UniProtKB - P17948 (VGFR1_HUMAN)
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- BLAST>sp|P17948|VGFR1_HUMAN Vascular endothelial growth factor receptor 1 OS=Homo sapiens OX=9606 GN=FLT1 PE=1 SV=2 MVSYWDTGVLLCALLSCLLLTGSSSGSKLKDPELSLKGTQHIMQAGQTLHLQCRGEAAHK WSLPEMVSKESERLSITKSACGRNGKQFCSTLTLNTAQANHTGFYSCKYLAVPTSKKKET ESAIYIFISDTGRPFVEMYSEIPEIIHMTEGRELVIPCRVTSPNITVTLKKFPLDTLIPD GKRIIWDSRKGFIISNATYKEIGLLTCEATVNGHLYKTNYLTHRQTNTIIDVQISTPRPV KLLRGHTLVLNCTATTPLNTRVQMTWSYPDEKNKRASVRRRIDQSNSHANIFYSVLTIDK MQNKDKGLYTCRVRSGPSFKSVNTSVHIYDKAFITVKHRKQQVLETVAGKRSYRLSMKVK AFPSPEVVWLKDGLPATEKSARYLTRGYSLIIKDVTEEDAGNYTILLSIKQSNVFKNLTA TLIVNVKPQIYEKAVSSFPDPALYPLGSRQILTCTAYGIPQPTIKWFWHPCNHNHSEARC DFCSNNEESFILDADSNMGNRIESITQRMAIIEGKNKMASTLVVADSRISGIYICIASNK VGTVGRNISFYITDVPNGFHVNLEKMPTEGEDLKLSCTVNKFLYRDVTWILLRTVNNRTM HYSISKQKMAITKEHSITLNLTIMNVSLQDSGTYACRARNVYTGEEILQKKEITIRDQEA PYLLRNLSDHTVAISSSTTLDCHANGVPEPQITWFKNNHKIQQEPGIILGPGSSTLFIER VTEEDEGVYHCKATNQKGSVESSAYLTVQGTSDKSNLELITLTCTCVAATLFWLLLTLFI RKMKRSSSEIKTDYLSIIMDPDEVPLDEQCERLPYDASKWEFARERLKLGKSLGRGAFGK VVQASAFGIKKSPTCRTVAVKMLKEGATASEYKALMTELKILTHIGHHLNVVNLLGACTK QGGPLMVIVEYCKYGNLSNYLKSKRDLFFLNKDAALHMEPKKEKMEPGLEQGKKPRLDSV TSSESFASSGFQEDKSLSDVEEEEDSDGFYKEPITMEDLISYSFQVARGMEFLSSRKCIH RDLAARNILLSENNVVKICDFGLARDIYKNPDYVRKGDTRLPLKWMAPESIFDKIYSTKS DVWSYGVLLWEIFSLGGSPYPGVQMDEDFCSRLREGMRMRAPEYSTPEIYQIMLDCWHRD PKERPRFAELVEKLGDLLQANVQQDGKDYIPINAILTGNSGFTYSTPAFSEDFFKESISA PKFNSGSSDDVRYVNAFKFMSLERIKTFEELLPNATSMFDDYQGDSSTLLASPMLKRFTW TDSKPKASLKIDLRVTSKSKESGLSDVSRPSFCHSSCGHVSEGKRRFTYDHAELERKIAC CSPPPDYNSVVLYSTPPI
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Vascular endothelial growth factor receptor 1
FLT1
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.2"Inhibition of vascular endothelial cell growth factor activity by an endogenously encoded soluble receptor."
Kendall R.L., Thomas K.A.
Proc. Natl. Acad. Sci. U.S.A. 90:10705-10709(1993) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF N-TERMINUS, SUBCELLULAR LOCATION (ISOFORM 2), INTERACTION WITH VEGFA, FUNCTION. - Ref.4"Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis."
Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D., Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.
Arthritis Res. Ther. 10:R73-R73(2008) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION IN LIGAND BINDING, SUBCELLULAR LOCATION. - Ref.5"A novel human-specific soluble vascular endothelial growth factor receptor 1: cell-type-specific splicing and implications to vascular endothelial growth factor homeostasis and preeclampsia."
Sela S., Itin A., Natanson-Yaron S., Greenfield C., Goldman-Wohl D., Yagel S., Keshet E.
Circ. Res. 102:1566-1574(2008) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ROLE IN PREECLAMPSIA, INDUCTION. - Ref.6"A novel intracellular isoform of VEGFR-1 activates Src and promotes cell invasion in MDA-MB-231 breast cancer cells."
Mezquita B., Mezquita J., Pau M., Mezquita C.
J. Cell. Biochem. 110:732-742(2010) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5; 6; 7 AND 8), ALTERNATIVE SPLICING, FUNCTION IN PHOSPHORYLATION OF SRC AND CANCER CELL INVASIVENESS, TISSUE SPECIFICITY. - Ref.15"A unique signal transduction from FLT tyrosine kinase, a receptor for vascular endothelial growth factor VEGF."
Seetharam L., Gotoh N., Maru Y., Neufeld G., Yamaguchi S., Shibuya M.
Oncogene 10:135-147(1995) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH VEGFA, AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY, FUNCTION IN PHOSPHORYLATION OF PLCG, ABSENCE OF MITOGENIC FUNCTION IN CULTURED FIBROBLASTS. - Ref.16"Migration of human monocytes in response to vascular endothelial growth factor (VEGF) is mediated via the VEGF receptor flt-1."
Barleon B., Sozzani S., Zhou D., Weich H.A., Mantovani A., Marme D.
Blood 87:3336-3343(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CELL MIGRATION, FUNCTION IN VEGFA AND PGF SIGNALING, INDUCTION. - Ref.17"The phosphorylated 1169-tyrosine containing region of flt-1 kinase (VEGFR-1) is a major binding site for PLCgamma."
Sawano A., Takahashi T., Yamaguchi S., Shibuya M.
Biochem. Biophys. Res. Commun. 238:487-491(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN PHOSPHORYLATION OF PLCG AND ACTIVATION OF MAP KINASES, INTERACTION WITH PLCG, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-861 AND TYR-1169, PHOSPHORYLATION AT TYR-1169 AND TYR-1213. - Ref.19"Vascular endothelial growth factor receptor-2-mediated mitogenesis is negatively regulated by vascular endothelial growth factor receptor-1 in tumor epithelial cells."
Dunk C., Ahmed A.
Am. J. Pathol. 158:265-273(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS NEGATIVE REGULATOR OF KDR-MEDIATED CELL PROLIFERATION. - Ref.21"Effect of placenta growth factor-1 on proliferation and release of nitric oxide, cyclic AMP and cyclic GMP in human epithelial cells expressing the FLT-1 receptor."
Angelucci C., Lama G., Iacopino F., Maglione D., Sica G.
Growth Factors 19:193-206(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN PGF-MEDIATED CHORIOCARCINOMA CELL PROLIFERATION. - Ref.22"Signaling properties of VEGF receptor-1 and -2 homo- and heterodimers."
Huang K., Andersson C., Roomans G.M., Ito N., Claesson-Welsh L.
Int. J. Biochem. Cell Biol. 33:315-324(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH KDR, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, FUNCTION IN VEGFA SIGNALING; PHOSPHORYLATION OF PLCG AND ACTIVATION OF PHOSPHATIDYLINOSITOL KINASE AND PHOSPHOLIPASE C. - Ref.23"Activation of vascular endothelial growth factor receptor-1 sustains angiogenesis and Bcl-2 expression via the phosphatidylinositol 3-kinase pathway in endothelial cells."
Cai J., Ahmad S., Jiang W.G., Huang J., Kontos C.D., Boulton M., Ahmed A.
Diabetes 52:2959-2968(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN SIGNALING VIA ACTIVATION OF THE PHOSPHATIDYLINOSITOL KINASE PATHWAY AND POSITIVE REGULATION OF ANGIOGENESIS IN RESPONSE TO PGF AND VEGFA. - Ref.24"Role of PlGF in the intra- and intermolecular cross talk between the VEGF receptors Flt1 and Flk1."
Autiero M., Waltenberger J., Communi D., Kranz A., Moons L., Lambrechts D., Kroll J., Plaisance S., De Mol M., Bono F., Kliche S., Fellbrich G., Ballmer-Hofer K., Maglione D., Mayr-Beyrle U., Dewerchin M., Dombrowski S., Stanimirovic D. , Van Hummelen P., Dehio C., Hicklin D.J., Persico G., Herbert J.M., Communi D., Shibuya M., Collen D., Conway E.M., Carmeliet P.
