Variant position: 255 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 467 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 GPGAFFRYMRQPIKQELSCK WIDEAQLSRPKKSCDRTFSTM
Mouse GPGAFFRYMRQPIKQELSCK WIEEAQLSRPKKSCDRTFSTM
Xenopus laevis GQGAFFRYMRQPIKQELSCK WLEESTMNHPQKTCDRTFSSM
Xenopus tropicalis GPGAFFRYMRQPIKQELSCK WLEESPMNRPQKTCDRTFSSM
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 – 467 Zinc finger protein ZIC 3
251 – 286 C2H2-type 1; atypical
248 – 248 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
268 – 268 C -> S. Increases weakly its cytoplasmic localization.
Functional and structural basis of the nuclear localization signal in the ZIC3 zinc finger domain.
Hatayama M.; Tomizawa T.; Sakai-Kato K.; Bouvagnet P.; Kose S.; Imamoto N.; Yokoyama S.; Utsunomiya-Tate N.; Mikoshiba K.; Kigawa T.; Aruga J.;
Hum. Mol. Genet. 17:3459-3473(2008)
Cited for: STRUCTURE BY NMR OF 246-329 IN COMPLEX WITH ZINC IONS; INTERACTION WITH KPNA1 AND KPNA6; CHARACTERIZATION OF VARIANTS HTX1 SER-253; GLY-255 AND ARG-286; MUTAGENESIS OF CYS-268; HIS-281; ARG-304; LYS-307; LYS-310; LYS-312; LYS-314; ARG-320; LYS-326; LYS-337; ARG-341; LYS-346; LYS-349; ARG-350 AND LYS-356;
Elucidation of penetrance variability of a ZIC3 mutation in a family with complex heart defects and functional analysis of ZIC3 mutations in the first zinc finger domain.
Chhin B.; Hatayama M.; Bozon D.; Ogawa M.; Schoen P.; Tohmonda T.; Sassolas F.; Aruga J.; Valard A.-G.; Chen S.-C.; Bouvagnet P.;
Hum. Mutat. 28:563-570(2007)
Cited for: VARIANT HTX1 GLY-255; CHARACTERIZATION OF VARIANT HTX1 GLY-255;
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.