Variant position: 158 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 488 The length of the canonical sequence.
Location on the 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.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human FHLMFYCTRTLPN-VLALPVV LLALAAWLRHEWARFIWLSAF
Mouse FHLMFYCTRTLPN-VLALAVV LPALTAWLQRRWALFVWLSA
Caenorhabditis elegans FHYIFYMSRPLPN-TFALILV MIVFERLLEGRYESAVRYAT
Drosophila FHFMFYMTRPLPN-IFALPIV LFAIAYWLRDQHKPFIICSG
Baker's yeast FHLMFYSTRTLPNFVMTLPLT NVALGWVLLGRYNAAIFLSA
Fission yeast FHLVYYMSRPLSN-IFGLIAT NHSLSLLLKNNYYGSISILV
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
1 – 488 Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase
145 – 165 Helical
Deficiency of dolichyl-P-Man:Man7GlcNAc2-PP-dolichyl mannosyltransferase causes congenital disorder of glycosylation type Ig.
Thiel C.; Schwarz M.; Hasilik M.; Grieben U.; Hanefeld F.; Lehle L.; von Figura K.; Koerner C.;
Biochem. J. 367:195-201(2002)
Cited for: CHARACTERIZATION OF VARIANT CDG1G PRO-158;
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