Nat. Med. 9:936-943(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PGF AND KDR, FUNCTION IN PHOSPHORYLATION OF KDR; VEGFA AND PGF SIGNALING, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT TYR-1213; TYR-1327 AND TYR-1309. - Ref.26"Expression and function of vascular endothelial growth factor receptor-1 on human colorectal cancer cells."
Fan F., Wey J.S., McCarty M.F., Belcheva A., Liu W., Bauer T.W., Somcio R.J., Wu Y., Hooper A., Hicklin D.J., Ellis L.M.
Oncogene 24:2647-2653(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN VEGFA AND VEGFB SIGNALING; CANCER CELL MIGRATION; INVASIVENESS AND ACTIVATION OF MAPK1/ERK2 AND MAPK3/ERK1. - Ref.27"Vascular endothelial growth factor receptor-1 mediates migration of human colorectal carcinoma cells by activation of Src family kinases."
Lesslie D.P., Summy J.M., Parikh N.U., Fan F., Trevino J.G., Sawyer T.K., Metcalf C.A., Shakespeare W.C., Hicklin D.J., Ellis L.M., Gallick G.E.
Br. J. Cancer 94:1710-1717(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CELL MIGRATION AND PHOSPHORYLATION OF PTK2/FAK1; YES1 AND SRC. - Ref.29"The molecular basis of VEGFR-1 signal transduction pathways in primary human monocytes."
Tchaikovski V., Fellbrich G., Waltenberger J.
Arterioscler. Thromb. Vasc. Biol. 28:322-328(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN PGF AND VEGFA SIGNALING; PHOSPHORYLATION OF AKT1; MAPK3/ERK1 AND MAP KINASES; CHEMOTAXIS AND ACTIVATION OF PHOSPHATIDYLINOSITOL 3-KINASE, AUTOPHOSPHORYLATION IN RESPONSE TO PGF AND VEGFA. - Ref.30"Vascular endothelial growth factor receptor-1 regulates postnatal angiogenesis through inhibition of the excessive activation of Akt."
Nishi J., Minamino T., Miyauchi H., Nojima A., Tateno K., Okada S., Orimo M., Moriya J., Fong G.H., Sunagawa K., Shibuya M., Komuro I.
Circ. Res. 103:261-268(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN ENDOTHELIAL CELL SURVIVAL AND ANGIOGENESIS. - Ref.31"Placental growth factor (PlGF) enhances breast cancer cell motility by mobilising ERK1/2 phosphorylation and cytoskeletal rearrangement."
Taylor A.P., Leon E., Goldenberg D.M.
Br. J. Cancer 103:82-89(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CANCER CELL MIGRATION AND ACTIVATION OF MAPK1/ERK2 AND/OR MAPK3/ERK1. - Ref.34"Autocrine activity of soluble Flt-1 controls endothelial cell function and angiogenesis."
Ahmad S., Hewett P.W., Al-Ani B., Sissaoui S., Fujisawa T., Cudmore M.J., Ahmed A.
Vasc. Cell 3:15-15(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS DECOY RECEPTORS; REGULATION OF VEGFA SIGNALING AND REGULATION OF KDR ACTIVITY (ISOFORMS 2/3/4), ROLE IN PREECLAMPSIA.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
5 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.14"Identification of vascular endothelial growth factor receptor-1 tyrosine phosphorylation sites and binding of SH2 domain-containing molecules."
Ito N., Wernstedt C., Engstrom U., Claesson-Welsh L.
J. Biol. Chem. 273:23410-23418(1998) [PubMed] [Europe PMC] [Abstract]Cited for: PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY, PHOSPHORYLATION AT TYR-914; TYR-1213; TYR-1242; TYR-1327 AND TYR-1333, MUTAGENESIS OF TYR-914; TYR-1213; TYR-1242; TYR-1327 AND TYR-1333, INTERACTION WITH PLCG; GRB2; CRK; NCK1 AND PTPN11. - Ref.15"A unique signal transduction from FLT tyrosine kinase, a receptor for vascular endothelial growth factor VEGF."
Seetharam L., Gotoh N., Maru Y., Neufeld G., Yamaguchi S., Shibuya M.
Oncogene 10:135-147(1995) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH VEGFA, AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY, FUNCTION IN PHOSPHORYLATION OF PLCG, ABSENCE OF MITOGENIC FUNCTION IN CULTURED FIBROBLASTS. - Ref.17"The phosphorylated 1169-tyrosine containing region of flt-1 kinase (VEGFR-1) is a major binding site for PLCgamma."
Sawano A., Takahashi T., Yamaguchi S., Shibuya M.
Biochem. Biophys. Res. Commun. 238:487-491(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN PHOSPHORYLATION OF PLCG AND ACTIVATION OF MAP KINASES, INTERACTION WITH PLCG, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-861 AND TYR-1169, PHOSPHORYLATION AT TYR-1169 AND TYR-1213. - Ref.22"Signaling properties of VEGF receptor-1 and -2 homo- and heterodimers."
Huang K., Andersson C., Roomans G.M., Ito N., Claesson-Welsh L.
Int. J. Biochem. Cell Biol. 33:315-324(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH KDR, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, FUNCTION IN VEGFA SIGNALING; PHOSPHORYLATION OF PLCG AND ACTIVATION OF PHOSPHATIDYLINOSITOL KINASE AND PHOSPHOLIPASE C. - Ref.24"Role of PlGF in the intra- and intermolecular cross talk between the VEGF receptors Flt1 and Flk1."
Autiero M., Waltenberger J., Communi D., Kranz A., Moons L., Lambrechts D., Kroll J., Plaisance S., De Mol M., Bono F., Kliche S., Fellbrich G., Ballmer-Hofer K., Maglione D., Mayr-Beyrle U., Dewerchin M., Dombrowski S., Stanimirovic D. , Van Hummelen P., Dehio C., Hicklin D.J., Persico G., Herbert J.M., Communi D., Shibuya M., Collen D., Conway E.M., Carmeliet P.
Nat. Med. 9:936-943(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PGF AND KDR, FUNCTION IN PHOSPHORYLATION OF KDR; VEGFA AND PGF SIGNALING, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT TYR-1213; TYR-1327 AND TYR-1309.
<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 861 | ATPPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | 1 | |
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 1022 | Proton acceptorPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | 1 |
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 833 – 841 | ATPPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | 9 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- growth factor binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- placental growth factor-activated receptor activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- transmembrane receptor protein tyrosine kinase activity Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- vascular endothelial growth factor-activated receptor activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- VEGF-A-activated receptor activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- VEGF-B-activated receptor activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- angiogenesis Source: UniProtKB-KW
- blood vessel morphogenesis Source: UniProtKB
- cell differentiation Source: UniProtKB-KW
- cell migration Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- cellular response to vascular endothelial growth factor stimulus Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- embryonic morphogenesis Source: UniProtKB
- monocyte chemotaxis Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- negative regulation of vascular endothelial cell proliferation Source: BHF-UCL <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactioni
- peptidyl-tyrosine phosphorylation Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of angiogenesis Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of cell migration Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of cell proliferation Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- positive regulation of MAPK cascade Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of MAP kinase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of phospholipase C activity Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein autophosphorylation Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- transmembrane receptor protein tyrosine kinase signaling pathway Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- vascular endothelial growth factor receptor-1 signaling pathway Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- vascular endothelial growth factor receptor signaling pathway Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase |
| Biological process | Angiogenesis, Chemotaxis, Differentiation |
| Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.7.10.1 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-194306 Neurophilin interactions with VEGF and VEGFR R-HSA-195399 VEGF binds to VEGFR leading to receptor dimerization |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | P17948 |
SIGNOR Signaling Network Open Resource More...SIGNORi | P17948 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Vascular endothelial growth factor receptor 1 (EC:2.7.10.1)Short name: VEGFR-1 Alternative name(s): Fms-like tyrosine kinase 1 Short name: FLT-1 Tyrosine-protein kinase FRT Tyrosine-protein kinase receptor FLT Short name: FLT Vascular permeability factor receptor |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:FLT1 Synonyms:FLT, FRT, VEGFR1 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000102755.10 |
Human Gene Nomenclature Database More...HGNCi | HGNC:3763 FLT1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 165070 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P17948 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Endosome
Plasma membrane
Note: Autophosphorylation promotes ubiquitination and endocytosis.
