P35918

※ Protein Information

Tag	Content
UniProt Accession	VGFR2_MOUSE; P35918;
Entrez ID	16542
GenBank Protein ID
GenBank Nucleotide ID
Protein Name	Vascular endothelial growth factor receptor 2 (VEGFR-2) (EC 2.7.10.1) (Fetal liver kinase 1) (FLK-1) (Kinase NYK) (Protein-tyrosine kinase receptor flk-1) (CD antigen CD309)
Gene Name	Kdr; Flk-1; Flk1
Organism	Mus musculus
NCBI Taxa ID	10090
Functional 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, may function as decoy receptors for VEGFA, VEGFC and/or VEGFD. Isoform 2 plays an important role as a negative regulator of VEGFA- (view all) Functional 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, may function as decoy receptors for VEGFA, VEGFC and/or VEGFD. Isoform 2 plays an important role as a negative regulator of VEGFA- and VEGFC-mediated lymphangiogenesis by limiting the amount of free VEGFA and/or VEGFC and by 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.
Sequence (Fasta)	MESKALLAVA LWFCVETRAA SVGLPGDFLH PPKLSTQKDI LTILANTTLQ ITCRGQRDLD 60 WLWPNAQRDS EERVLVTECG GGDSIFCKTL TIPRVVGNDT GAYKCSYRDV DIASTVYVYV 120 RDYRSPFIAS VSDQHGIVYI TENKNKTVVI PCRGSISNLN VSLCARYPEK RFVPDGNRIS 180 WDSEIGFTLP SYMISYAGMV FCEAKINDET YQSIMYIVVV VGYRIYDVIL SPPHEIELSA 240 GEKLVLNCTA RTELNVGLDF TWHSPPSKSH HKKIVNRDVK PFPGTVAKMF LSTLTIESVT 300 KSDQGEYTCV ASSGRMIKRN RTFVRVHTKP FIAFGSGMKS LVEATVGSQV RIPVKYLSYP 360 APDIKWYRNG RPIESNYTMI VGDELTIMEV TERDAGNYTV ILTNPISMEK QSHMVSLVVN 420 VPPQIGEKAL ISPMDSYQYG TMQTLTCTVY ANPPLHHIQW YWQLEEACSY RPGQTSPYAC 480 KEWRHVEDFQ GGNKIEVTKN QYALIEGKNK TVSTLVIQAA NVSALYKCEA INKAGRGERV 540 ISFHVIRGPE ITVQPAAQPT EQESVSLLCT ADRNTFENLT WYKLGSQATS VHMGESLTPV 600 CKNLDALWKL NGTMFSNSTN DILIVAFQNA SLQDQGDYVC SAQDKKTKKR HCLVKQLIIL 660 ERMAPMITGN LENQTTTIGE TIEVTCPASG NPTPHITWFK DNETLVEDSG IVLRDGNRNL 720 TIRRVRKEDG GLYTCQACNV LGCARAETLF IIEGAQEKTN LEVIILVGTA VIAMFFWLLL 780 VILVRTVKRA NEGELKTGYL SIVMDPDELP LDERCERLPY DASKWEFPRD RLKLGKPLGR 840 GAFGQVIEAD AFGIDKTATC KTVAVKMLKE GATHSEHRAL MSELKILIHI GHHLNVVNLL 900 GACTKPGGPL MVIVEFSKFG NLSTYLRGKR NEFVPYKSKG ARFRQGKDYV GELSVDLKRR 960 LDSITSSQSS ASSGFVEEKS LSDVEEEEAS EELYKDFLTL EHLICYSFQV AKGMEFLASR 1020 KCIHRDLAAR NILLSEKNVV KICDFGLARD IYKDPDYVRK GDARLPLKWM APETIFDRVY 1080 TIQSDVWSFG VLLWEIFSLG ASPYPGVKID EEFCRRLKEG TRMRAPDYTT PEMYQTMLDC 1140 WHEDPNQRPS FSELVEHLGN LLQANAQQDG KDYIVLPMSE TLSMEEDSGL SLPTSPVSCM 1200 EEEEVCDPKF HYDNTAGISH YLQNSKRKSR PVSVKTFEDI PLEEPEVKVI PDDSQTDSGM 1260 VLASEELKTL EDRNKLSPSF GGMMPSKSRE SVASEGSNQT SGYQSGYHSD DTDTTVYSSD 1320 EAGLLKMVDA AVHADSGTTL QLTSCLNGSG PVPAPPPTPG NHERGAA 1368 Fasta Sequence >P35918\|Kdr; Flk-1; Flk1\|Mus musculus (Mouse) MESKALLAVALWFCVETRAASVGLPGDFLHPPKLSTQKDILTILANTTLQITCRGQRDLDWLWPNAQRDSEERVLVTECGGGDSIFCKTLTIPRVVGNDTGAYKCSYRDVDIASTVYVYVRDYRSPFIASVSDQHGIVYITENKNKTVVIPCRGSISNLNVSLCARYPEKRFVPDGNRISWDSEIGFTLPSYMISYAGMVFCEAKINDETYQSIMYIVVVVGYRIYDVILSPPHEIELSAGEKLVLNCTARTELNVGLDFTWHSPPSKSHHKKIVNRDVKPFPGTVAKMFLSTLTIESVTKSDQGEYTCVASSGRMIKRNRTFVRVHTKPFIAFGSGMKSLVEATVGSQVRIPVKYLSYPAPDIKWYRNGRPIESNYTMIVGDELTIMEVTERDAGNYTVILTNPISMEKQSHMVSLVVNVPPQIGEKALISPMDSYQYGTMQTLTCTVYANPPLHHIQWYWQLEEACSYRPGQTSPYACKEWRHVEDFQGGNKIEVTKNQYALIEGKNKTVSTLVIQAANVSALYKCEAINKAGRGERVISFHVIRGPEITVQPAAQPTEQESVSLLCTADRNTFENLTWYKLGSQATSVHMGESLTPVCKNLDALWKLNGTMFSNSTNDILIVAFQNASLQDQGDYVCSAQDKKTKKRHCLVKQLIILERMAPMITGNLENQTTTIGETIEVTCPASGNPTPHITWFKDNETLVEDSGIVLRDGNRNLTIRRVRKEDGGLYTCQACNVLGCARAETLFIIEGAQEKTNLEVIILVGTAVIAMFFWLLLVILVRTVKRANEGELKTGYLSIVMDPDELPLDERCERLPYDASKWEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATCKTVAVKMLKEGATHSEHRALMSELKILIHIGHHLNVVNLLGACTKPGGPLMVIVEFSKFGNLSTYLRGKRNEFVPYKSKGARFRQGKDYVGELSVDLKRRLDSITSSQSSASSGFVEEKSLSDVEEEEASEELYKDFLTLEHLICYSFQVAKGMEFLASRKCIHRDLAARNILLSEKNVVKICDFGLARDIYKDPDYVRKGDARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKIDEEFCRRLKEGTRMRAPDYTTPEMYQTMLDCWHEDPNQRPSFSELVEHLGNLLQANAQQDGKDYIVLPMSETLSMEEDSGLSLPTSPVSCMEEEEVCDPKFHYDNTAGISHYLQNSKRKSRPVSVKTFEDIPLEEPEVKVIPDDSQTDSGMVLASEELKTLEDRNKLSPSFGGMMPSKSRESVASEGSNQTSGYQSGYHSDDTDTTVYSSDEAGLLKMVDAAVHADSGTTLQLTSCLNGSGPVPAPPPTPGNHERGAA

