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Protein

Vascular endothelial growth factor receptor 2

Gene

Kdr

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.8 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation1 Publication

Enzyme regulationi

Present in an inactive conformation in the absence of bound ligand. Binding of VEGFA, VEGFC or VEGFD leads to dimerization and activation by autophosphorylation on tyrosine residues. May be regulated by hydrogen sulfide (H2S) levels via a sensitive intracellular disulfide bond (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei866 – 8661ATPPROSITE-ProRule annotation
Active sitei1026 – 10261Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi838 – 8469ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • blood vessel endothelial cell differentiation Source: DFLAT
  • branching morphogenesis of an epithelial tube Source: MGI
  • calcium ion homeostasis Source: MGI
  • calcium-mediated signaling using intracellular calcium source Source: UniProtKB
  • cell fate commitment Source: MGI
  • cell maturation Source: MGI
  • cell migration Source: MGI
  • cell migration involved in sprouting angiogenesis Source: BHF-UCL
  • cellular response to vascular endothelial growth factor stimulus Source: UniProtKB
  • embryonic hemopoiesis Source: UniProtKB
  • endocardium development Source: UniProtKB
  • endothelial cell differentiation Source: DFLAT
  • endothelium development Source: UniProtKB
  • hemopoiesis Source: MGI
  • lung alveolus development Source: MGI
  • lung development Source: MGI
  • lymph vessel development Source: MGI
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of endothelial cell apoptotic process Source: UniProtKB
  • ovarian follicle development Source: MGI
  • peptidyl-tyrosine autophosphorylation Source: BHF-UCL
  • peptidyl-tyrosine phosphorylation Source: UniProtKB
  • positive regulation of angiogenesis Source: DFLAT
  • positive regulation of BMP signaling pathway Source: DFLAT
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway Source: MGI
  • positive regulation of endothelial cell migration Source: DFLAT
  • positive regulation of endothelial cell proliferation Source: UniProtKB
  • positive regulation of epithelial cell proliferation Source: MGI
  • positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • positive regulation of focal adhesion assembly Source: MGI
  • positive regulation of macroautophagy Source: MGI
  • positive regulation of MAPK cascade Source: UniProtKB
  • positive regulation of mesenchymal cell proliferation Source: MGI
  • positive regulation of mitochondrial depolarization Source: MGI
  • positive regulation of mitochondrial fission Source: MGI
  • positive regulation of nitric-oxide synthase biosynthetic process Source: UniProtKB
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
  • positive regulation of positive chemotaxis Source: MGI
  • positive regulation of protein phosphorylation Source: UniProtKB
  • positive regulation of vascular endothelial growth factor receptor signaling pathway Source: DFLAT
  • positive regulation of vasculogenesis Source: UniProtKB
  • post-embryonic camera-type eye morphogenesis Source: MGI
  • protein autophosphorylation Source: UniProtKB
  • regulation of bone development Source: MGI
  • regulation of cell shape Source: MGI
  • regulation of endothelial cell differentiation Source: MGI
  • regulation of endothelial cell proliferation Source: DFLAT
  • regulation of hematopoietic progenitor cell differentiation Source: MGI
  • surfactant homeostasis Source: MGI
  • vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
  • vasculogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Angiogenesis, Differentiation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.
ReactomeiR-MMU-4420097. VEGFA-VEGFR2 Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Vascular endothelial growth factor receptor 2 (EC:2.7.10.1)
Short name:
VEGFR-2
Alternative name(s):
Fetal liver kinase 1
Short name:
FLK-1
Kinase NYK
Protein-tyrosine kinase receptor flk-1
CD_antigen: CD309
Gene namesi
Name:Kdr
Synonyms:Flk-1, Flk1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:96683. Kdr.

Subcellular locationi

Isoform 1 :
  • Cell membrane; Single-pass type I membrane protein
  • Cytoplasm By similarity
  • Nucleus By similarity
  • Cytoplasmic vesicle By similarity
  • Early endosome By similarity

