Variant position: 388 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 781 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 LHLTDPSQRLVQNCLWTLRN LSDAATKQEGMEGLLGTLVQL
Mouse LHLTDPSQRLVQNCLWTLRN LSDAATKQEGMEGLLGTLVQL
Rat PHLTDPSQRLVQNCLWTLRN LSDAATKQEGMEGLLGTLVQL
Bovine LHLTDPSQRLVQNCLWTLRN LSDAATKQEGMEGLLGTLVQL
Xenopus laevis LHLTDSSQRLVQNCLWTLRN LSDAATKQEGMEGLLGTLVQL
Zebrafish LHLTDPSQRLVQNCLWTLRN LSDAATKQEGMEGLLGTLVQL
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 – 781 Catenin beta-1
361 – 389 ARM 6
383 – 383 W -> A. Abolishes APC binding. Strongly reduces phosphorylation and degradation; when associated with A-260 and A-386.
386 – 386 R -> A. Strongly reduces APC binding. Strongly reduces phosphorylation and degradation; when associated with A-260 and A-383.
375 – 389
De novo mutations in beta-catenin (CTNNB1) appear to be a frequent cause of intellectual disability: expanding the mutational and clinical spectrum.
Kuechler A.; Willemsen M.H.; Albrecht B.; Bacino C.A.; Bartholomew D.W.; van Bokhoven H.; van den Boogaard M.J.; Bramswig N.; Buettner C.; Cremer K.; Czeschik J.C.; Engels H.; van Gassen K.; Graf E.; van Haelst M.; He W.; Hogue J.S.; Kempers M.; Koolen D.; Monroe G.; de Munnik S.; Pastore M.; Reis A.; Reuter M.S.; Tegay D.H.; Veltman J.; Visser G.; van Hasselt P.; Smeets E.E.; Vissers L.; Wieland T.; Wissink W.; Yntema H.; Zink A.M.; Strom T.M.; Luedecke H.J.; Kleefstra T.; Wieczorek D.;
Hum. Genet. 134:97-109(2015)
Cited for: VARIANT NEDSDV PRO-388;
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.