※ PTM-Disease Association

Num	PTM	Disease	Type	PTM Site	PMID
1	Arginine Methylation	cancer and age-related macular degeneration	P	R817	24300896
1	[Reference]: we report a previously unknown mechanism by which the activation of VEGFR-2, a potent angiogenic RTK, is controlled by the methylation of Lys1041. Methylation of Lys1041?is important for phosphorylation of VEGFR-2, and interfering with its methylation by site-directed mutagenesis and chemical inhibitors blocks the ability of VEGFR-2 to stimulate angiogenesis and tumor growth.
2	Lysine Methylation	cancer and age-related macular degeneration	P	K856	24300896
2	[Reference]: we report a previously unknown mechanism by which the activation of VEGFR-2, a potent angiogenic RTK, is controlled by the methylation of Lys1041. Methylation of Lys1041?is important for phosphorylation of VEGFR-2, and interfering with its methylation by site-directed mutagenesis and chemical inhibitors blocks the ability of VEGFR-2 to stimulate angiogenesis and tumor growth.
3	Lysine Methylation	cancer and age-related macular degeneration	P	K861	24300896
3	[Reference]: we report a previously unknown mechanism by which the activation of VEGFR-2, a potent angiogenic RTK, is controlled by the methylation of Lys1041. Methylation of Lys1041?is important for phosphorylation of VEGFR-2, and interfering with its methylation by site-directed mutagenesis and chemical inhibitors blocks the ability of VEGFR-2 to stimulate angiogenesis and tumor growth.
4	Lysine Methylation	cancer and age-related macular degeneration	P	K1041	24300896
4	[Reference]: we report a previously unknown mechanism by which the activation of VEGFR-2, a potent angiogenic RTK, is controlled by the methylation of Lys1041. Methylation of Lys1041?is important for phosphorylation of VEGFR-2, and interfering with its methylation by site-directed mutagenesis and chemical inhibitors blocks the ability of VEGFR-2 to stimulate angiogenesis and tumor growth.
5	Arginine Methylation	cancer and age-related macular degeneration	P	R1115	24300896
5	[Reference]: we report a previously unknown mechanism by which the activation of VEGFR-2, a potent angiogenic RTK, is controlled by the methylation of Lys1041. Methylation of Lys1041?is important for phosphorylation of VEGFR-2, and interfering with its methylation by site-directed mutagenesis and chemical inhibitors blocks the ability of VEGFR-2 to stimulate angiogenesis and tumor growth.