Extracellular region or secreted
- Secreted 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.2"Inhibition of vascular endothelial cell growth factor activity by an endogenously encoded soluble receptor."
Kendall R.L., Thomas K.A.
Proc. Natl. Acad. Sci. U.S.A. 90:10705-10709(1993) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF N-TERMINUS, SUBCELLULAR LOCATION (ISOFORM 2), INTERACTION WITH VEGFA, FUNCTION.
- Secreted 1 Publication
Cytoskeleton
- actin cytoskeleton Source: HPA
Endosome
- endosome Source: UniProtKB-SubCell
Extracellular region or secreted
- extracellular space Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
Plasma Membrane
- integral component of plasma membrane Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- plasma membrane Source: HPA
Other locations
- focal adhesion Source: UniProtKBInferred from high throughput direct assayi
- receptor complex Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Topology
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 27 – 758 | ExtracellularSequence analysisAdd BLAST | 732 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 759 – 780 | HelicalSequence analysisAdd BLAST | 22 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 781 – 1338 | CytoplasmicSequence analysisAdd BLAST | 558 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cell membrane, Cytoplasm, Endosome, Membrane, Secreted<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 767 | V → A: Abolishes proteolytic cleavage by PSEN1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 861 | K → M: Abolishes enzyme activity. Abolishes interaction with PLCG. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 914 | Y → F: Reduces phosphorylation at other tyrosine residues. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 1050 | N → D: Strongly increases kinase activity. Increases activity in promoting proliferation of endothelial cells. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 1169 | Y → F: Loss of phosphorylation site. Abolishes interaction with PLCG. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 1213 | Y → F: Loss of phosphorylation site. Abolishes interaction with PIK3R1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 1242 | Y → F: Loss of phosphorylation site. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 1327 | Y → F: Loss of phosphorylation site. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 1333 | Y → F: Loss of phosphorylation site. Abolishes interaction with CBL. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Organism-specific databases
DisGeNET More...DisGeNETi | 2321 |
MalaCards human disease database More...MalaCardsi | FLT1 |
Open Targets More...OpenTargetsi | ENSG00000102755 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA28180 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL1868 |
Drug and drug target database More...DrugBanki | DB06080 ABT-869 DB06626 Axitinib DB06101 IMC-1C11 DB09078 Lenvatinib DB07288 N-(4-chlorophenyl)-2-[(pyridin-4-ylmethyl)amino]benzamide DB09079 Nintedanib DB05913 OSI-930 DB06589 Pazopanib DB08896 Regorafenib DB00398 Sorafenib DB01268 Sunitinib DB05075 TG100801 DB04879 Vatalanib |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 1812 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | FLT1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 143811474 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei | 1 – 26 | 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 26 | |
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000016768 | 27 – 1338 | Vascular endothelial growth factor receptor 1Add BLAST | 1312 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 53 ↔ 107 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 100 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 158 ↔ 207 | |||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 164 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 196 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 251 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 252 ↔ 311 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 323 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 402 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 417 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 454 ↔ 535 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 474 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 547 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 577 ↔ 636 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 597 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 620 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 625 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 666 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 682 ↔ 731 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 914 | Phosphotyrosine; by autocatalysis1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1053 | Phosphotyrosine; by autocatalysisBy similarity | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1169 | Phosphotyrosine; by autocatalysis1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1213 | Phosphotyrosine; by autocatalysis5 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1242 | Phosphotyrosine; by autocatalysis1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1309 | Phosphotyrosine; by autocatalysis1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1327 | Phosphotyrosine; by autocatalysis2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1333 | Phosphotyrosine; by autocatalysis1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.3"Characterization of the VEGF binding site on the Flt-1 receptor."
Herley M.T., Yu Y., Whitney R.G., Sato J.D.
Biochem. Biophys. Res. Commun. 262:731-738(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH VEGFA, GLYCOSYLATION. - Ref.20"Direct identification of a major autophosphorylation site on vascular endothelial growth factor receptor Flt-1 that mediates phosphatidylinositol 3'-kinase binding."
Yu Y., Hulmes J.D., Herley M.T., Whitney R.G., Crabb J.W., Sato J.D.
Biochem. J. 358:465-472(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PIK3R1 AND VEGFA, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT TYR-1213, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.25"The c-Cbl/CD2AP complex regulates VEGF-induced endocytosis and degradation of Flt-1 (VEGFR-1)."
Kobayashi S., Sawano A., Nojima Y., Shibuya M., Maru Y.
FASEB J. 18:929-931(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CBL AND CD2AP, UBIQUITINATION, AUTOPHOSPHORYLATION IN RESPONSE TO VEGFA, MUTAGENESIS OF TYR-1333, SUBCELLULAR LOCATION.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.14"Identification of vascular endothelial growth factor receptor-1 tyrosine phosphorylation sites and binding of SH2 domain-containing molecules."
Ito N., Wernstedt C., Engstrom U., Claesson-Welsh L.
J. Biol. Chem. 273:23410-23418(1998) [PubMed] [Europe PMC] [Abstract]Cited for: PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY, PHOSPHORYLATION AT TYR-914; TYR-1213; TYR-1242; TYR-1327 AND TYR-1333, MUTAGENESIS OF TYR-914; TYR-1213; TYR-1242; TYR-1327 AND TYR-1333, INTERACTION WITH PLCG; GRB2; CRK; NCK1 AND PTPN11. - Ref.17"The phosphorylated 1169-tyrosine containing region of flt-1 kinase (VEGFR-1) is a major binding site for PLCgamma."
Sawano A., Takahashi T., Yamaguchi S., Shibuya M.
Biochem. Biophys. Res. Commun. 238:487-491(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN PHOSPHORYLATION OF PLCG AND ACTIVATION OF MAP KINASES, INTERACTION WITH PLCG, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-861 AND TYR-1169, PHOSPHORYLATION AT TYR-1169 AND TYR-1213. - Ref.18"Tyrosine 1213 of Flt-1 is a major binding site of Nck and SHP-2."
Igarashi K., Isohara T., Kato T., Shigeta K., Yamano T., Uno I.
Biochem. Biophys. Res. Commun. 246:95-99(1998) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PIK3R1; PTPN11 AND NCK1, PHOSPHORYLATION AT TYR-1213. - Ref.20"Direct identification of a major autophosphorylation site on vascular endothelial growth factor receptor Flt-1 that mediates phosphatidylinositol 3'-kinase binding."
Yu Y., Hulmes J.D., Herley M.T., Whitney R.G., Crabb J.W., Sato J.D.
Biochem. J. 358:465-472(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PIK3R1 AND VEGFA, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT TYR-1213, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION. - Ref.24"Role of PlGF in the intra- and intermolecular cross talk between the VEGF receptors Flt1 and Flk1."
Autiero M., Waltenberger J., Communi D., Kranz A., Moons L., Lambrechts D., Kroll J., Plaisance S., De Mol M., Bono F., Kliche S., Fellbrich G., Ballmer-Hofer K., Maglione D., Mayr-Beyrle U., Dewerchin M., Dombrowski S., Stanimirovic D. , Van Hummelen P., Dehio C., Hicklin D.J., Persico G., Herbert J.M., Communi D., Shibuya M., Collen D., Conway E.M., Carmeliet P.
Nat. Med. 9:936-943(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PGF AND KDR, FUNCTION IN PHOSPHORYLATION OF KDR; VEGFA AND PGF SIGNALING, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT TYR-1213; TYR-1327 AND TYR-1309.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 767 – 768 | Cleavage; by PSEN1Curated | 2 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P17948 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P17948 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P17948 |
PeptideAtlas More...PeptideAtlasi | P17948 |
PRoteomics IDEntifications database More...PRIDEi | P17948 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 53530 53531 [P17948-2] 53532 [P17948-3] 53533 [P17948-4] 53534 [P17948-5] 53535 [P17948-6] 53536 [P17948-7] |
PTM databases
GlyConnect protein glycosylation platform More...GlyConnecti | 771 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P17948 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P17948 |
UniCarbKB; an annotated and curated database of glycan structures More...UniCarbKBi | P17948 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.5"A novel human-specific soluble vascular endothelial growth factor receptor 1: cell-type-specific splicing and implications to vascular endothelial growth factor homeostasis and preeclampsia."
