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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9H3H5: Variant p.Tyr170Cys

UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
Gene: DPAGT1
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Variant information Variant position: help 170 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 Tyrosine (Y) to Cysteine (C) at position 170 (Y170C, p.Tyr170Cys). 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 aromatic (Y) to medium size and polar (C) 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 CDG1J; strongly reduced enzyme activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 170 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 408 The length of the canonical sequence.
Location on the sequence: help VVPKPFRPILGLHLDLGILY Y VYMGLLAVFCTNAINILAGI 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                         VVPK-----PFRPILG-LHLDLGILYYVYMGLLAVFCTNAINILAGI

Mouse                         VVPK-----PFRWILG-LHLDLGILYYVYMGLLAVFCTNAI

Bovine                        VVPK-----PLRPILG-LHLDLGILYYVYMGLLAVFCTNAI

Slime mold                    VVPDINFPVPLREWLG-VVFDLGIFYRIYLLMLAIFCTNSI

Baker's yeast                 LIPG-----FMERWLKKTSVDLGLWYYVYMASMAIFCPNSI

Fission yeast                 SVPS-----IVRPFLKRSLINLGFLYYFYMAAVAIFCPNSI

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 – 408 UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
Transmembrane 167 – 186 Helical; Name=Helix 5
Binding site 185 – 185
Binding site 185 – 185
Mutagenesis 168 – 168 L -> P. Strongly reduced enzyme activity.
Mutagenesis 182 – 182 N -> A. Loss of enzyme activity.
Mutagenesis 185 – 185 N -> AD. Loss of enzyme activity.
Helix 167 – 186



Literature citations
Structures of DPAGT1 Explain Glycosylation Disease Mechanisms and Advance TB Antibiotic Design.
Dong Y.Y.; Wang H.; Pike A.C.W.; Cochrane S.A.; Hamedzadeh S.; Wyszynski F.J.; Bushell S.R.; Royer S.F.; Widdick D.A.; Sajid A.; Boshoff H.I.; Park Y.; Lucas R.; Liu W.M.; Lee S.S.; Machida T.; Minall L.; Mehmood S.; Belaya K.; Liu W.W.; Chu A.; Shrestha L.; Mukhopadhyay S.M.M.; Strain-Damerell C.; Chalk R.; Burgess-Brown N.A.; Bibb M.J.; Barry Iii C.E.; Robinson C.V.; Beeson D.; Davis B.G.; Carpenter E.P.;
Cell 175:1045-1058(2018)
Cited for: X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF WILD-TYPE AND VARIANT CMS13 GLY-264 IN COMPLEXES WITH UDP-N-ACETYLGLUCOSAMINE AND TUNICAMYCIN; FUNCTION; CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES; COFACTOR; PATHWAY; ACTIVITY REGULATION; SUBUNIT; TOPOLOGY; CHARACTERIZATION OF VARIANT CDG1J CYS-170; CHARACTERIZATION OF VARIANTS CMS13 ILE-108; MET-120; SER-160; LEU-168; ILE-171; SER-192 AND GLY-264; MUTAGENESIS OF PRO-30; ILE-69; ALA-114; ASP-115; ASP-116; TRP-122; LYS-125; LEU-168; ASN-182; ASN-185; ASP-252; VAL-264; ARG-301; HIS-302 AND ARG-303; Deficiency of UDP-GlcNAc:dolichol phosphate N-acetylglucosamine-1 phosphate transferase (DPAGT1) causes a novel congenital disorder of glycosylation type Ij.
Wu X.; Rush J.S.; Karaoglu D.; Krasnewich D.; Lubinsky M.S.; Waechter C.J.; Gilmore R.; Freeze H.H.;
Hum. Mutat. 22:144-150(2003)
Cited for: VARIANT CDG1J CYS-170;
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.