-36157(2004).
Cited for: INTERACTION WITH VEGFA AND VEGFD, PHOSPHORYLATION AT TYR-1054 ANDTYR-1059, FUNCTION IN VEGFA AND VEGFD SIGNALING; ACTIVATION OFMAPK1/ERK2 AND MAPK3/ERK1; ACTIVATION OF AKT1; PHOSPHORYLATION OFPLCG1 AND NOS3; MODULATION OF INTRACELLULAR CA(2+) LEVELS; CELLSURVIVAL AND POSITIVE REGULATION OF CELL PROLIFERATION; CELL MIGRATIONAND ANGIOGENESIS, AND ENZYME REGULATION.
"A single autophosphorylation site on KDR/Flk-1 is essential for VEGF-A-dependent activation of PLC-gamma and DNA synthesis in vascularendothelial cells.";
Takahashi T., Yamaguchi S., Chida K., Shibuya M.;
EMBO J. 20:2768-2778(2001).
Cited for: FUNCTION IN ENDOTHELIAL CELL PROLIFERATION; PHOSPHORYLATION OF PLCG1AND ACTIVIATION OF MAP KINASES, PHOSPHORYLATION AT TYR-1175 ANDTYR-1214, AND MUTAGENESIS OF LYS-868 AND TYR-1175.
"Autophosphorylation of KDR in the kinase domain is required formaximal VEGF-stimulated kinase activity and receptorinternalization.";
Dougher M., Terman B.I.;
Oncogene 18:1619-1627(1999).
Cited for: FUNCTION IN PHOSPHORYLATION OF PLCG1 AND PTK2/FAK1, INTERACTION WITHVEGFA, CATALYTIC ACTIVITY, PHOSPHORYLATION AT TYR-996; TYR-1054 ANDTYR-1059, MUTAGENESIS OF TYR-996; TYR-1054 AND TYR-1059, SUBCELLULARLOCATION, AND ENZYME REGULATION.
"Vascular endothelial growth factor receptor KDR tyrosine kinaseactivity is increased by autophosphorylation of two activation looptyrosine residues.";
Kendall R.L., Rutledge R.Z., Mao X., Tebben A.J., Hungate R.W.,Thomas K.A.;
J. Biol. Chem. 274:6453-6460(1999).
Cited for: CATALYTIC ACTIVITY, CHARACTERIZATION OF VARIANT GLU-848,PHOSPHORYLATION AT TYR-1054 AND TYR-1059, AND ENZYME REGULATION.

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