Sela S., Itin A., Natanson-Yaron S., Greenfield C., Goldman-Wohl D., Yagel S., Keshet E.
Circ. Res. 102:1566-1574(2008) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ROLE IN PREECLAMPSIA, INDUCTION. - Ref.6"A novel intracellular isoform of VEGFR-1 activates Src and promotes cell invasion in MDA-MB-231 breast cancer cells."
Mezquita B., Mezquita J., Pau M., Mezquita C.
J. Cell. Biochem. 110:732-742(2010) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5; 6; 7 AND 8), ALTERNATIVE SPLICING, FUNCTION IN PHOSPHORYLATION OF SRC AND CANCER CELL INVASIVENESS, TISSUE SPECIFICITY.
<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.5"A novel human-specific soluble vascular endothelial growth factor receptor 1: cell-type-specific splicing and implications to vascular endothelial growth factor homeostasis and preeclampsia."
Sela S., Itin A., Natanson-Yaron S., Greenfield C., Goldman-Wohl D., Yagel S., Keshet E.
Circ. Res. 102:1566-1574(2008) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ROLE IN PREECLAMPSIA, INDUCTION. - Ref.16"Migration of human monocytes in response to vascular endothelial growth factor (VEGF) is mediated via the VEGF receptor flt-1."
Barleon B., Sozzani S., Zhou D., Weich H.A., Mantovani A., Marme D.
Blood 87:3336-3343(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CELL MIGRATION, FUNCTION IN VEGFA AND PGF SIGNALING, INDUCTION.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000102755 |
CleanEx database of gene expression profiles More...CleanExi | HS_FLT1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P17948 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P17948 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB068189 CAB068190 HPA011740 HPA014290 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.2"Inhibition of vascular endothelial cell growth factor activity by an endogenously encoded soluble receptor."
Kendall R.L., Thomas K.A.
Proc. Natl. Acad. Sci. U.S.A. 90:10705-10709(1993) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF N-TERMINUS, SUBCELLULAR LOCATION (ISOFORM 2), INTERACTION WITH VEGFA, FUNCTION. - Ref.3"Characterization of the VEGF binding site on the Flt-1 receptor."
Herley M.T., Yu Y., Whitney R.G., Sato J.D.
Biochem. Biophys. Res. Commun. 262:731-738(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH VEGFA, GLYCOSYLATION. - Ref.14"Identification of vascular endothelial growth factor receptor-1 tyrosine phosphorylation sites and binding of SH2 domain-containing molecules."
Ito N., Wernstedt C., Engstrom U., Claesson-Welsh L.
J. Biol. Chem. 273:23410-23418(1998) [PubMed] [Europe PMC] [Abstract]Cited for: PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY, PHOSPHORYLATION AT TYR-914; TYR-1213; TYR-1242; TYR-1327 AND TYR-1333, MUTAGENESIS OF TYR-914; TYR-1213; TYR-1242; TYR-1327 AND TYR-1333, INTERACTION WITH PLCG; GRB2; CRK; NCK1 AND PTPN11. - Ref.15"A unique signal transduction from FLT tyrosine kinase, a receptor for vascular endothelial growth factor VEGF."
Seetharam L., Gotoh N., Maru Y., Neufeld G., Yamaguchi S., Shibuya M.
Oncogene 10:135-147(1995) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH VEGFA, AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY, FUNCTION IN PHOSPHORYLATION OF PLCG, ABSENCE OF MITOGENIC FUNCTION IN CULTURED FIBROBLASTS. - Ref.17"The phosphorylated 1169-tyrosine containing region of flt-1 kinase (VEGFR-1) is a major binding site for PLCgamma."
Sawano A., Takahashi T., Yamaguchi S., Shibuya M.
Biochem. Biophys. Res. Commun. 238:487-491(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN PHOSPHORYLATION OF PLCG AND ACTIVATION OF MAP KINASES, INTERACTION WITH PLCG, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-861 AND TYR-1169, PHOSPHORYLATION AT TYR-1169 AND TYR-1213. - Ref.18"Tyrosine 1213 of Flt-1 is a major binding site of Nck and SHP-2."
Igarashi K., Isohara T., Kato T., Shigeta K., Yamano T., Uno I.
Biochem. Biophys. Res. Commun. 246:95-99(1998) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PIK3R1; PTPN11 AND NCK1, PHOSPHORYLATION AT TYR-1213. - Ref.20"Direct identification of a major autophosphorylation site on vascular endothelial growth factor receptor Flt-1 that mediates phosphatidylinositol 3'-kinase binding."
Yu Y., Hulmes J.D., Herley M.T., Whitney R.G., Crabb J.W., Sato J.D.
Biochem. J. 358:465-472(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PIK3R1 AND VEGFA, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT TYR-1213, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION. - Ref.22"Signaling properties of VEGF receptor-1 and -2 homo- and heterodimers."
Huang K., Andersson C., Roomans G.M., Ito N., Claesson-Welsh L.
Int. J. Biochem. Cell Biol. 33:315-324(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH KDR, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, FUNCTION IN VEGFA SIGNALING; PHOSPHORYLATION OF PLCG AND ACTIVATION OF PHOSPHATIDYLINOSITOL KINASE AND PHOSPHOLIPASE C. - Ref.24"Role of PlGF in the intra- and intermolecular cross talk between the VEGF receptors Flt1 and Flk1."
Autiero M., Waltenberger J., Communi D., Kranz A., Moons L., Lambrechts D., Kroll J., Plaisance S., De Mol M., Bono F., Kliche S., Fellbrich G., Ballmer-Hofer K., Maglione D., Mayr-Beyrle U., Dewerchin M., Dombrowski S., Stanimirovic D. , Van Hummelen P., Dehio C., Hicklin D.J., Persico G., Herbert J.M., Communi D., Shibuya M., Collen D., Conway E.M., Carmeliet P.
Nat. Med. 9:936-943(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PGF AND KDR, FUNCTION IN PHOSPHORYLATION OF KDR; VEGFA AND PGF SIGNALING, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT TYR-1213; TYR-1327 AND TYR-1309. - Ref.25"The c-Cbl/CD2AP complex regulates VEGF-induced endocytosis and degradation of Flt-1 (VEGFR-1)."
Kobayashi S., Sawano A., Nojima Y., Shibuya M., Maru Y.
FASEB J. 18:929-931(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CBL AND CD2AP, UBIQUITINATION, AUTOPHOSPHORYLATION IN RESPONSE TO VEGFA, MUTAGENESIS OF TYR-1333, SUBCELLULAR LOCATION. - Ref.32"RACK1 regulates VEGF/Flt1-mediated cell migration via activation of a PI3-K/Akt pathway."
Wang F., Yamauchi M., Muramatsu M., Osawa T., Tsuchida R., Shibuya M.
J. Biol. Chem. 286:9097-9106(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RACK1. - Ref.33"gamma-Secretase and presenilin mediate cleavage and phosphorylation of vascular endothelial growth factor receptor-1."
Cai J., Chen Z., Ruan Q., Han S., Liu L., Qi X., Boye S.L., Hauswirth W.W., Grant M.B., Boulton M.E.
J. Biol. Chem. 286:42514-42523(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PSEN1 AND PTPRB, DEPHOSPHORYLATION BY PTPRB, MUTAGENESIS OF VAL-767, PROTEOLYTIC CLEAVAGE BY PSEN1 AT VAL-767. - Ref.42"Crystal structure at 1.7 A resolution of VEGF in complex with domain 2 of the Flt-1 receptor."
Wiesmann C., Fuh G., Christinger H.W., Eigenbrot C., Wells J.A., de Vos A.M.
Cell 91:695-704(1997) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 132-226 IN COMPLEX WITH VEGFA, DOMAIN. - Ref.43"Solution structure of the VEGF-binding domain of Flt-1: comparison of its free and bound states."
Starovasnik M.A., Christinger H.W., Wiesmann C., Champe M.A., de Vos A.M., Skelton N.J.
J. Mol. Biol. 293:531-544(1999) [PubMed] [Europe PMC] [Abstract] - Ref.44"The crystal structure of placental growth factor in complex with domain 2 of vascular endothelial growth factor receptor-1."
Christinger H.W., Fuh G., de Vos A.M., Wiesmann C.
J. Biol. Chem. 279:10382-10388(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 130-229 IN COMPLEX WITH PGF. - Ref.45"Structural insights into the binding of vascular endothelial growth factor-B by VEGFR-1(D2): recognition and specificity."
