Sequence information
Variant position: 526 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 821 The length of the canonical sequence.
Location on the sequence:
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: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human DKPKEAVTVAVKMLKDDATEK DLSDLVSEMEMMKMIGKHKN
Mouse DKPKEAVTVAVKMLKDDATEK DLSDLVSEMEMMKMIGKHKN
Chicken DRPKEAVTVAVKMLKDDATEK DLSDLVSEMEMMKMIGKHKN
Xenopus laevis ERPKESVTVAVKMLKDNATEK DLADLVSEMEMMKMIGKHKN
Zebrafish DKPKEAVTVAVKMLKDDATEK DLSDLVSEMEMMKMIGRHKN
Drosophila SPQLAETIVAVKMVKEEHTDT DMASLVREMEVMKMIGKHIN
Sequence annotation in neighborhood: 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.
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.