Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9H267: Variant p.Ser243Phe

Vacuolar protein sorting-associated protein 33B
Gene: VPS33B
Feedback?
Variant information Variant position: help 243 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 Serine (S) to Phenylalanine (F) at position 243 (S243F, p.Ser243Phe). 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 small size and polar (S) to large size and aromatic (F) 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 ARCS1; no effect on interaction with VIPAS39; impairs localization to VIPAS39-containing endosomal compartment. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 243 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 617 The length of the canonical sequence.
Location on the sequence: help PEIGHIFLLDRDVDFVTALC S QVVYEGLVDDTFRIKCGSVD 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                         PEIGHIFLLDRDVDFVTALCSQVVYEGLVDDTFRIKCGSVD

Mouse                         PEIGHIFLLDRDVDFVTALCSQVVYEGLVDDTFRIKCGSVD

Rat                           PEIGHIFLLDRDVDFVTALCSQVVYEGLVDDTFRIKCGSVD

Bovine                        PEIGHIFLLDRDVDFVTALCSQVVYEGLVDDTFRIKCGSVD

Zebrafish                     PEFAKVFLIDRDVDFVTPLCSQVVYEGLVDDIFRIKCSSVE

Caenorhabditis elegans        P-ISHLFLFDRQLDPVPVLLTGASYEGLLHEFFTIDCGKLA
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 2 – 617 Vacuolar protein sorting-associated protein 33B
Mutagenesis 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.
Mutagenesis 249 – 249 G -> V. Disrupts interaction with VIPAS39; no effect on interaction with STX7; impairs localization to VIPAS39-containing endosomal compartment.
Mutagenesis 252 – 252 D -> E. No effect on interaction with VIPAS39 and STX7; impairs localization to VIPAS39-containing endosomal compartment.



Literature citations
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;
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.