Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q8IXL6: Variant p.Pro328Ser

Extracellular serine/threonine protein kinase FAM20C
Gene: FAM20C
Feedback?
Variant information Variant position: help 328 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 Proline (P) to Serine (S) at position 328 (P328S, p.Pro328Ser). 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 medium size and hydrophobic (P) to small size and polar (S) 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 RNS; mild non-lethal form; decreased protein kinase activity; FAM20A is still able to increase remaining protein 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 328 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 HNAEIAAFHLDRILDFRRVP P VAGRMVNMTKEIRDVTRDKK 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                         HNAEIAAFHLDRILDFRRVPPVAGRMVNMTKEIRDVTRDKK

Mouse                         HNAEIAAFHLDRILDFRRVPPVAGRMINMTKEIRDVTRDKK

Caenorhabditis elegans        HHAEIATFHLDRVLGFRRAIPTVGRVLNMTTELFEKA-EKK

Drosophila                    HNAEIAAFHLDRILGFRRAMPVAGRTLNITTEIYQLA-EEN
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
Glycosylation 335 – 335 N-linked (GlcNAc...) asparagine
Alternative sequence 1 – 332 Missing. In isoform 2.
Mutagenesis 311 – 311 E -> A. Reduced kinase activity.
Mutagenesis 335 – 335 N -> A. Impaired secretion; when associated with A-101 and A-470.



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; A secretory kinase complex regulates extracellular protein phosphorylation.
Cui J.; Xiao J.; Tagliabracci V.S.; Wen J.; Rahdar M.; Dixon J.E.;
Elife 4:0-0(2015)
Cited for: FUNCTION; CATALYTIC ACTIVITY; ACTIVITY REGULATION; INTERACTION WITH FAM20A; MUTAGENESIS OF GLU-306 AND ASP-478; VARIANTS RNS MET-268 AND SER-328; CHARACTERIZATION OF VARIANTS RNS MET-268 AND SER-328;
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.