Iyer S., Darley P.I., Acharya K.R.
J. Biol. Chem. 285:23779-23789(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 129-226 IN COMPLEX WITH VEGFB, INTERACTION WITH VEGFB, SUBUNIT, DOMAIN.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| CBL | P22681 | 2 | EBI-1026718,EBI-518228 | |
| CRKL | P46109 | 9 | EBI-1026718,EBI-910 | |
| CTNNB1 | P35222 | 2 | EBI-1026718,EBI-491549 | |
| HCK | P08631 | 2 | EBI-1026718,EBI-346340 | |
| HSPG2 | P98160 | 2 | EBI-6530464,EBI-6896259 | |
| PGF | P49763 | 2 | EBI-1026718,EBI-1037633 | |
| PIK3R1 | P27986 | 2 | EBI-1026718,EBI-79464 | |
| PLCG1 | P19174 | 2 | EBI-1026718,EBI-79387 | |
| PTK2 | Q05397 | 2 | EBI-1026718,EBI-702142 | |
| PTPN11 | Q06124 | 2 | EBI-1026718,EBI-297779 | |
| PTPRJ | Q12913 | 2 | EBI-1026718,EBI-2264500 | |
| VEGFA | P15692 | 4 | EBI-1026718,EBI-1026643 | |
| VEGFA | P15692-4 | 3 | EBI-1026718,EBI-1026691 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- growth factor binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 108609, 14 interactors |
Database of interacting proteins More...DIPi | DIP-643N |
Protein interaction database and analysis system More...IntActi | P17948, 30 interactors |
Molecular INTeraction database More...MINTi | P17948 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000282397 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P17948 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 130 – 132 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 135 – 137 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 140 – 142 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 144 – 148 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 150 – 152 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 154 – 156 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 160 – 162 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 163 – 165 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 168 – 171 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 172 – 174 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 175 – 177 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 181 – 187 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 188 – 190 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 191 – 196 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 199 – 201 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 203 – 211 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 214 – 224 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 806 – 809 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 817 – 820 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 824 – 826 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 827 – 835 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 837 – 848 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 849 – 851 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 854 – 863 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 869 – 883 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 894 – 898 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 906 – 910 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 917 – 922 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 996 – 1014 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 19 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 1015 – 1017 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 1025 – 1027 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 1028 – 1030 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 1032 – 1034 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 1036 – 1038 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 1042 – 1044 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 1047 – 1049 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 1053 – 1055 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 1063 – 1065 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 1068 – 1073 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 1078 – 1093 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 16 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 1107 – 1113 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 1114 – 1116 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 1127 – 1136 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 1141 – 1143 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 1147 – 1157 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1FLT | X-ray | 1.70 | X/Y | 132-226 | [»] | |
| 1QSV | NMR | - | A | 129-229 | [»] | |
| 1QSZ | NMR | - | A | 129-229 | [»] | |
| 1QTY | X-ray | 2.70 | T/U/X/Y | 129-229 | [»] | |
| 1RV6 | X-ray | 2.45 | X/Y | 130-229 | [»] | |
| 2XAC | X-ray | 2.71 | C/X | 129-226 | [»] | |
| 3HNG | X-ray | 2.70 | A | 801-1158 | [»] | |
| 4CKV | X-ray | 2.06 | X | 132-225 | [»] | |
| 4CL7 | X-ray | 2.00 | A/B/C/D | 132-225 | [»] | |
| 5ABD | X-ray | 2.00 | E/I/X | 132-226 | [»] | |
| 5EX3 | X-ray | 2.41 | D | 827-835 | [»] | |
| 5T89 | X-ray | 4.00 | X/Y | 27-656 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P17948 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P17948 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P17948 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 32 – 123 | Ig-like C2-type 1Add BLAST | 92 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 151 – 214 | Ig-like C2-type 2Add BLAST | 64 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 230 – 327 | Ig-like C2-type 3Add BLAST | 98 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 335 – 421 | Ig-like C2-type 4Add BLAST | 87 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 428 – 553 | Ig-like C2-type 5Add BLAST | 126 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 556 – 654 | Ig-like C2-type 6Add BLAST | 99 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 661 – 747 | Ig-like C2-type 7Add BLAST | 87 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 827 – 1158 | Protein kinasePROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 332 |
<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.42"Crystal structure at 1.7 A resolution of VEGF in complex with domain 2 of the Flt-1 receptor."
Wiesmann C., Fuh G., Christinger H.W., Eigenbrot C., Wells J.A., de Vos A.M.
Cell 91:695-704(1997) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 132-226 IN COMPLEX WITH VEGFA, DOMAIN. - Ref.45"Structural insights into the binding of vascular endothelial growth factor-B by VEGFR-1(D2): recognition and specificity."
Iyer S., Darley P.I., Acharya K.R.
J. Biol. Chem. 285:23779-23789(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 129-226 IN COMPLEX WITH VEGFB, INTERACTION WITH VEGFB, SUBUNIT, DOMAIN.
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Domaini
Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helixPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0200 Eukaryota COG0515 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000118923 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000037949 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG053432 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P17948 |
KEGG Orthology (KO) More...KOi | K05096 |
Identification of Orthologs from Complete Genome Data More...OMAi | ITLTCTC |
Database of Orthologous Groups More...OrthoDBi | EOG091G01TL |
Database for complete collections of gene phylogenies More...PhylomeDBi | P17948 |
TreeFam database of animal gene trees More...TreeFami | TF325768 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.60.40.10, 7 hits |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR007110 Ig-like_dom IPR036179 Ig-like_dom_sf IPR013783 Ig-like_fold IPR013098 Ig_I-set IPR003599 Ig_sub IPR003598 Ig_sub2 IPR013106 Ig_V-set IPR013151 Immunoglobulin IPR011009 Kinase-like_dom_sf 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 IPR009135 VEGFR1_rcpt |
Pfam protein domain database More...Pfami | View protein in Pfam PF07679 I-set, 2 hits PF00047 ig, 1 hit PF07714 Pkinase_Tyr, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR01833 VEGFRECEPTR1 |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00409 IG, 7 hits SM00408 IGc2, 5 hits SM00406 IGv, 2 hits SM00219 TyrKc, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF48726 SSF48726, 8 hits SSF56112 SSF56112, 2 hits |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50835 IG_LIKE, 6 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 |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (8)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 8 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
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.
