Sequence information
Variant position: 641 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:
KCIHRDLAARNVLVTENNVM
K IADFGLARDINNIDYYKKTT
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 KCIHRDLAARNVLVTENNVMK IADFGLARDINNIDYYKKTT
Mouse KCIHRDLAARNVLVTENNVMK IADFGLARDINNIDYYKKTT
Chicken KCIHRDLAARNVLVTENNVMK IADFGLARDINNIDYYKKTT
Xenopus laevis KCIHRDLAARNVLVTENNVMK IADFGLARDVNNIDYYKKTS
Zebrafish KCIHRDLAARNVLVTESNVMK IADFGLARDVHNIDYYKKTT
Drosophila RCIHRDLAARNVLVSDGYVMK IADFGLARDIQDTEYYRKNT
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.
Type Positions Description
Chain
22 – 821
Fibroblast growth factor receptor 2
Topological domain
399 – 821
Cytoplasmic
Domain
481 – 770
Protein kinase
Active site
626 – 626
Proton acceptor
Modified residue
656 – 656
Phosphotyrosine; by autocatalysis
Modified residue
657 – 657
Phosphotyrosine; by autocatalysis
Alternative sequence
255 – 821
Missing. In isoform 8.
Alternative sequence
366 – 821
Missing. In isoform 13.
Beta strand
640 – 642
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;
Genomic screening of fibroblast growth-factor receptor 2 reveals a wide spectrum of mutations in patients with syndromic craniosynostosis.
Kan S.-H.; Elanko N.; Johnson D.; Cornejo-Roldan L.R.; Cook J.; Reich E.W.; Tomkins S.; Verloes A.; Twigg S.R.F.; Rannan-Eliya S.; McDonald-McGinn D.M.; Zackai E.H.; Wall S.A.; Muenke M.; Wilkie A.O.M.;
Am. J. Hum. Genet. 70:472-486(2002)
Cited for: VARIANTS CS CYS-105; PRO-267; VAL-276; CYS-281; PRO-289; ARG-338; HIS-340; PHE-342; TRP-342; CYS-347; CYS-354; HIS-549 AND GLY-678; VARIANTS PS PHE-172; 252-PHE-SER-253; CYS-290; CYS-340; PRO-341; ARG-342; SER-342; CYS-375; GLY-565; ARG-641 AND GLU-663; VARIANTS APRS TRP-252 AND ARG-253; VARIANTS CS/PS PHE-278 AND TYR-342; VARIANT CRANIOSYNOSTOSIS ASN-659; VARIANTS THR-186 AND SER-315;
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.