  • Note: Detected on caveolae-enriched lipid rafts at the cell surface. Is recycled from the plasma membrane to endosomes and back again. Phosphorylation triggered by VEGFA binding promotes internalization and subsequent degradation. VEGFA binding triggers internalization and translocation to the nucleus (By similarity).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 762743ExtracellularSequence analysisAdd
BLAST
Transmembranei763 – 78321HelicalSequence analysisAdd
BLAST
Topological domaini784 – 1367584CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell junction Source: UniProtKB
  • cell periphery Source: MGI
  • cell surface Source: BHF-UCL
  • cytoplasm Source: MGI
  • cytoplasmic, membrane-bounded vesicle Source: UniProtKB-SubCell
  • early endosome Source: BHF-UCL
  • endoplasmic reticulum Source: UniProtKB
  • endosome Source: MGI
  • external side of plasma membrane Source: MGI
  • extracellular region Source: UniProtKB-SubCell
  • Golgi apparatus Source: MGI
  • integral component of plasma membrane Source: UniProtKB
  • membrane raft Source: MGI
  • nucleus Source: MGI
  • plasma membrane Source: BHF-UCL
  • sorting endosome Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Membrane, Nucleus, Secreted

Pathology & Biotechi

Disruption phenotypei

Embryonic lethality at 8.5 to 9.5 dpc, due to early defects in the development of hematopoietic and endothelial cells, leading to defects in vasculogenesis and endocardium development. At 7.5 dpc, there are no blood islands in the yolk sac. Organized blood vessels are absent in the yolk sac and in the embryo.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi866 – 8661K → R: Loss of enzyme activity. Abolishes ubiquitination in response to VEGFA binding. 1 Publication
Mutagenesisi1173 – 11731Y → F: Loss of interaction with SHB. 1 Publication
Mutagenesisi1188 – 11881S → A: Strongly reduces internalization and down-regulation of the activated receptor; when associated with A-1191. 1 Publication
Mutagenesisi1191 – 11911S → A: Strongly reduces internalization and down-regulation of the activated receptor; when associated with A-1188. 1 Publication
Mutagenesisi1212 – 12121Y → F: Strongly reduced autophosphorylation. 1 Publication

Chemistry

ChEMBLiCHEMBL3337.
GuidetoPHARMACOLOGYi1813.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 13671348Vascular endothelial growth factor receptor 2PRO_0000016772Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi46 – 461N-linked (GlcNAc...)Sequence analysis
Disulfide bondi53 ↔ 105PROSITE-ProRule annotation
Glycosylationi98 – 981N-linked (GlcNAc...)Sequence analysis
Glycosylationi145 – 1451N-linked (GlcNAc...)Sequence analysis
Disulfide bondi152 ↔ 202PROSITE-ProRule annotation
Glycosylationi160 – 1601N-linked (GlcNAc...)Sequence analysis
Glycosylationi247 – 2471N-linked (GlcNAc...)Sequence analysis
Disulfide bondi248 ↔ 309PROSITE-ProRule annotation
Glycosylationi320 – 3201N-linked (GlcNAc...)Sequence analysis
Glycosylationi376 – 3761N-linked (GlcNAc...)Sequence analysis
Glycosylationi397 – 3971N-linked (GlcNAc...)Sequence analysis
Disulfide bondi447 ↔ 528PROSITE-ProRule annotation
Glycosylationi509 – 5091N-linked (GlcNAc...)Sequence analysis
Glycosylationi521 – 5211N-linked (GlcNAc...)Sequence analysis
Disulfide bondi569 ↔ 640PROSITE-ProRule annotation
Glycosylationi578 – 5781N-linked (GlcNAc...)Sequence analysis
Glycosylationi611 – 6111N-linked (GlcNAc...)Sequence analysis
Glycosylationi617 – 6171N-linked (GlcNAc...)Sequence analysis
Glycosylationi629 – 6291N-linked (GlcNAc...)Sequence analysis
Glycosylationi673 – 6731N-linked (GlcNAc...)Sequence analysis
Disulfide bondi686 ↔ 735PROSITE-ProRule annotation
Glycosylationi702 – 7021N-linked (GlcNAc...)Sequence analysis
Glycosylationi719 – 7191N-linked (GlcNAc...)Sequence analysis
Modified residuei799 – 7991PhosphotyrosineBy similarity
Modified residuei949 – 9491Phosphotyrosine; by autocatalysisBy similarity
Modified residuei980 – 9801PhosphoserineBy similarity
Modified residuei982 – 9821PhosphoserineBy similarity
Modified residuei994 – 9941Phosphotyrosine; by autocatalysisBy similarity
Disulfide bondi1022 ↔ 1043Redox-activePROSITE-ProRule annotation
Modified residuei1052 – 10521Phosphotyrosine; by autocatalysis1 Publication
Modified residuei1057 – 10571Phosphotyrosine; by autocatalysis1 Publication
Modified residuei1173 – 11731Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1212 – 12121Phosphotyrosine; by autocatalysis1 Publication
Modified residuei1229 – 12291PhosphoserineCombined sources
Modified residuei1233 – 12331PhosphoserineCombined sources
Modified residuei1236 – 12361PhosphothreonineCombined sources
Modified residuei1303 – 13031Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1307 – 13071Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1317 – 13171Phosphotyrosine; by autocatalysisBy similarity

