Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9Y5P6: Variant p.Asn322Lys

Mannose-1-phosphate guanylyltransferase catalytic subunit beta
Gene: GMPPB
Feedback?
Variant information Variant position: help 322 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 Asparagine (N) to Lysine (K) at position 322 (N322K, p.Asn322Lys). 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 (N) to large size and basic (K) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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 MDDGC14; no change in protein abundance. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 322 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 360 The length of the canonical sequence.
Location on the sequence: help WLESCIVGWRCRVGQWVRME N VTVLGEDVIVNDELYLNGAS 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                         WLESCIVGWRCRVGQWVRMENVTVLGEDVIVNDELYLNGAS

Mouse                         WLESCIVGWRCRVGQWVRMENVTVLGEDVIVNDELYLNGAS

Pig                           WLESCIVCWRCRVGQWVRMENVTVLGEDVIVNDELYLNGAS

Bovine                        WLESCIVGWRCRVGQWVRMENVTVLGEDVIVNDELYLNGAS

Xenopus tropicalis            WLESSIVGWSSSVGQWVRMENVTVLGEDVIVNDELYLNGAN

Zebrafish                     WLESCIVGWSSSVGQWVRMENVTVLGEDVIVNDELYINGAN

Caenorhabditis elegans        WVSGSIVGRKCHIGSWVRIENICVIGDDVVVKDELYLNGAS

Drosophila                    WLDSCIVGWRSTVGRWVRIEGITVLGEDVIVKDELYINGGQ

Slime mold                    WIKSTIIGWNSSIGKWVRMENTSVLGEDVHVSDELYINGGK
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 – 360 Mannose-1-phosphate guanylyltransferase catalytic subunit beta
Region 245 – 360 Hexapeptide repeat domain
Alternative sequence 317 – 317 W -> WVSLWAGLGGERGGECACLPDKAYPLLE. In isoform 2.
Mutagenesis 303 – 303 L -> F. Reduces interaction with GMPPB but not with GMPPA.
Mutagenesis 335 – 335 E -> R. Disrupted interaction with GMPPA and other GMPPB molecules.
Beta strand 319 – 323



Literature citations
Novel mutations in the C-terminal region of GMPPB causing limb-girdle muscular dystrophy overlapping with congenital syndrome.
Luo S.; Cai S.; Maxwell S.; Yue D.; Zhu W.; Qiao K.; Zhu Z.; Zhou L.; Xi J.; Lu J.; Beeson D.; Zhao C.;
Neuromuscul. Disord. 27:557-564(2017)
Cited for: VARIANTS MDDGC14 TRP-293; LYS-322; ARG-340 AND HIS-357; CHARACTERIZATION OF VARIANTS MDDGC14 TRP-293; LYS-322; ARG-340 AND HIS-357;
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.