10 20 30 40 50
MVSYWDTGVL LCALLSCLLL TGSSSGSKLK DPELSLKGTQ HIMQAGQTLH
60 70 80 90 100
LQCRGEAAHK WSLPEMVSKE SERLSITKSA CGRNGKQFCS TLTLNTAQAN
110 120 130 140 150
HTGFYSCKYL AVPTSKKKET ESAIYIFISD TGRPFVEMYS EIPEIIHMTE
160 170 180 190 200
GRELVIPCRV TSPNITVTLK KFPLDTLIPD GKRIIWDSRK GFIISNATYK
210 220 230 240 250
EIGLLTCEAT VNGHLYKTNY LTHRQTNTII DVQISTPRPV KLLRGHTLVL
260 270 280 290 300
NCTATTPLNT RVQMTWSYPD EKNKRASVRR RIDQSNSHAN IFYSVLTIDK
310 320 330 340 350
MQNKDKGLYT CRVRSGPSFK SVNTSVHIYD KAFITVKHRK QQVLETVAGK
360 370 380 390 400
RSYRLSMKVK AFPSPEVVWL KDGLPATEKS ARYLTRGYSL IIKDVTEEDA
410 420 430 440 450
GNYTILLSIK QSNVFKNLTA TLIVNVKPQI YEKAVSSFPD PALYPLGSRQ
460 470 480 490 500
ILTCTAYGIP QPTIKWFWHP CNHNHSEARC DFCSNNEESF ILDADSNMGN
510 520 530 540 550
RIESITQRMA IIEGKNKMAS TLVVADSRIS GIYICIASNK VGTVGRNISF
560 570 580 590 600
YITDVPNGFH VNLEKMPTEG EDLKLSCTVN KFLYRDVTWI LLRTVNNRTM
610 620 630 640 650
HYSISKQKMA ITKEHSITLN LTIMNVSLQD SGTYACRARN VYTGEEILQK
660 670 680 690 700
KEITIRDQEA PYLLRNLSDH TVAISSSTTL DCHANGVPEP QITWFKNNHK
710 720 730 740 750
IQQEPGIILG PGSSTLFIER VTEEDEGVYH CKATNQKGSV ESSAYLTVQG
760 770 780 790 800
TSDKSNLELI TLTCTCVAAT LFWLLLTLFI RKMKRSSSEI KTDYLSIIMD
810 820 830 840 850
PDEVPLDEQC ERLPYDASKW EFARERLKLG KSLGRGAFGK VVQASAFGIK
860 870 880 890 900
KSPTCRTVAV KMLKEGATAS EYKALMTELK ILTHIGHHLN VVNLLGACTK
910 920 930 940 950
QGGPLMVIVE YCKYGNLSNY LKSKRDLFFL NKDAALHMEP KKEKMEPGLE
960 970 980 990 1000
QGKKPRLDSV TSSESFASSG FQEDKSLSDV EEEEDSDGFY KEPITMEDLI
1010 1020 1030 1040 1050
SYSFQVARGM EFLSSRKCIH RDLAARNILL SENNVVKICD FGLARDIYKN
1060 1070 1080 1090 1100
PDYVRKGDTR LPLKWMAPES IFDKIYSTKS DVWSYGVLLW EIFSLGGSPY
1110 1120 1130 1140 1150
PGVQMDEDFC SRLREGMRMR APEYSTPEIY QIMLDCWHRD PKERPRFAEL
1160 1170 1180 1190 1200
VEKLGDLLQA NVQQDGKDYI PINAILTGNS GFTYSTPAFS EDFFKESISA
1210 1220 1230 1240 1250
PKFNSGSSDD VRYVNAFKFM SLERIKTFEE LLPNATSMFD DYQGDSSTLL
1260 1270 1280 1290 1300
ASPMLKRFTW TDSKPKASLK IDLRVTSKSK ESGLSDVSRP SFCHSSCGHV
1310 1320 1330
SEGKRRFTYD HAELERKIAC CSPPPDYNSV VLYSTPPI
The sequence of this isoform differs from the canonical sequence as follows:
657-687: DQEAPYLLRNLSDHTVAISSSTTLDCHANGV → GEHCNKKAVFSRISKFKSTRNDCTTQSNVKH
688-1338: Missing.
10 20 30 40 50
MVSYWDTGVL LCALLSCLLL TGSSSGSKLK DPELSLKGTQ HIMQAGQTLH
60 70 80 90 100
LQCRGEAAHK WSLPEMVSKE SERLSITKSA CGRNGKQFCS TLTLNTAQAN
110 120 130 140 150
HTGFYSCKYL AVPTSKKKET ESAIYIFISD TGRPFVEMYS EIPEIIHMTE
160 170 180 190 200
GRELVIPCRV TSPNITVTLK KFPLDTLIPD GKRIIWDSRK GFIISNATYK
210 220 230 240 250
EIGLLTCEAT VNGHLYKTNY LTHRQTNTII DVQISTPRPV KLLRGHTLVL
260 270 280 290 300
NCTATTPLNT RVQMTWSYPD EKNKRASVRR RIDQSNSHAN IFYSVLTIDK
310 320 330 340 350
MQNKDKGLYT CRVRSGPSFK SVNTSVHIYD KAFITVKHRK QQVLETVAGK
360 370 380 390 400
RSYRLSMKVK AFPSPEVVWL KDGLPATEKS ARYLTRGYSL IIKDVTEEDA
410 420 430 440 450
GNYTILLSIK QSNVFKNLTA TLIVNVKPQI YEKAVSSFPD PALYPLGSRQ
460 470 480 490 500
ILTCTAYGIP QPTIKWFWHP CNHNHSEARC DFCSNNEESF ILDADSNMGN
510 520 530 540 550
RIESITQRMA IIEGKNKMAS TLVVADSRIS GIYICIASNK VGTVGRNISF
560 570 580 590 600
YITDVPNGFH VNLEKMPTEG EDLKLSCTVN KFLYRDVTWI LLRTVNNRTM
610 620 630 640 650
HYSISKQKMA ITKEHSITLN LTIMNVSLQD SGTYACRARN VYTGEEILQK
660 670 680
KEITIRGEHC NKKAVFSRIS KFKSTRNDCT TQSNVKH
The sequence of this isoform differs from the canonical sequence as follows:
706-733: GIILGPGSSTLFIERVTEEDEGVYHCKA → ELYTSTSPSSSSSSPLSSSSSSSSSSSS
734-1338: Missing.
10 20 30 40 50
MVSYWDTGVL LCALLSCLLL TGSSSGSKLK DPELSLKGTQ HIMQAGQTLH
60 70 80 90 100
LQCRGEAAHK WSLPEMVSKE SERLSITKSA CGRNGKQFCS TLTLNTAQAN
110 120 130 140 150
HTGFYSCKYL AVPTSKKKET ESAIYIFISD TGRPFVEMYS EIPEIIHMTE
160 170 180 190 200
GRELVIPCRV TSPNITVTLK KFPLDTLIPD GKRIIWDSRK GFIISNATYK
210 220 230 240 250
EIGLLTCEAT VNGHLYKTNY LTHRQTNTII DVQISTPRPV KLLRGHTLVL
260 270 280 290 300
NCTATTPLNT RVQMTWSYPD EKNKRASVRR RIDQSNSHAN IFYSVLTIDK
310 320 330 340 350
MQNKDKGLYT CRVRSGPSFK SVNTSVHIYD KAFITVKHRK QQVLETVAGK
360 370 380 390 400
RSYRLSMKVK AFPSPEVVWL KDGLPATEKS ARYLTRGYSL IIKDVTEEDA
410 420 430 440 450
GNYTILLSIK QSNVFKNLTA TLIVNVKPQI YEKAVSSFPD PALYPLGSRQ
460 470 480 490 500
ILTCTAYGIP QPTIKWFWHP CNHNHSEARC DFCSNNEESF ILDADSNMGN
510 520 530 540 550
RIESITQRMA IIEGKNKMAS TLVVADSRIS GIYICIASNK VGTVGRNISF
560 570 580 590 600
YITDVPNGFH VNLEKMPTEG EDLKLSCTVN KFLYRDVTWI LLRTVNNRTM
610 620 630 640 650
HYSISKQKMA ITKEHSITLN LTIMNVSLQD SGTYACRARN VYTGEEILQK
660 670 680 690 700
KEITIRDQEA PYLLRNLSDH TVAISSSTTL DCHANGVPEP QITWFKNNHK
710 720 730
IQQEPELYTS TSPSSSSSSP LSSSSSSSSS SSS
The sequence of this isoform differs from the canonical sequence as follows:
518-541: MASTLVVADSRISGIYICIASNKV → LPPANSSFMLPPTSFSSNYFHFLP
542-1338: Missing.
10 20 30 40 50
MVSYWDTGVL LCALLSCLLL TGSSSGSKLK DPELSLKGTQ HIMQAGQTLH
60 70 80 90 100
LQCRGEAAHK WSLPEMVSKE SERLSITKSA CGRNGKQFCS TLTLNTAQAN
110 120 130 140 150
HTGFYSCKYL AVPTSKKKET ESAIYIFISD TGRPFVEMYS EIPEIIHMTE
160 170 180 190 200
GRELVIPCRV TSPNITVTLK KFPLDTLIPD GKRIIWDSRK GFIISNATYK
210 220 230 240 250
EIGLLTCEAT VNGHLYKTNY LTHRQTNTII DVQISTPRPV KLLRGHTLVL
260 270 280 290 300
NCTATTPLNT RVQMTWSYPD EKNKRASVRR RIDQSNSHAN IFYSVLTIDK
310 320 330 340 350
MQNKDKGLYT CRVRSGPSFK SVNTSVHIYD KAFITVKHRK QQVLETVAGK
360 370 380 390 400
RSYRLSMKVK AFPSPEVVWL KDGLPATEKS ARYLTRGYSL IIKDVTEEDA
410 420 430 440 450
GNYTILLSIK QSNVFKNLTA TLIVNVKPQI YEKAVSSFPD PALYPLGSRQ
460 470 480 490 500
ILTCTAYGIP QPTIKWFWHP CNHNHSEARC DFCSNNEESF ILDADSNMGN
510 520 530 540
RIESITQRMA IIEGKNKLPP ANSSFMLPPT SFSSNYFHFL P
The sequence of this isoform differs from the canonical sequence as follows:
1-782: Missing.