※ Disease Cross-ref Annotation

Database	Annotation
CTD (Curated) (count: 18) (view all)	MESH:D000230 ; Adenocarcinoma MESH:D001943 ; Breast Neoplasms MESH:D002543 ; Cerebral Hemorrhage MESH:D015179 ; Colorectal Neoplasms MESH:D003928 ; Diabetic Nephropathies MESH:D004833 ; Epilepsy, Temporal Lobe MESH:D004938 ; Esophageal Neoplasms MESH:C535860 ; Hemangioma, capillary infantile MESH:D006394 ; Hemangiosarcoma MESH:D008114 ; Liver Neoplasms, Experimental MESH:D017202 ; Myocardial Ischemia MESH:D009389 ; Neovascularization, Pathologic MESH:D010009 ; Osteochondrodysplasias MESH:D010190 ; Pancreatic Neoplasms MESH:D015427 ; Reperfusion Injury MESH:D012559 ; Schizophrenia MESH:D014511 ; Uremia MESH:D020246 ; Venous Thrombosis

Database

Annotation

CTD (Curated)
(count: 18)
(view all)

MESH:D000230 ; Adenocarcinoma
MESH:D001943 ; Breast Neoplasms
MESH:D002543 ; Cerebral Hemorrhage
MESH:D015179 ; Colorectal Neoplasms
MESH:D003928 ; Diabetic Nephropathies
MESH:D004833 ; Epilepsy, Temporal Lobe

※ PTM Sites

PTM	Modification Sites
Phosphorylation (count: 20) (view all)	1006 TLEHLICYSFQVAKG dbPAF 1052 FGLARDIYKDPDYVR dbPAF 1057 DIYKDPDYVRKGDAR dbPAF 1173 AQQDGKDYIVLPMSE dbPAF 1188 TLSMEEDSGLSLPTS dbPAF 1191 MEEDSGLSLPTSPVS dbPAF 1212 VCDPKFHYDNTAGIS dbPAF 1229 LQNSKRKSRPVSVKT dbPAF 1233 KRKSRPVSVKTFEDI dbPAF 1236 SRPVSVKTFEDIPLE dbPAF 188 WDSEIGFTLPSYMIS dbPAF 192 IGFTLPSYMISYAGM dbPAF 358 RIPVKYLSYPAPDIK dbPAF 359 IPVKYLSYPAPDIKW dbPAF 616 KLNGTMFSNSTNDIL dbPAF 618 NGTMFSNSTNDILIV dbPAF 619 GTMFSNSTNDILIVA dbPAF 949 RFRQGKDYVGELSVD dbPAF 973 SSQSSASSGFVEEKS dbPAF 994 EEASEELYKDFLTLE dbPAF
Ubiquitination (count: 8) (view all)	1037 RNILLSEKNVVKICD PLMD 1287 FGGMMPSKSRESVAS PLMD 796 RANEGELKTGYLSIV PLMD 824 RLPYDASKWEFPRDR PLMD 856 ADAFGIDKTATCKTV PLMD 861 IDKTATCKTVAVKML PLMD 947 GARFRQGKDYVGELS PLMD 958 GELSVDLKRRLDSIT PLMD

PTM

Modification Sites

Phosphorylation
(count: 20)
(view all)

1006      TLEHLICYSFQVAKG     dbPAF
1052      FGLARDIYKDPDYVR     dbPAF
1057      DIYKDPDYVRKGDAR     dbPAF
1173      AQQDGKDYIVLPMSE     dbPAF
1188      TLSMEEDSGLSLPTS     dbPAF
1191      MEEDSGLSLPTSPVS     dbPAF

Ubiquitination
(count: 8)
(view all)

1037      RNILLSEKNVVKICD     PLMD
1287      FGGMMPSKSRESVAS     PLMD
796       RANEGELKTGYLSIV     PLMD
824       RLPYDASKWEFPRDR     PLMD
856       ADAFGIDKTATCKTV     PLMD
861       IDKTATCKTVAVKML     PLMD

PTMD Annotation Information

※ Protein Information

Functional Description

Fasta Sequence

※ PTM-Disease Association

※ Disease Cross-ref Annotation

※ PTM Sites