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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot A6NI61: Variant p.Cys185Arg

Protein myomaker
Gene: MYMK
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Variant information Variant position: help 185 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 Cysteine (C) to Arginine (R) at position 185 (C185R, p.Cys185Arg). 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 polar (C) to large size and basic (R) 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 CFZS1; loss of localization at the plasma membrane; loss of cell fusion in a heterologous cell fusion assay in vitro; no rescue of mymk knockout fish; primary myoblasts from a compound heterozygote associating T-91 and R-185 exhibit no difference in their capability to differentiate compared to control myoblasts, but show a significant difference in the fusion index, with a higher percentage of singly-nucleated relative to multinucleated cells in compound heterozygous compared to control myoblasts. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 185 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 221 The length of the canonical sequence.
Location on the sequence: help LMLRFFFEDWDYTYVHSFYH C ALAMSFVLLLPKVNKKAGSP 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                         LMLRFFFEDWDYTYVHSFYHCALAMSFVLLLPKVNKKAGSP

Mouse                         LMLRFFFEEWDYTYVHSFYHCALAMSFVLLLPKVNKKAGNA

Zebrafish                     LMLRFYFEEWDYAYVHSFYHVSLAMSFILLLPKKNRYAGTG
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 1 – 221 Protein myomaker
Topological domain 175 – 175 Extracellular
Transmembrane 176 – 196 Helical



Literature citations
A defect in myoblast fusion underlies Carey-Fineman-Ziter syndrome.
Di Gioia S.A.; Connors S.; Matsunami N.; Cannavino J.; Rose M.F.; Gilette N.M.; Artoni P.; de Macena Sobreira N.L.; Chan W.M.; Webb B.D.; Robson C.D.; Cheng L.; Van Ryzin C.; Ramirez-Martinez A.; Mohassel P.; Leppert M.; Scholand M.B.; Grunseich C.; Ferreira C.R.; Hartman T.; Hayes I.M.; Morgan T.; Markie D.M.; Fagiolini M.; Swift A.; Chines P.S.; Speck-Martins C.E.; Collins F.S.; Jabs E.W.; Boennemann C.G.; Olson E.N.; Carey J.C.; Robertson S.P.; Manoli I.; Engle E.C.;
Nat. Commun. 8:16077-16077(2017)
Cited for: VARIANTS CFZS1 THR-91; SER-100; THR-154 AND ARG-185; FUNCTION; SUBCELLULAR LOCATION;
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.