Variant position: 243 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 617 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 PEIGHIFLLDRDVDFVTALC SQVVYEGLVDDTFRIKCGSVD
Mouse PEIGHIFLLDRDVDFVTALC SQVVYEGLVDDTFRIKCGSVD
Rat PEIGHIFLLDRDVDFVTALC SQVVYEGLVDDTFRIKCGSVD
Bovine PEIGHIFLLDRDVDFVTALC SQVVYEGLVDDTFRIKCGSVD
Zebrafish PEFAKVFLIDRDVDFVTPLC SQVVYEGLVDDIFRIKCSSVE
Caenorhabditis elegans P-ISHLFLFDRQLDPVPVLL TGASYEGLLHEFFTIDCGKLA
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
2 – 617 Vacuolar protein sorting-associated protein 33B
234 – 234 D -> H. No effect on interaction with VIPAS39; no effect on interaction with STX7 and association with the HOPS complex; impairs localization to VIPAS39-containing endosomal compartment.
249 – 249 G -> V. Disrupts interaction with VIPAS39; no effect on interaction with STX7; impairs localization to VIPAS39-containing endosomal compartment.
252 – 252 D -> E. No effect on interaction with VIPAS39 and STX7; impairs localization to VIPAS39-containing endosomal compartment.
Vps33b pathogenic mutations preferentially affect VIPAS39/SPE-39-positive endosomes.
Tornieri K.; Zlatic S.A.; Mullin A.P.; Werner E.; Harrison R.; L'hernault S.W.; Faundez V.;
Hum. Mol. Genet. 22:5215-5228(2013)
Cited for: FUNCTION; CHARACTERIZATION OF VARIANTS ARCS1 PRO-30 AND PHE-243; MUTAGENESIS OF 232-ASP--ASP-234; ASP-234; 235-VAL--PHE-237; GLY-249; 251-VAL--ASP-253 AND ASP-252; INTERACTION WITH VIPAS39; STX7; VPS18 AND VPS41;
Molecular investigations to improve diagnostic accuracy in patients with ARC syndrome.
Cullinane A.R.; Straatman-Iwanowska A.; Seo J.K.; Ko J.S.; Song K.S.; Gizewska M.; Gruszfeld D.; Gliwicz D.; Tuysuz B.; Erdemir G.; Sougrat R.; Wakabayashi Y.; Hinds R.; Barnicoat A.; Mandel H.; Chitayat D.; Fischler B.; Garcia-Cazorla A.; Knisely A.S.; Kelly D.A.; Maher E.R.; Gissen P.;
Hum. Mutat. 30:E330-E337(2009)
Cited for: VARIANT ARCS1 PHE-243;
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