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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q96IJ6: Variant p.Arg390Pro

Mannose-1-phosphate guanylyltransferase regulatory subunit alpha
Gene: GMPPA
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Variant information Variant position: help 390 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 Proline (P) at position 390 (R390P, p.Arg390Pro). 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 medium size and hydrophobic (P) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 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 AAMR; drastically reduced protein expression. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 390 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 420 The length of the canonical sequence.
Location on the sequence: help DSESLFKDGKLLPAITILGC R VRIPAEVLILNSIVLPHKEL 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                         DSESLFKDGKLLPAITILGCRVRIPAEVLILNSIVLPHKEL

Mouse                         DSESLFKDGKLLPAITILGCRVRIPAEVLILNSIVLPHKEL

Rat                           DSESLFKDGKLLPAITILGCRVRIPAEVLILNSIVLPHKEL

Pig                           DSESLFKDGKLLPAITILGCRVRIPAEVLILNSIVLPHKEL

Xenopus tropicalis            DSETLFREGKLTPSITILGCNVSIPAEVVILNSIVLPHKEL

Slime mold                    ----LYSQDK-RRGVTIFGAGAQANGEIIVSNCIVMPHKQL
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 – 420 Mannose-1-phosphate guanylyltransferase regulatory subunit alpha
Region 273 – 420 Hexapeptide repeat domain
Mutagenesis 372 – 372 E -> A. Reduces the efficiency of GMPPB allosteric inhibition.
Mutagenesis 372 – 372 E -> R. Disrupts the interaction with other GMPPA molecules slightly but not with GMPPB.
Mutagenesis 396 – 396 E -> R. Disrupts the interaction with other GMPPA molecules but not with GMPPB.
Mutagenesis 408 – 408 K -> E. Does not disrupt the interaction with GMPPB or other GMPPA molecules.



Literature citations
Mutations in GMPPA cause a glycosylation disorder characterized by intellectual disability and autonomic dysfunction.
Koehler K.; Malik M.; Mahmood S.; Giesselmann S.; Beetz C.; Hennings J.C.; Huebner A.K.; Grahn A.; Reunert J.; Nurnberg G.; Thiele H.; Altmuller J.; Nurnberg P.; Mumtaz R.; Babovic-Vuksanovic D.; Basel-Vanagaite L.; Borck G.; Bramswig J.; Muhlenberg R.; Sarda P.; Sikiric A.; Anyane-Yeboa K.; Zeharia A.; Ahmad A.; Coubes C.; Wada Y.; Marquardt T.; Vanderschaeghe D.; Van Schaftingen E.; Kurth I.; Huebner A.; Hubner C.A.;
Am. J. Hum. Genet. 93:727-734(2013)
Cited for: VARIANTS AAMR ASP-182; MET-334; PRO-334; PRO-390 AND THR-401; FUNCTION; SUBCELLULAR LOCATION; TISSUE SPECIFICITY;
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.