Sequence information
Variant position: 182 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 292 The length of the canonical sequence.
Location on the sequence:
GWSSHKAHQVVKKASGDKIV
V VVRDRPFQRTVTMHKDSMGH
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 GWSSHKAHQVVKKASGDKIVV VVRDRPFQRTVTMHKDSMGH
Mouse GWNTHKAHKVLKKASAEKIVM VIRDRPFQRTVTMHKDSSGQ
Rat GWSTHKAQKALKKASAEKIVM VVRDRPFQRTVTMHKDSSGQ
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 – 292
Syntenin-2
Domain
108 – 187
PDZ 1
Mutagenesis
167 – 167
K -> A. Abolishes phosphatidylinositol 4,5-bisphosphate binding and targeting to plasma membrane, speckles and nucleoli; when associated with A-113; A-197 and A-244. Reduces phosphatidylinositol 4,5-bisphosphate binding and does not change subcellular localization; when associated with A-113.
Mutagenesis
197 – 197
K -> A. Abolishes phosphatidylinositol 4,5-bisphosphate binding and targeting to plasma membrane, speckles and nucleoli; when associated with A-113; A-167 and A-244. Reduces phosphatidylinositol 4,5-bisphosphate binding and does not change subcellular localization; when associated with A-244.
Literature citations
The neural cell recognition molecule neurofascin interacts with syntenin-1 but not with syntenin-2, both of which reveal self-associating activity.
Koroll M.; Rathjen F.G.; Volkmer H.;
J. Biol. Chem. 276:10646-10654(2001)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3); VARIANT MET-182; SUBUNIT; INTERACTION WITH SDCBP;
Submission
Mei G.; Yu W.; Gibbs R.A.;
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3); VARIANT MET-182;
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.