Post-translational modificationi

N-glycosylated.By similarity
Ubiquitinated. Tyrosine phosphorylation of the receptor promotes its poly-ubiquitination, leading to its degradation via the proteasome or lysosomal proteases (By similarity).By similarity
Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-949 is important for interaction with SH2D2A/TSAD and VEGFA-mediated reorganization of the actin cytoskeleton. Phosphorylation at Tyr-1173 is important for interaction with PLCG1 and SHB. Phosphorylation at Tyr-1212 is important for interaction with NCK1 and FYN. Dephosphorylated by PTPRJ at Tyr-799, Tyr-949, Tyr-994, Tyr-1052, Tyr-1057, Tyr-1173 and Tyr-1212 (By similarity).By similarity
The inhibitory disulfide bond between Cys-1022 and Cys-1043 may serve as a specific molecular switch for H2S-induced modification that regulates VEGFR2 function.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP35918.
PaxDbiP35918.
PRIDEiP35918.

PTM databases

iPTMnetiP35918.
PhosphoSiteiP35918.

Expressioni

Tissue specificityi

Expressed in endothelial cells (at protein level). Detected in embryonic endothelial cells, as well as hematopoietic stem and progenitor cells. Detected in vascular endothelium. Expressed at high levels in adult heart, lung, kidney, brain and skeletal muscle, but is also expressed at lower levels in most other adult tissues.4 Publications

Developmental stagei

Expressed in endothelial cells of allantois/umbilical vessels at 8.5 dpc (at protein level). Increases moderately during pregnancy (maximum 2.7-fold at 19 days), and increases further during lactation (maximum 3.7-fold increase on day 7).2 Publications

Gene expression databases

CleanExiMM_KDR.

Interactioni

Subunit structurei

Homodimer in the presence of bound dimeric VEGFA, VEGFC or VEGFD ligands; monomeric in the absence of bound ligands. Can also form heterodimers with FLT1/VEGFR1 and FLT4/VEGFR2. Interacts (tyrosine phosphorylated) with LFYN, NCK1, PLCG1. Interacts (tyrosine-phosphorylated active form preferentially) with DAB2IP (via C2 domain and active form preferentially); the interaction occurs at the late phase of VEGFA response and inhibits KDR/VEGFR2 activity. Interacts with SHBSH2D2A/TSAD, GRB2, MYOF, CBL and PDCD6 (PubMed:12796773, PubMed:12881528, PubMed:15026417, PubMed:15673613, PubMed:17702744, PubMed:19668192, PubMed:7681362, PubMed:8356051). Interacts (via C-terminus domain) with ERN1 (via kinase domain); the interaction is facilitated in a XBP1 isoform 1- and vascular endothelial growth factor (VEGF)-dependent manner in endothelial cells (By similarity).By similarity8 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei1173 – 11731Interaction with SHB

Binary interactionsi

WithEntry#Exp.IntActNotes
Flt4P359172EBI-1555005,EBI-7845747
METP085813EBI-1555005,EBI-1039152From a different organism.
MetP160563EBI-1555005,EBI-1798780

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-215N.
IntActiP35918. 8 interactions.
MINTiMINT-4996697.
STRINGi10090.ENSMUSP00000109144.

Chemistry

BindingDBiP35918.

Structurei

3D structure databases

ProteinModelPortaliP35918.
SMRiP35918. Positions 124-327, 665-754, 757-793, 810-1166.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 11166Ig-like C2-type 1Add
BLAST
Domaini143 – 20967Ig-like C2-type 2Add
BLAST
Domaini226 – 325100Ig-like C2-type 3Add
BLAST
Domaini330 – 41687Ig-like C2-type 4Add
BLAST
Domaini423 – 542120Ig-like C2-type 5Add
BLAST
Domaini549 – 656108Ig-like C2-type 6Add
BLAST
Domaini665 – 75187Ig-like C2-type 7Add
BLAST
Domaini832 – 1160329Protein kinasePROSITE-ProRule annotationAdd
BLAST

Domaini

The second and third Ig-like C2-type (immunoglobulin-like) domains are sufficient for VEGFC binding.By similarity

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0200. Eukaryota.
COG0515. LUCA.
HOGENOMiHOG000037949.
HOVERGENiHBG053432.
InParanoidiP35918.
PhylomeDBiP35918.

