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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q8IXL6: Variant p.Arg549Trp

Extracellular serine/threonine protein kinase FAM20C
Gene: FAM20C
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Variant information Variant position: help 549 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 Arginine (R) to Tryptophan (W) at position 549 (R549W, p.Arg549Trp). 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 (R) to large size and aromatic (W) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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 RNS. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 549 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 584 The length of the canonical sequence.
Location on the sequence: help LRGDQVAPVLYQPHLEALDR R LRVVLKAVRDCVERNGLHSV 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                         LRGDQVAPVLYQPHLEALDRRLRVVLKAVRDCVERNGLHSV---------------

Mouse                         LQHDKVAPVLYQLHLEALDRRLRIVLQAVRDCVEKDGLSSV

Caenorhabditis elegans        LSKDPAHPILAYKHYPAMERRLAKIMSHILECFESRGVAEV

Drosophila                    LSQDPVSPVLWQPHLEALDRRTGIILQSIRDCIKRNPPGDV
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 93 – 584 Extracellular serine/threonine protein kinase FAM20C
Topological domain 32 – 584 Lumenal
Region 354 – 565 Kinase domain
Disulfide bond 501 – 560
Helix 540 – 564



Literature citations
Secreted kinase phosphorylates extracellular proteins that regulate biomineralization.
Tagliabracci V.S.; Engel J.L.; Wen J.; Wiley S.E.; Worby C.A.; Kinch L.N.; Xiao J.; Grishin N.V.; Dixon J.E.;
Science 336:1150-1153(2012)
Cited for: FUNCTION; CATALYTIC ACTIVITY; MANGANESE-BINDING; MUTAGENESIS OF ASP-478; VARIANTS RNS ASN-258; ARG-280; SER-328; ARG-379; GLU-379; ARG-388; ASN-451 AND TRP-549; CHARACTERIZATION OF VARIANTS RNS SER-328 AND ASN-451; Mutations in FAM20C are associated with lethal osteosclerotic bone dysplasia (Raine syndrome), highlighting a crucial molecule in bone development.
Simpson M.A.; Hsu R.; Keir L.S.; Hao J.; Sivapalan G.; Ernst L.M.; Zackai E.H.; Al-Gazali L.I.; Hulskamp G.; Kingston H.M.; Prescott T.E.; Ion A.; Patton M.A.; Murday V.; George A.; Crosby A.H.;
Am. J. Hum. Genet. 81:906-912(2007)
Cited for: VARIANTS RNS ARG-379; GLU-379; ARG-388 AND TRP-549;
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.