| UniProt ID | VEGFA_HUMAN | |
|---|---|---|
| UniProt AC | P15692 | |
| Protein Name | Vascular endothelial growth factor A | |
| Gene Name | VEGFA | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 232 | |
| Subcellular Localization | Secreted . VEGF121 is acidic and freely secreted. VEGF165 is more basic, has heparin-binding properties and, although a signicant proportion remains cell-associated, most is freely secreted. VEGF189 is very basic, it is cell-associated after secretio | |
| Protein Description | Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. NRP1/Neuropilin-1 binds isoforms VEGF-165 and VEGF-145. Isoform VEGF165B binds to KDR but does not activate downstream signaling pathways, does not activate angiogenesis and inhibits tumor growth. Binding to NRP1 receptor initiates a signaling pathway needed for motor neuron axon guidance and cell body migration, including for the caudal migration of facial motor neurons from rhombomere 4 to rhombomere 6 during embryonic development (By similarity).. | |
| Protein Sequence | MNFLLSWVHWSLALLLYLHHAKWSQAAPMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQEKKSVRGKGKGQKRKRKKSRYKSWSVYVGARCCLMPWSLPGPHPCGPCSERRKHLFVQDPQTCKCSCKNTDSRCKARQLELNERTCRCDKPRR | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 77 (in isoform 12) | Phosphorylation | - | 5.05 | - | |
| 77 (in isoform 14) | Phosphorylation | - | 5.05 | - | |
| 77 (in isoform 13) | Phosphorylation | - | 5.05 | - | |
| 77 (in isoform 17) | Phosphorylation | - | 5.05 | - | |
| 77 (in isoform 16) | Phosphorylation | - | 5.05 | - | |
| 77 (in isoform 11) | Phosphorylation | - | 5.05 | - | |
| 77 (in isoform 18) | Phosphorylation | - | 5.05 | - | |
| 77 (in isoform 15) | Phosphorylation | - | 5.05 | - | |
| 82 (in isoform 15) | Phosphorylation | - | 24.50 | - | |
| 82 (in isoform 11) | Phosphorylation | - | 24.50 | - | |
| 82 (in isoform 17) | Phosphorylation | - | 24.50 | - | |
| 82 (in isoform 16) | Phosphorylation | - | 24.50 | - | |
| 82 (in isoform 18) | Phosphorylation | - | 24.50 | - | |
| 82 (in isoform 14) | Phosphorylation | - | 24.50 | - | |
| 82 (in isoform 12) | Phosphorylation | - | 24.50 | - | |
| 82 (in isoform 13) | Phosphorylation | - | 24.50 | - | |
| 84 (in isoform 15) | Phosphorylation | - | 23.08 | - | |
| 84 (in isoform 17) | Phosphorylation | - | 23.08 | - | |
| 84 (in isoform 14) | Phosphorylation | - | 23.08 | - | |
| 84 (in isoform 13) | Phosphorylation | - | 23.08 | - | |
| 84 (in isoform 18) | Phosphorylation | - | 23.08 | - | |
| 84 (in isoform 12) | Phosphorylation | - | 23.08 | - | |
| 84 (in isoform 11) | Phosphorylation | - | 23.08 | - | |
| 84 (in isoform 16) | Phosphorylation | - | 23.08 | - | |
| 85 (in isoform 14) | Phosphorylation | - | 19.21 | - | |
| 85 (in isoform 12) | Phosphorylation | - | 19.21 | - | |
| 85 (in isoform 15) | Phosphorylation | - | 19.21 | - | |
| 85 (in isoform 13) | Phosphorylation | - | 19.21 | - | |
| 85 (in isoform 17) | Phosphorylation | - | 19.21 | - | |
| 85 (in isoform 11) | Phosphorylation | - | 19.21 | - | |
| 85 (in isoform 18) | Phosphorylation | - | 19.21 | - | |
| 85 (in isoform 16) | Phosphorylation | - | 19.21 | - | |