10 20 30 40 50
MKRSSSEIKT DYLSIIMDPD EVPLDEQCER LPYDASKWEF ARERLKLGKS
60 70 80 90 100
LGRGAFGKVV QASAFGIKKS PTCRTVAVKM LKEGATASEY KALMTELKIL
110 120 130 140 150
THIGHHLNVV NLLGACTKQG GPLMVIVEYC KYGNLSNYLK SKRDLFFLNK
160 170 180 190 200
DAALHMEPKK EKMEPGLEQG KKPRLDSVTS SESFASSGFQ EDKSLSDVEE
210 220 230 240 250
EEDSDGFYKE PITMEDLISY SFQVARGMEF LSSRKCIHRD LAARNILLSE
260 270 280 290 300
NNVVKICDFG LARDIYKNPD YVRKGDTRLP LKWMAPESIF DKIYSTKSDV
310 320 330 340 350
WSYGVLLWEI FSLGGSPYPG VQMDEDFCSR LREGMRMRAP EYSTPEIYQI
360 370 380 390 400
MLDCWHRDPK ERPRFAELVE KLGDLLQANV QQDGKDYIPI NAILTGNSGF
410 420 430 440 450
TYSTPAFSED FFKESISAPK FNSGSSDDVR YVNAFKFMSL ERIKTFEELL
460 470 480 490 500
PNATSMFDDY QGDSSTLLAS PMLKRFTWTD SKPKASLKID LRVTSKSKES
510 520 530 540 550
GLSDVSRPSF CHSSCGHVSE GKRRFTYDHA ELERKIACCS PPPDYNSVVL
YSTPPI
The sequence of this isoform differs from the canonical sequence as follows:
1-875: Missing.
10 20 30 40 50
MTELKILTHI GHHLNVVNLL GACTKQGGPL MVIVEYCKYG NLSNYLKSKR
60 70 80 90 100
DLFFLNKDAA LHMEPKKEKM EPGLEQGKKP RLDSVTSSES FASSGFQEDK
110 120 130 140 150
SLSDVEEEED SDGFYKEPIT MEDLISYSFQ VARGMEFLSS RKCIHRDLAA
160 170 180 190 200
RNILLSENNV VKICDFGLAR DIYKNPDYVR KGDTRLPLKW MAPESIFDKI
210 220 230 240 250
YSTKSDVWSY GVLLWEIFSL GGSPYPGVQM DEDFCSRLRE GMRMRAPEYS
260 270 280 290 300
TPEIYQIMLD CWHRDPKERP RFAELVEKLG DLLQANVQQD GKDYIPINAI
310 320 330 340 350
LTGNSGFTYS TPAFSEDFFK ESISAPKFNS GSSDDVRYVN AFKFMSLERI
360 370 380 390 400
KTFEELLPNA TSMFDDYQGD SSTLLASPML KRFTWTDSKP KASLKIDLRV
410 420 430 440 450
TSKSKESGLS DVSRPSFCHS SCGHVSEGKR RFTYDHAELE RKIACCSPPP
460
DYNSVVLYST PPI
The sequence of this isoform differs from the canonical sequence as follows:
1-995: Missing.
10 20 30 40 50
MEDLISYSFQ VARGMEFLSS RKCIHRDLAA RNILLSENNV VKICDFGLAR
60 70 80 90 100
DIYKNPDYVR KGDTRLPLKW MAPESIFDKI YSTKSDVWSY GVLLWEIFSL
110 120 130 140 150
GGSPYPGVQM DEDFCSRLRE GMRMRAPEYS TPEIYQIMLD CWHRDPKERP
160 170 180 190 200
RFAELVEKLG DLLQANVQQD GKDYIPINAI LTGNSGFTYS TPAFSEDFFK
210 220 230 240 250
ESISAPKFNS GSSDDVRYVN AFKFMSLERI KTFEELLPNA TSMFDDYQGD
260 270 280 290 300
SSTLLASPML KRFTWTDSKP KASLKIDLRV TSKSKESGLS DVSRPSFCHS
310 320 330 340
SCGHVSEGKR RFTYDHAELE RKIACCSPPP DYNSVVLYST PPI
The sequence of this isoform differs from the canonical sequence as follows:
1-7: MVSYWDT → MNSDLLV
8-984: Missing.
10 20 30 40 50
MNSDLLVDSD GFYKEPITME DLISYSFQVA RGMEFLSSRK CIHRDLAARN
60 70 80 90 100
ILLSENNVVK ICDFGLARDI YKNPDYVRKG DTRLPLKWMA PESIFDKIYS
110 120 130 140 150
TKSDVWSYGV LLWEIFSLGG SPYPGVQMDE DFCSRLREGM RMRAPEYSTP
160 170 180 190 200
EIYQIMLDCW HRDPKERPRF AELVEKLGDL LQANVQQDGK DYIPINAILT
210 220 230 240 250
GNSGFTYSTP AFSEDFFKES ISAPKFNSGS SDDVRYVNAF KFMSLERIKT
260 270 280 290 300
FEELLPNATS MFDDYQGDSS TLLASPMLKR FTWTDSKPKA SLKIDLRVTS
310 320 330 340 350
KSKESGLSDV SRPSFCHSSC GHVSEGKRRF TYDHAELERK IACCSPPPDY
360
NSVVLYSTPP I
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 490 | F → S in AAC16449 (PubMed:10471394).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 779 | F → L in CAA35946 (PubMed:2158038).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1029 | L → F in ABI53803 (PubMed:20512933).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1029 | L → F in ABI53804 (PubMed:20512933).Curated | 1 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_042045 | 60 | K → T1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_049719 | 128 | I → L. Corresponds to variant dbSNP:rs35073261Ensembl. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_042046 | 144 | E → K1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_042047 | 281 | R → Q1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_042048 | 422 | L → I in a lung adenocarcinoma sample; somatic mutation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_042049 | 781 | R → Q in a glioma low grade oligodendroglioma sample; somatic mutation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_042050 | 938 | M → V1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_042051 | 982 | E → A1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_042052 | 1061 | L → V in a bladder transitional cell carcinoma sample; somatic mutation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_041983 | 1 – 995 | Missing in isoform 7. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 995 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_041984 | 1 – 875 | Missing in isoform 6. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 875 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_041985 | 1 – 782 | Missing in isoform 5. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 782 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_047759 | 1 – 7 | MVSYWDT → MNSDLLV in isoform 8. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 7 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_047760 | 8 – 984 | Missing in isoform 8. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 977 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_041929 | 518 – 541 | MASTL…ASNKV → LPPANSSFMLPPTSFSSNYF HFLP in isoform 4. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 24 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_041930 | 542 – 1338 | Missing in isoform 4. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 797 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_002955 | 657 – 687 | DQEAP…HANGV → GEHCNKKAVFSRISKFKSTR NDCTTQSNVKH in isoform 2. 3 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 31 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_002956 | 688 – 1338 | Missing in isoform 2. 3 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 651 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_041927 | 706 – 733 | GIILG…YHCKA → ELYTSTSPSSSSSSPLSSSS SSSSSSSS in isoform 3. 3 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 28 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_041928 | 734 – 1338 | Missing in isoform 3. 3 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 605 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | X51602 mRNA Translation: CAA35946.1 U01134 mRNA Translation: AAC50060.1 AF063657 mRNA Translation: AAC16449.2 EU826561 mRNA Translation: ACF47597.1 EU368830 mRNA Translation: ACA62948.1 DQ836394 mRNA Translation: ABI53803.1 DQ836395 mRNA Translation: ABI53804.1 DQ836396 mRNA Translation: ABI53805.1 EF491868 mRNA Translation: ABS32268.1 EF491869 mRNA Translation: ABS32269.1 EF491870 mRNA Translation: ABS32270.1 EU360600 mRNA Translation: ACB05747.1 EU332841 Genomic DNA Translation: ABY87530.1 AK292936 mRNA Translation: BAF85625.1 AK300392 mRNA Translation: BAG62125.1 AL138712 Genomic DNA No translation available. AL139005 Genomic DNA No translation available. CH471075 Genomic DNA Translation: EAX08431.1 CH471075 Genomic DNA Translation: EAX08432.1 BC039007 mRNA Translation: AAH39007.1 D00133 Genomic DNA Translation: BAA00080.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS53860.1 [P17948-3] CCDS53861.1 [P17948-4] CCDS73556.1 [P17948-2] CCDS9330.1 [P17948-1] |
Protein sequence database of the Protein Information Resource More...PIRi | A49636 S09982 |
NCBI Reference Sequences More...RefSeqi | NP_001153392.1, NM_001159920.1 [P17948-2] NP_001153502.1, NM_001160030.1 [P17948-3] NP_001153503.1, NM_001160031.1 [P17948-4] NP_002010.2, NM_002019.4 [P17948-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.594454 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000282397; ENSP00000282397; ENSG00000102755 [P17948-1] ENST00000539099; ENSP00000442630; ENSG00000102755 [P17948-4] ENST00000541932; ENSP00000437631; ENSG00000102755 [P17948-3] ENST00000543394; ENSP00000437841; ENSG00000102755 [P17948-8] ENST00000615840; ENSP00000484039; ENSG00000102755 [P17948-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 2321 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:2321 |