Family and domain databases

Gene3Di2.60.40.10. 7 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR001824. Tyr_kinase_rcpt_3_CS.
IPR009136. VEGFR2_rcpt.
[Graphical view]
PANTHERiPTHR24416:SF45. PTHR24416:SF45. 3 hits.
PfamiPF07679. I-set. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR01834. VEGFRECEPTR2.
SMARTiSM00409. IG. 7 hits.
SM00408. IGc2. 4 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 8 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS50835. IG_LIKE. 5 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P35918-1) [UniParc]FASTAAdd to basket
Also known as: mbVegfr-2

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MESKALLAVA LWFCVETRAA SVGLPGDFLH PPKLSTQKDI LTILANTTLQ
60 70 80 90 100
ITCRGQRDLD WLWPNAQRDS EERVLVTECG GGDSIFCKTL TIPRVVGNDT
110 120 130 140 150
GAYKCSYRDV DIASTVYVYV RDYRSPFIAS VSDQHGIVYI TENKNKTVVI
160 170 180 190 200
PCRGSISNLN VSLCARYPEK RFVPDGNRIS WDSEIGFTLP SYMISYAGMV
210 220 230 240 250
FCEAKINDET YQSIMYIVVV VGYRIYDVIL SPPHEIELSA GEKLVLNCTA
260 270 280 290 300
RTELNVGLDF TWHSPPSKSH HKKIVNRDVK PFPGTVAKMF LSTLTIESVT
310 320 330 340 350
KSDQGEYTCV ASSGRMIKRN RTFVRVHTKP FIAFGSGMKS LVEATVGSQV
360 370 380 390 400
RIPVKYLSYP APDIKWYRNG RPIESNYTMI VGDELTIMEV TERDAGNYTV
410 420 430 440 450
ILTNPISMEK QSHMVSLVVN VPPQIGEKAL ISPMDSYQYG TMQTLTCTVY
460 470 480 490 500
ANPPLHHIQW YWQLEEACSY RPGQTSPYAC KEWRHVEDFQ GGNKIEVTKN
510 520 530 540 550
QYALIEGKNK TVSTLVIQAA NVSALYKCEA INKAGRGERV ISFHVIRGPE
560 570 580 590 600
ITVQPAAQPT EQESVSLLCT ADRNTFENLT WYKLGSQATS VHMGESLTPV
610 620 630 640 650
CKNLDALWKL NGTMFSNSTN DILIVAFQNA SLQDQGDYVC SAQDKKTKKR
660 670 680 690 700
HCLVKQLIIL ERMAPMITGN LENQTTTIGE TIEVTCPASG NPTPHITWFK
710 720 730 740 750
DNETLVEDSG IVLRDGNRNL TIRRVRKEDG GLYTCQACNV LGCARAETLF
760 770 780 790 800
IIEGAQEKTN LEVIILVGTA VIAMFFWLLL VILVRTVKRA NEGELKTGYL
810 820 830 840 850
SIVMDPDELP LDERCERLPY DASKWEFPRD RLKLGKPLGR GAFGQVIEAD
860 870 880 890 900
AFGIDKTATC KTVAVKMLKE GATHSEHRAL MSELKILIHI GHHLNVVNLL
910 920 930 940 950
GACTKPGGPL MVIVEFSKFG NLSTYLRGKR NEFVPYKSKG ARFRQGKDYV
960 970 980 990 1000
GELSVDLKRR LDSITSSQSS ASSGFVEEKS LSDVEEEEAS EELYKDFLTL
1010 1020 1030 1040 1050
EHLICYSFQV AKGMEFLASR KCIHRDLAAR NILLSEKNVV KICDFGLARD
1060 1070 1080 1090 1100
IYKDPDYVRK GDARLPLKWM APETIFDRVY TIQSDVWSFG VLLWEIFSLG
1110 1120 1130 1140 1150
ASPYPGVKID EEFCRRLKEG TRMRAPDYTT PEMYQTMLDC WHEDPNQRPS
1160 1170 1180 1190 1200
FSELVEHLGN LLQANAQQDG KDYIVLPMSE TLSMEEDSGL SLPTSPVSCM
1210 1220 1230 1240 1250
EEEEVCDPKF HYDNTAGISH YLQNSKRKSR PVSVKTFEDI PLEEPEVKVI
1260 1270 1280 1290 1300
PDDSQTDSGM VLASEELKTL EDRNKLSPSF GGMMPSKSRE SVASEGSNQT
1310 1320 1330 1340 1350
SGYQSGYHSD DTDTTVYSSD EAGLLKMVDA AVHADSGTTL QLTSCLNGSG
1360
PVPAPPPTPG NHERGAA
Length:1,367
Mass (Da):152,517
Last modified:June 1, 1994 - v1
Checksum:iEFC99704F1DCA266
GO
Isoform 2 (identifier: P35918-2) [UniParc]FASTAAdd to basket
Also known as: sVegfr-2