| 101 | N-linked_Glycosylation | CVPTEESNITMQIMR CCCCCCCCEEEEEEE | 36.71 | UniProtKB CARBOHYD | |
| 118 (in isoform 15) | Phosphorylation | - | 23.56 | 24719451 | |
| 118 (in isoform 14) | Phosphorylation | - | 23.56 | 24719451 | |
| 118 (in isoform 16) | Phosphorylation | - | 23.56 | 24719451 | |
| 118 (in isoform 13) | Phosphorylation | - | 23.56 | 24719451 | |
| 118 (in isoform 18) | Phosphorylation | - | 23.56 | 24719451 | |
| 118 (in isoform 12) | Phosphorylation | - | 23.56 | 24719451 | |
| 118 (in isoform 11) | Phosphorylation | - | 23.56 | 24719451 | |
| 118 (in isoform 17) | Phosphorylation | - | 23.56 | 24719451 | |
| 147 | Acetylation | EKKSVRGKGKGQKRK HHHHHCCCCCCCCCC | 47.05 | 19666589 | |
| 149 | Acetylation | KSVRGKGKGQKRKRK HHHCCCCCCCCCCCC | 62.75 | 19666589 | |
| 152 | Acetylation | RGKGKGQKRKRKKSR CCCCCCCCCCCCHHH | 69.43 | 16916647 | |
| 154 | Acetylation | KGKGQKRKRKKSRYK CCCCCCCCCCHHHCC | 75.50 | 19666589 | |
| 162 (in isoform 17) | Phosphorylation | - | 18.69 | 30624053 | |
| 162 (in isoform 16) | Phosphorylation | - | 18.69 | 30624053 | |
| 162 (in isoform 15) | Phosphorylation | - | 18.69 | 30624053 | |
| 162 (in isoform 14) | Phosphorylation | - | 18.69 | 30624053 | |
| 162 (in isoform 13) | Phosphorylation | - | 18.69 | 30624053 | |
| 162 (in isoform 12) | Phosphorylation | - | 18.69 | 30624053 | |
| 162 (in isoform 18) | Phosphorylation | - | 18.69 | 30624053 | |
| 162 (in isoform 11) | Phosphorylation | - | 18.69 | 30624053 | |
| 166 | Phosphorylation | RYKSWSVYVGARCCL HCCHHHHEECCEEEE | 6.40 | - |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of VEGFA_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of VEGFA_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of VEGFA_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| VGFR2_HUMAN | KDR | physical | 12716911 | |
| VEGFA_HUMAN | VEGFA | physical | 12086892 | |
| CTGF_HUMAN | CTGF | physical | 11744618 | |
| VEGFA_HUMAN | VEGFA | physical | 8631822 | |
| GPC1_HUMAN | GPC1 | physical | 10196157 | |
| VEGFA_HUMAN | VEGFA | physical | 9207067 | |
| HS90A_HUMAN | HSP90AA1 | physical | 18211808 | |
| HSP74_HUMAN | HSPA4 | physical | 18211808 | |
| CRYAB_HUMAN | CRYAB | physical | 21984182 | |
| VGFR3_MOUSE | Flt4 | physical | 9012504 | |
| VGFR2_HUMAN | KDR | physical | 18325345 | |
| NRP1_HUMAN | NRP1 | physical | 18325345 | |
| LYVE1_HUMAN | LYVE1 | physical | 7829517 | |
| VGFR2_HUMAN | KDR | physical | 16423422 | |
| NRP1_HUMAN | NRP1 | physical | 16423422 | |
| VGFR1_HUMAN | FLT1 | physical | 21939755 | |
| NRP1_HUMAN | NRP1 | physical | 21939755 | |
| VPS35_HUMAN | VPS35 | physical | 21988832 | |
| VGFR2_HUMAN | KDR | physical | 25644401 | |
| PTPRB_HUMAN | PTPRB | physical | 25644401 | |
| PTPRZ_HUMAN | PTPRZ1 | physical | 25644401 | |
| CLUS_HUMAN | CLU | physical | 26716898 | |
| VHL_HUMAN | VHL | genetic | 28319113 | |
| VGFR1_HUMAN | FLT1 | physical | 28514442 | |
| ACTBL_HUMAN | ACTBL2 | physical | 28514442 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 603933 | Microvascular complications of diabetes 1 (MVCD1) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-147; LYS-149 AND LYS-152,AND MASS SPECTROMETRY. | |
