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UniProtKB/Swiss-Prot P07902: Variant p.Asn314Asp

Galactose-1-phosphate uridylyltransferase
Gene: GALT
Variant information

Variant position:  314
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Disease [Disclaimer]
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Asparagine (N) to Aspartate (D) at position 314 (N314D, p.Asn314Asp).
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 polar (N) to medium size and acidic (D)
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

Involvement in disease:  Galactosemia (GALCT) [MIM:230400]: Inherited disorder of galactose metabolism that causes jaundice, cataracts, and mental retardation. {ECO:0000269|PubMed:10220154, ECO:0000269|PubMed:11754113, ECO:0000269|PubMed:11919338, ECO:0000269|PubMed:1373122, ECO:0000269|PubMed:1427861, ECO:0000269|PubMed:15841485, ECO:0000269|PubMed:1610789, ECO:0000269|PubMed:17041746, ECO:0000269|PubMed:17876724, ECO:0000269|PubMed:18956253, ECO:0000269|PubMed:1897530, ECO:0000269|PubMed:2011574, ECO:0000269|PubMed:22461411, ECO:0000269|PubMed:23022339, ECO:0000269|PubMed:25592817, ECO:0000269|PubMed:25614870, ECO:0000269|PubMed:27005423, ECO:0000269|PubMed:7550229, ECO:0000269|PubMed:7887416, ECO:0000269|PubMed:7887417, ECO:0000269|PubMed:8112740, ECO:0000269|PubMed:8499924, ECO:0000269|PubMed:8598637, ECO:0000269|PubMed:8741038, ECO:0000269|PubMed:8869397, ECO:0000269|PubMed:8956044, ECO:0000269|PubMed:9222760}. Note=The disease is caused by mutations affecting the gene represented in this entry.
The name and a short description of the disease associated with the variant. For more information about the disease, the user can refer to OMIM, following the link provided after the disease acronym.

Variant description:  In GALCT; allele Duarte; exists as allelic variants Duarte-1 and Duarte-2; Duarte-1 has normal or increased activity; Duarte-2 has activity reduced to about 35-45% of normal.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.

Sequence information

Variant position:  314
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  379
The length of the canonical sequence.

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.

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.

Chain 1 – 379 Galactose-1-phosphate uridylyltransferase
Metal binding 301 – 301 Zinc 2
Metal binding 319 – 319 Zinc 2
Metal binding 321 – 321 Zinc 2

Literature citations

Cloning of human full-length CDSs in BD Creator(TM) system donor vector.
Kalnine N.; Chen X.; Rolfs A.; Halleck A.; Hines L.; Eisenstein S.; Koundinya M.; Raphael J.; Moreira D.; Kelley T.; LaBaer J.; Lin Y.; Phelan M.; Farmer A.;

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
The MGC Project Team;
Genome Res. 14:2121-2127(2004)

Molecular basis of galactosemia: mutations and polymorphisms in the gene encoding human galactose-1-phosphate uridylyltransferase.
Reichardt J.K.V.; Woo S.L.C.;
Proc. Natl. Acad. Sci. U.S.A. 88:2633-2637(1991)

On the molecular nature of the Duarte variant of galactose-1-phosphate uridyl transferase (GALT).
Lin H.-C.; Kirby L.T.; Ng W.G.; Reichardt J.K.V.;
Hum. Genet. 93:167-169(1994)
Cited for: VARIANT GALCT ASP-314;

Molecular characterization of galactosemia (type 1) mutations in Japanese.
Ashino J.; Okano Y.; Suyama I.; Yamazaki T.; Yoshino M.; Furuyama J.; Lin H.-C.; Reichardt J.K.V.; Isshiki G.;
Hum. Mutat. 6:36-43(1995)

Molecular analysis in newborns from Texas affected with galactosemia.
Yang Y.P.; Corley N.; Garcia-Heras J.;
Hum. Mutat. 19:82-83(2002)
Cited for: VARIANTS GALCT ALA-23; LEU-135; MET-138; GLN-184; ARG-188; PRO-195; SER-251; ASN-285; LYS-344 AND ASP-345; VARIANT ASP-314;

Low allelic heterogeneity in a sample of Mexican patients with classical galactosaemia.
Velazquez-Aragon J.; Alcantara-Ortigoza M.A.; Vela-Amieva M.; Monroy S.; Martinez-Cruz V.; Todd-Quinones C.; Gonzalez-del Angel A.;
J. Inherit. Metab. Dis. 31:S333-S337(2008)

Biochemical and molecular characterization of GALT gene from Indian galactosemia patients: Identification of 10 novel mutations and their structural and functional implications.
Singh R.; Thapa B.R.; Kaur G.; Prasad R.;
Clin. Chim. Acta 414:191-196(2012)
Cited for: VARIANTS GALCT HIS-89; ARG-103; ALA-166; SER-171; PHE-181; LEU-185; ARG-188; ARG-285; GLN-319 AND LEU-333; VARIANT ASP-314;

Functional and structural impact of the most prevalent missense mutations in classic galactosemia.
Coelho A.I.; Trabuco M.; Ramos R.; Silva M.J.; Tavares de Almeida I.; Leandro P.; Rivera I.; Vicente J.B.;
Mol. Genet. Genomic Med. 2:484-496(2014)
Cited for: VARIANTS GALCT LEU-135; GLN-148; ASP-175; SER-185; ARG-188; CYS-231; HIS-231; ASN-285 AND ASP-314; CHARACTERIZATION OF VARIANTS GALCT LEU-135; ASP-175 AND ARG-188;

Clinical and molecular spectra in galactosemic patients from neonatal screening in northeastern Italy: Structural and functional characterization of new variations in the galactose-1-phosphate uridyltransferase (GALT) gene.
Viggiano E.; Marabotti A.; Burlina A.P.; Cazzorla C.; D'Apice M.R.; Giordano L.; Fasan I.; Novelli G.; Facchiano A.; Burlina A.B.;
Gene 559:112-118(2015)
Cited for: VARIANTS GALCT PRO-33; ASN-34; VAL-83; THR-142; ARG-188; SER-244; ARG-267; VAL-267; ASP-271; ASN-285; ASP-314 AND TRP-333;

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.