UniProtKB/Swiss-Prot Q9Y5P6: Variant p.Asp27His

Mannose-1-phosphate guanylyltransferase catalytic subunit beta
Gene: GMPPB
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Variant information Variant position:

27 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

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:

From Aspartate (D) to Histidine (H) at position 27 (D27H, p.Asp27His). 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:

Change from medium size and acidic (D) to medium size and polar (H) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-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:

In MDDGC14; the protein remains distributed in the cytoplasm and has no discernable changes compared to wild-type; reduces catalytic activity. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs142336618 [ dbSNP | Ensembl ]

Sequence information Variant position:

27 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

360 The length of the canonical sequence.
Location on the sequence:

VGGYGTRLRPLTLSTPKPLV D FCNKPILLHQVEALAAAGVD 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:

The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         VGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVD

Mouse                         VGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVD

Pig                           VGGYGTRLRPLTLSIPKPLVDFCNKPILLHQVEALASAGVD

Bovine                        VGGYGTRLRPLTLSIPKPLADFCNKPILLHQVEALAAAGVD

Xenopus tropicalis            VGGYGTRLRPLTLSVPKPLVDFCNKPILLHQVEALVKAGVN

Zebrafish                     VGGYGTRLRPLTLTVPKPLVEFCNKPILLHQVEALVKAGVR

Caenorhabditis elegans        VGGYGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAEVGVD

Drosophila                    VGGYGTRLRPLTLSTPKPLVEFANKPILLHQLEALVDAGCR

Slime mold                    VGGFGTRLRPLTLSKPKPIVEFANKAMILHQIEALCKIGVN

Sequence annotation in neighborhood:

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.

Type	Positions	Description
Chain	1 – 360	Mannose-1-phosphate guanylyltransferase catalytic subunit beta
Region	2 – 222	Substrate-binding domain
Beta strand	26 – 32

Literature citations
Cryo-EM structures of human GMPPA-GMPPB complex reveal how cells maintain GDP-mannose homeostasis.
Zheng L.; Liu Z.; Wang Y.; Yang F.; Wang J.; Huang W.; Qin J.; Tian M.; Cai X.; Liu X.; Mo X.; Gao N.; Jia D.;
Nat. Struct. Mol. Biol. 28:1-12(2021)
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) OF 1-420 IN COMPLEXES WITH GMPPB; MG2+; GTP AND GDP-MANNOSE; FUNCTION; CATALYTIC ACTIVITY; COFACTOR MG; ACTIVITY REGULATION; BIOPHYSICOCHEMICAL PROPERTIES; PATHWAY; SUBUNIT; DOMAIN; ACTIVE SITE; CHARACTERIZATION OF VARIANT MDDGA14 ASN-334; CHARACTERIZATION OF VARIANT MDDGB14 LEU-32; CHARACTERIZATION OF VARIANT MDDGC14 SER-22; HIS-27; THR-219; TRP-293 AND HIS-357; MUTAGENESIS OF ILE-193; ASP-218; CYS-266; ARG-287; LEU-303; GLU-335; 344-LEU--LYS-347 AND 358-ILE--MET-360; Mutations in GDP-mannose pyrophosphorylase B cause congenital and limb-girdle muscular dystrophies associated with hypoglycosylation of alpha-dystroglycan.
Carss K.J.; Stevens E.; Foley A.R.; Cirak S.; Riemersma M.; Torelli S.; Hoischen A.; Willer T.; van Scherpenzeel M.; Moore S.A.; Messina S.; Bertini E.; Boennemann C.G.; Abdenur J.E.; Grosmann C.M.; Kesari A.; Punetha J.; Quinlivan R.; Waddell L.B.; Young H.K.; Wraige E.; Yau S.; Brodd L.; Feng L.; Sewry C.; MacArthur D.G.; North K.N.; Hoffman E.; Stemple D.L.; Hurles M.E.; van Bokhoven H.; Campbell K.P.; Lefeber D.J.; Lin Y.Y.; Muntoni F.;
Am. J. Hum. Genet. 93:29-41(2013)
Cited for: SUBCELLULAR LOCATION; TISSUE SPECIFICITY (ISOFORMS 1 AND 2); DEVELOPMENTAL STAGE (ISOFORM 2); VARIANT MDDGA14 ASN-334; VARIANTS MDDGB14 LEU-32; CYS-185 AND GLN-287; VARIANTS MDDGC14 SER-22; HIS-27 AND ILE-330; CHARACTERIZATION OF VARIANT MDDGA14 ASN-334; CHARACTERIZATION OF VARIANTS MDDGB14 LEU-32; CYS-185 AND GLN-287; CHARACTERIZATION OF VARIANTS MDDGC14 SER-22; HIS-27 AND ILE-330; GMPPB-associated dystroglycanopathy: Emerging common variants with phenotype correlation.
Jensen B.S.; Willer T.; Saade D.N.; Cox M.O.; Mozaffar T.; Scavina M.; Stefans V.A.; Winder T.L.; Campbell K.P.; Moore S.A.; Mathews K.D.;
Hum. Mutat. 36:1159-1163(2015)
Cited for: VARIANTS MDDGC14 HIS-27; SER-32; CYS-132; THR-219; SER-241; MET-254; GLN-287; TRP-287; ALA-318 AND ILE-330; Late-onset limb-girdle muscular dystrophy caused by GMPPB mutations.
Balcin H.; Palmio J.; Penttilae S.; Nennesmo I.; Lindfors M.; Solders G.; Udd B.;
Neuromuscul. Disord. 27:627-630(2017)
Cited for: VARIANTS MDDGC14 HIS-27 AND TRP-287;

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.