The sequence of this isoform differs from the canonical sequence as follows:
     661-673: ERMAPMITGNLEN → GMEASLGDRIAMP
     674-1367: Missing.

Show »
Length:673
Mass (Da):75,230
Checksum:iCCEFE9DA9B53B300
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251P → T in CAA50192 (PubMed:7681362).Curated
Sequence conflicti679 – 6791G → D in AAB25043 (PubMed:8423988).Curated
Sequence conflicti783 – 7842LV → VL in CAA50192 (PubMed:7681362).Curated
Sequence conflicti917 – 9171S → C in CAA50192 (PubMed:7681362).Curated
Sequence conflicti1341 – 136727QLTSC…ERGAA → RSPPV in AAB25043 (PubMed:8423988).CuratedAdd
BLAST

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei661 – 67313ERMAP…GNLEN → GMEASLGDRIAMP in isoform 2. 1 PublicationVSP_041986Add
BLAST
Alternative sequencei674 – 1367694Missing in isoform 2. 1 PublicationVSP_041987Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70842 mRNA. Translation: CAA50192.1.
X59397 mRNA. Translation: CAA42040.1.
S53103 mRNA. Translation: AAB25043.1.
EU884114 mRNA. Translation: ACJ66293.1.
X89777 Genomic DNA. Translation: CAA61917.1.
PIRiA41228.
UniGeneiMm.285.

Genome annotation databases

UCSCiuc012dxk.2. mouse. [P35918-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70842 mRNA. Translation: CAA50192.1.
X59397 mRNA. Translation: CAA42040.1.
S53103 mRNA. Translation: AAB25043.1.
EU884114 mRNA. Translation: ACJ66293.1.
X89777 Genomic DNA. Translation: CAA61917.1.
PIRiA41228.
UniGeneiMm.285.

3D structure databases

ProteinModelPortaliP35918.
SMRiP35918. Positions 124-327, 665-754, 757-793, 810-1166.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-215N.
IntActiP35918. 8 interactions.
MINTiMINT-4996697.
STRINGi10090.ENSMUSP00000109144.

Chemistry

BindingDBiP35918.
ChEMBLiCHEMBL3337.
GuidetoPHARMACOLOGYi1813.

PTM databases

iPTMnetiP35918.
PhosphoSiteiP35918.

Proteomic databases

MaxQBiP35918.
PaxDbiP35918.
PRIDEiP35918.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiuc012dxk.2. mouse. [P35918-2]

Organism-specific databases

MGIiMGI:96683. Kdr.

Phylogenomic databases

eggNOGiKOG0200. Eukaryota.
COG0515. LUCA.
HOGENOMiHOG000037949.
HOVERGENiHBG053432.
InParanoidiP35918.
PhylomeDBiP35918.

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.
ReactomeiR-MMU-4420097. VEGFA-VEGFR2 Pathway.

Miscellaneous databases

ChiTaRSiKdr. mouse.
PROiP35918.
SOURCEiSearch...

Gene expression databases

CleanExiMM_KDR.

Family and domain databases

Gene3Di2.60.40.10. 7 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR001824. Tyr_kinase_rcpt_3_CS.
IPR009136. VEGFR2_rcpt.
[Graphical view]
PANTHERiPTHR24416:SF45. PTHR24416:SF45. 3 hits.
PfamiPF07679. I-set. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR01834. VEGFRECEPTR2.
SMARTiSM00409. IG. 7 hits.
SM00408. IGc2. 4 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 8 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS50835. IG_LIKE. 5 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiVGFR2_MOUSE
AccessioniPrimary (citable) accession number: P35918
Secondary accession number(s): C5H7S5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: September 7, 2016
This is version 169 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.