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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P21802: Variant p.Lys526Glu

Fibroblast growth factor receptor 2
Gene: FGFR2
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Variant information Variant position: help 526 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] 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 Lysine (K) to Glutamate (E) at position 526 (K526E, p.Lys526Glu). 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 large size and basic (K) to medium size and acidic (E) 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
Variant description: help In FSPC; constitutive kinase activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 526 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 821 The length of the canonical sequence.
Location on the sequence: help DKPKEAVTVAVKMLKDDATE K DLSDLVSEMEMMKMIGKHKN 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                         DKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKN

Mouse                         DKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKN

Chicken                       DRPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKN

Xenopus laevis                ERPKESVTVAVKMLKDNATEKDLADLVSEMEMMKMIGKHKN

Zebrafish                     DKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGRHKN

Drosophila                    SPQLAETIVAVKMVKEEHTDTDMASLVREMEVMKMIGKHIN
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 22 – 821 Fibroblast growth factor receptor 2
Topological domain 399 – 821 Cytoplasmic
Domain 481 – 770 Protein kinase
Binding site 517 – 517
Alternative sequence 255 – 821 Missing. In isoform 8.
Alternative sequence 366 – 821 Missing. In isoform 13.
Helix 525 – 541



Literature citations
A molecular brake in the kinase hinge region regulates the activity of receptor tyrosine kinases.
Chen H.; Ma J.; Li W.; Eliseenkova A.V.; Xu C.; Neubert T.A.; Miller W.T.; Mohammadi M.;
Mol. Cell 27:717-730(2007)
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 458-778 IN COMPLEX WITH ATP ANALOG; PEPTIDE SUBSTRATE AND MAGNESIUM; ACTIVITY REGULATION; PHOSPHORYLATION AT TYR-586; TYR-656 AND TYR-657; MUTAGENESIS OF ASN-549 AND GLU-565; CHARACTERIZATION OF VARIANT FSPC GLU-526; CHARACTERIZATION OF VARIANT CS HIS-549; CHARACTERIZATION OF VARIANTS PS GLY-565 AND ARG-641; CHARACTERIZATION OF VARIANT CRANIOSYNOSTOSIS ASN-659; Familial scaphocephaly syndrome caused by a novel mutation in the FGFR2 tyrosine kinase domain.
McGillivray G.; Savarirayan R.; Cox T.C.; Stojkoski C.; McNeil R.; Bankier A.; Bateman J.F.; Roscioli T.; Gardner R.J.M.; Lamande S.R.;
J. Med. Genet. 42:656-662(2005)
Cited for: VARIANT FSPC GLU-526;
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.