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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P35916: Variant p.Asp1049Asn

Vascular endothelial growth factor receptor 3
Gene: FLT4
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Variant information Variant position: help 1049 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LB/B The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance

Residue change: help From Aspartate (D) to Asparagine (N) at position 1049 (D1049N, p.Asp1049Asn). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Change from medium size and acidic (D) to medium size and polar (N) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 1 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page

Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 1049 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1363 The length of the canonical sequence.
Location on the sequence: help ASRKCIHRDLAARNILLSES D VVKICDFGLARDIYKDPDYV The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: help The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human                         ASRKCIHRDLAARNILLSESDVVKICDFGLARDIYKDPDYV

Mouse                         ASRKCIHRDLAARNILLSESDIVKICDFGLARDIYKDPDYV

Rat                           ASRKCIHRDLAARNILLSESDIVKICDFGLARDIYKDPDYV

Zebrafish                     ASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDYV

Sequence annotation in neighborhood: help The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
  • Type: the type of sequence feature.
  • Positions: endpoints of the sequence feature.
  • Description: contains additional information about the feature.
TypePositionsDescription
Chain 25 – 1363 Vascular endothelial growth factor receptor 3
Topological domain 797 – 1363 Cytoplasmic
Domain 845 – 1173 Protein kinase
Active site 1037 – 1037 Proton acceptor
Modified residue 1063 – 1063 Phosphotyrosine; by autocatalysis and SRC
Modified residue 1068 – 1068 Phosphotyrosine; by autocatalysis
Alternative sequence 766 – 1298 Missing. In isoform 3.
Mutagenesis 1063 – 1063 Y -> F. Loss of phosphorylation site. No effect on stimulation of cell proliferation and cell migration.
Mutagenesis 1068 – 1068 Y -> F. Global loss of autophosphorylation. Abolishes stimulation of cell proliferation and cell migration.



Literature citations
Patterns of somatic mutation in human cancer genomes.
Greenman C.; Stephens P.; Smith R.; Dalgliesh G.L.; Hunter C.; Bignell G.; Davies H.; Teague J.; Butler A.; Stevens C.; Edkins S.; O'Meara S.; Vastrik I.; Schmidt E.E.; Avis T.; Barthorpe S.; Bhamra G.; Buck G.; Choudhury B.; Clements J.; Cole J.; Dicks E.; Forbes S.; Gray K.; Halliday K.; Harrison R.; Hills K.; Hinton J.; Jenkinson A.; Jones D.; Menzies A.; Mironenko T.; Perry J.; Raine K.; Richardson D.; Shepherd R.; Small A.; Tofts C.; Varian J.; Webb T.; West S.; Widaa S.; Yates A.; Cahill D.P.; Louis D.N.; Goldstraw P.; Nicholson A.G.; Brasseur F.; Looijenga L.; Weber B.L.; Chiew Y.-E.; DeFazio A.; Greaves M.F.; Green A.R.; Campbell P.; Birney E.; Easton D.F.; Chenevix-Trench G.; Tan M.-H.; Khoo S.K.; Teh B.T.; Yuen S.T.; Leung S.Y.; Wooster R.; Futreal P.A.; Stratton M.R.;
Nature 446:153-158(2007)
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASP-149; CYS-378; ALA-494; SER-527; SER-641; TYR-868; ILE-1010; GLN-1031; ASN-1049; GLN-1075 AND HIS-1146;
Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.