Sequence information
Variant position: 693 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 972 The length of the canonical sequence.
Location on the sequence:
NFLRRKAEAMLGPSLSPGQD
P EGGVDYKNIHLEKKYVRRDS
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 NFLRRKAEAMLGPSLSPGQDP EGGVDYKNIHLEKKYVRRDS
Mouse NFLRRKAEAMLGPSLSPGQDS EGDSSYKNIHLEKKYVRRDS
Rat NFLRRKAEAMLGPSLSPGQDS EGDSSYKNIHLEKKYVRRDS
Cat NFLRRQAEAMLGPSLSVGQDP EAGAGYKNIHLEKKYVRRDS
Zebrafish NFLRSKAENFLNFVMTIPNFP EPMTDYKNVSTERMFVRSDS
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
20 – 972
Macrophage colony-stimulating factor 1 receptor
Topological domain
539 – 972
Cytoplasmic
Domain
582 – 910
Protein kinase
Modified residue
699 – 699
Phosphotyrosine; by autocatalysis
Modified residue
708 – 708
Phosphotyrosine; by autocatalysis
Modified residue
713 – 713
Phosphoserine
Alternative sequence
307 – 972
Missing. In isoform 2.
Mutagenesis
708 – 708
Y -> F. Impairs degradation of activated CSF1R.
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] GLY-32; ARG-362; SER-413; VAL-536; HIS-693; ASP-920 AND GLN-921;
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.