UniProtKB/Swiss-Prot Q9BT22: Variant p.Ser267Asn

Chitobiosyldiphosphodolichol beta-mannosyltransferase
Gene: ALG1
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Variant information Variant position:

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

LB/B 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 Serine (S) to Asparagine (N) at position 267 (S267N, p.Ser267Asn). 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 small size and polar (S) to medium size and polar (N) 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:

No effect on function in protein glycosylation. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs17849848 [ dbSNP | Ensembl ]

Sequence information Variant position:

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

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

RSEPEDPVTERSAFTERDAG S GLVTRLRERPALLVSSTSWT 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                         RSEPEDPVTERSAFTERDAGSGLVTRLRERPALLVSSTSWT

Mouse                         CSDPSHPDTERSAFTERDCQSGVVRRLHGRPALLVSSTSWT

Slime mold                    -----SIKGEDKVYIESVISKKSIRNPKQQTSIIISSTSWT

Baker's yeast                 ----DDFDTEKG------------------DKIIVTSTSFT

Fission yeast                 -----NPSS---------------------TKLLITSTSWT

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 – 464	Chitobiosyldiphosphodolichol beta-mannosyltransferase
Topological domain	24 – 464	Lumenal

Literature citations
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)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1); VARIANTS ASN-267; MET-325 AND ARG-455; ALG1-CDG: Clinical and Molecular Characterization of 39 Unreported Patients.
Ng B.G.; Shiryaev S.A.; Rymen D.; Eklund E.A.; Raymond K.; Kircher M.; Abdenur J.E.; Alehan F.; Midro A.T.; Bamshad M.J.; Barone R.; Berry G.T.; Brumbaugh J.E.; Buckingham K.J.; Clarkson K.; Cole F.S.; O'Connor S.; Cooper G.M.; Van Coster R.; Demmer L.A.; Diogo L.; Fay A.J.; Ficicioglu C.; Fiumara A.; Gahl W.A.; Ganetzky R.; Goel H.; Harshman L.A.; He M.; Jaeken J.; James P.M.; Katz D.; Keldermans L.; Kibaek M.; Kornberg A.J.; Lachlan K.; Lam C.; Yaplito-Lee J.; Nickerson D.A.; Peters H.L.; Race V.; Regal L.; Rush J.S.; Rutledge S.L.; Shendure J.; Souche E.; Sparks S.E.; Trapane P.; Sanchez-Valle A.; Vilain E.; Voello A.; Waechter C.J.; Wang R.Y.; Wolfe L.A.; Wong D.A.; Wood T.; Yang A.C.; Matthijs G.; Freeze H.H.;
Hum. Mutat. 37:653-660(2016)
Cited for: INVOLVEMENT IN CDG1K; FUNCTION; VARIANTS CDG1K ARG-50; PHE-71; LEU-74; VAL-88; LEU-98; PHE-114; ARG-150; SER-209; LEU-258; TRP-276; PHE-281; GLY-289; VAL-291; ASP-353; ARG-358; LEU-359; VAL-360; ALA-363; GLN-366; GLN-367; LYS-382; ARG-384; SER-388 AND TRP-438; CHARACTERIZATION OF VARIANTS CDG1K ARG-50; PHE-71; LEU-74; VAL-88; LEU-98; PHE-114; ARG-150; SER-209; LEU-258; TRP-276; PHE-281; GLY-289; VAL-291; ASP-353; ARG-358; LEU-359; VAL-360; ALA-363; GLN-366; GLN-367; LYS-382; ARG-384; SER-388 AND TRP-438; CHARACTERIZATION OF VARIANT ASN-267;

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.