UCSC genome browser More...UCSCi | uc001usb.4 human [P17948-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative splicing, Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | X51602 mRNA Translation: CAA35946.1 U01134 mRNA Translation: AAC50060.1 AF063657 mRNA Translation: AAC16449.2 EU826561 mRNA Translation: ACF47597.1 EU368830 mRNA Translation: ACA62948.1 DQ836394 mRNA Translation: ABI53803.1 DQ836395 mRNA Translation: ABI53804.1 DQ836396 mRNA Translation: ABI53805.1 EF491868 mRNA Translation: ABS32268.1 EF491869 mRNA Translation: ABS32269.1 EF491870 mRNA Translation: ABS32270.1 EU360600 mRNA Translation: ACB05747.1 EU332841 Genomic DNA Translation: ABY87530.1 AK292936 mRNA Translation: BAF85625.1 AK300392 mRNA Translation: BAG62125.1 AL138712 Genomic DNA No translation available. AL139005 Genomic DNA No translation available. CH471075 Genomic DNA Translation: EAX08431.1 CH471075 Genomic DNA Translation: EAX08432.1 BC039007 mRNA Translation: AAH39007.1 D00133 Genomic DNA Translation: BAA00080.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS53860.1 [P17948-3] CCDS53861.1 [P17948-4] CCDS73556.1 [P17948-2] CCDS9330.1 [P17948-1] |
Protein sequence database of the Protein Information Resource More...PIRi | A49636 S09982 |
NCBI Reference Sequences More...RefSeqi | NP_001153392.1, NM_001159920.1 [P17948-2] NP_001153502.1, NM_001160030.1 [P17948-3] NP_001153503.1, NM_001160031.1 [P17948-4] NP_002010.2, NM_002019.4 [P17948-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.594454 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1FLT | X-ray | 1.70 | X/Y | 132-226 | [»] | |
| 1QSV | NMR | - | A | 129-229 | [»] | |
| 1QSZ | NMR | - | A | 129-229 | [»] | |
| 1QTY | X-ray | 2.70 | T/U/X/Y | 129-229 | [»] | |
| 1RV6 | X-ray | 2.45 | X/Y | 130-229 | [»] | |
| 2XAC | X-ray | 2.71 | C/X | 129-226 | [»] | |
| 3HNG | X-ray | 2.70 | A | 801-1158 | [»] | |
| 4CKV | X-ray | 2.06 | X | 132-225 | [»] | |
| 4CL7 | X-ray | 2.00 | A/B/C/D | 132-225 | [»] | |
| 5ABD | X-ray | 2.00 | E/I/X | 132-226 | [»] | |
| 5EX3 | X-ray | 2.41 | D | 827-835 | [»] | |
| 5T89 | X-ray | 4.00 | X/Y | 27-656 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P17948 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P17948 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 108609, 14 interactors |
Database of interacting proteins More...DIPi | DIP-643N |
Protein interaction database and analysis system More...IntActi | P17948, 30 interactors |
Molecular INTeraction database More...MINTi | P17948 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000282397 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P17948 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL1868 |
Drug and drug target database More...DrugBanki | DB06080 ABT-869 DB06626 Axitinib DB06101 IMC-1C11 DB09078 Lenvatinib DB07288 N-(4-chlorophenyl)-2-[(pyridin-4-ylmethyl)amino]benzamide DB09079 Nintedanib DB05913 OSI-930 DB06589 Pazopanib DB08896 Regorafenib DB00398 Sorafenib DB01268 Sunitinib DB05075 TG100801 DB04879 Vatalanib |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 1812 |
PTM databases
GlyConnect protein glycosylation platform More...GlyConnecti | 771 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P17948 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P17948 |
UniCarbKB; an annotated and curated database of glycan structures More...UniCarbKBi | P17948 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | FLT1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 143811474 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P17948 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P17948 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P17948 |
PeptideAtlas More...PeptideAtlasi | P17948 |
PRoteomics IDEntifications database More...PRIDEi | P17948 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 53530 53531 [P17948-2] 53532 [P17948-3] 53533 [P17948-4] 53534 [P17948-5] 53535 [P17948-6] 53536 [P17948-7] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 2321 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000282397; ENSP00000282397; ENSG00000102755 [P17948-1] ENST00000539099; ENSP00000442630; ENSG00000102755 [P17948-4] ENST00000541932; ENSP00000437631; ENSG00000102755 [P17948-3] ENST00000543394; ENSP00000437841; ENSG00000102755 [P17948-8] ENST00000615840; ENSP00000484039; ENSG00000102755 [P17948-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 2321 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:2321 |
UCSC genome browser More...UCSCi | uc001usb.4 human [P17948-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 2321 |
DisGeNET More...DisGeNETi | 2321 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000102755.10 |
GeneCards: human genes, protein and diseases More...GeneCardsi | FLT1 |
H-Invitational Database, human transcriptome db More...H-InvDBi | HIX0130593 |
Human Gene Nomenclature Database More...HGNCi | HGNC:3763 FLT1 |
Human Protein Atlas More...HPAi | CAB068189 CAB068190 HPA011740 HPA014290 |
MalaCards human disease database More...MalaCardsi | FLT1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 165070 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P17948 |
Open Targets More...OpenTargetsi | ENSG00000102755 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA28180 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0200 Eukaryota COG0515 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000118923 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000037949 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG053432 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P17948 |
KEGG Orthology (KO) More...KOi | K05096 |
Identification of Orthologs from Complete Genome Data More...OMAi | ITLTCTC |
Database of Orthologous Groups More...OrthoDBi | EOG091G01TL |
Database for complete collections of gene phylogenies More...PhylomeDBi | P17948 |
TreeFam database of animal gene trees More...TreeFami | TF325768 |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.7.10.1 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-194306 Neurophilin interactions with VEGF and VEGFR R-HSA-195399 VEGF binds to VEGFR leading to receptor dimerization |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | P17948 |
SIGNOR Signaling Network Open Resource More...SIGNORi | P17948 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | FLT1 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P17948 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | FLT1 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 2321 |
Protein Ontology More...PROi | PR:P17948 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000102755 |
CleanEx database of gene expression profiles More...CleanExi | HS_FLT1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P17948 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P17948 HS |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.60.40.10, 7 hits |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR007110 Ig-like_dom IPR036179 Ig-like_dom_sf IPR013783 Ig-like_fold IPR013098 Ig_I-set IPR003599 Ig_sub IPR003598 Ig_sub2 IPR013106 Ig_V-set IPR013151 Immunoglobulin IPR011009 Kinase-like_dom_sf 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 IPR009135 VEGFR1_rcpt |
Pfam protein domain database More...Pfami | View protein in Pfam PF07679 I-set, 2 hits PF00047 ig, 1 hit PF07714 Pkinase_Tyr, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR01833 VEGFRECEPTR1 |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00409 IG, 7 hits SM00408 IGc2, 5 hits SM00406 IGv, 2 hits SM00219 TyrKc, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF48726 SSF48726, 8 hits SSF56112 SSF56112, 2 hits |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50835 IG_LIKE, 6 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 |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | VGFR1_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P17948Primary (citable) accession number: P17948 Secondary accession number(s): A3E342 , A3E344, A8KA71, B0LPF1, B2BF46, B2BF47, B2BF48, B3FR89, B5A923, F5H5L6, O60722, P16057, Q12954 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1990 |
| Last sequence update: | April 3, 2007 | |
| Last modified: | June 20, 2018 | |
| This is version 217 of the entry and version 2 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 13
Human chromosome 13: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - Human and mouse protein kinases
Human and mouse protein kinases: classification and index - SIMILARITY comments
Index of protein domains and families
