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UniProtKB/Swiss-Prot Q9BYC5: Variant p.Arg337Gly

Alpha-(1,6)-fucosyltransferase
Gene: FUT8
Chromosomal location: 14q24.3
Variant information

Variant position:  337
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 Arginine (R) to Glycine (G) at position 337 (R337G, p.Arg337Gly).
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 large size and basic (R) to glycine (G)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -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

Involvement in disease:  Congenital disorder of glycosylation with defective fucosylation (CDGF) [MIM:618005]: A form of congenital disorder of glycosylation, a genetically heterogeneous group of multisystem disorders caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions. CDGF is an autosomal recessive disorder, apparent from birth, characterized by poor growth, failure to thrive, hypotonia, skeletal anomalies, and delayed psychomotor development with intellectual disability. {ECO:0000269|PubMed:29304374}. 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 CDGF; drastic decrease of protein level in patient's fibroblasts and complete loss of total core fucosylated N-glycans in serum and fibroblasts compared to controls.
Any additional useful information about the variant.



Sequence information

Variant position:  337
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  575
The length of the canonical sequence.

Location on the sequence:   VRVHGDPAVWWVSQFVKYLI  R PQPWLEKEIEEATKKLGFKH
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                         VRVHGDPAVWWVSQFVKYLIRPQPWLEKEIEEATKKLGFKH-

                              VRVHGDPAVWWVSQFVKYLIRPQPWLEKEIEEATKKLGFNI

Chimpanzee                    VRVHGDPAVWWVSQFVKYLIRPQPWLEKEIEEATKKLGFKH

Mouse                         LRVHGDPAVWWVSQFVKYLIRPQPWLEKEIEEATKKLGFKH

Rat                           VRVHGDPAVWWVSQFVKYLIRPQPWLEKEIEEATKKLGFKH

Pig                           VRVHGDPAVWWVSQFVKYLIRPQPWLEKEIEEATKKLGFKH

Bovine                        VRVHGDPAVWWVSQFVKYLIRPQPWLEKEIEEATKKLGFKH

Xenopus tropicalis            IRLHGDPAVWWVSQFVKYLIRPQPWLEKEIEESTKKLGFKH

Caenorhabditis elegans        TSLHSHPPAFFVGTFISYLMRFNSATQEKLDKALKSIPLDK

Drosophila                    KRLHGDPIVWWVGQFLKYLLRPQPTTRDFLTSGMRNLGWER

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.

TypePositionsDescription
Chain 1 – 575 Alpha-(1,6)-fucosyltransferase
Topological domain 31 – 575 Lumenal
Domain 206 – 493 GT23
Alternative sequence 15 – 420 Missing. In isoform 4.
Alternative sequence 330 – 575 Missing. In isoform 2.


Literature citations

Biallelic Mutations in FUT8 Cause a Congenital Disorder of Glycosylation with Defective Fucosylation.
Ng B.G.; Xu G.; Chandy N.; Steyermark J.; Shinde D.N.; Radtke K.; Raymond K.; Lebrilla C.B.; AlAsmari A.; Suchy S.F.; Powis Z.; Faqeih E.A.; Berry S.A.; Kronn D.F.; Freeze H.H.;
Am. J. Hum. Genet. 102:188-195(2018)
Cited for: INVOLVEMENT IN CDGF; VARIANTS CDGF 239-ARG--LYS-575 DEL; 315-ARG--LYS-557 DEL AND GLY-337; FUNCTION; CHARACTERIZATION OF VARIANTS CDGF 239-ARG--LYS-575 DEL; 315-ARG--LYS-557? DEL AND GLY-337;

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.