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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O60481: Variant p.His318Asn

Zinc finger protein ZIC 3
Gene: ZIC3
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Variant information Variant position: help 318 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 Histidine (H) to Asparagine (N) at position 318 (H318N, p.His318Asn). 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 Similar physico-chemical property. Both residues are medium size and polar. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 1 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 VACTERLX; decrease in transcriptional activator activity; significant decrease in nuclear localization. Any additional useful information about the variant.


Sequence information Variant position: help 318 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 467 The length of the canonical sequence.
Location on the sequence: help YWEECPREGKSFKAKYKLVN H IRVHTGEKPFPCPFPGCGKI 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                         YWEECPREGKSFKAKYKLVNHIRVHTGEKPFPCPFPGCGKI

Mouse                         YWEECPREGKSFKAKYKLVNHIRVHTGEKPFPCPFPGCGKI

Xenopus laevis                YWEECPRGGKSFKAKYKLVNHIRVHTGEKPFPCPFPGCGKI

Xenopus tropicalis            YWEECPRGGKSFKAKYKLVNHIRVHTGEKPFPCPFPGCGKI
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 1 – 467 Zinc finger protein ZIC 3
Zinc finger 295 – 322 C2H2-type 2; atypical
Motif 297 – 322 Nuclear localization signal
Mutagenesis 304 – 304 R -> M. Increases its cytoplasmic localization.
Mutagenesis 307 – 307 K -> M. Increases its cytoplasmic localization.
Mutagenesis 310 – 310 K -> M. Increases its cytoplasmic localization.
Mutagenesis 312 – 312 K -> M. Increases its cytoplasmic localization.
Mutagenesis 314 – 314 K -> M. Does not increase its cytoplasmic localization.
Mutagenesis 320 – 320 R -> A. Increases its cytoplasmic localization. Does not interact with KPNA1 and KPNA6 and increases strongly its cytoplasmic localization; when associated with A-337; A-341; A-346; A-349 and A-350.
Mutagenesis 326 – 326 K -> M. Does not increase its cytoplasmic localization.
Mutagenesis 337 – 337 K -> A. Increases its cytoplasmic localization. Does not interact with KPNA1 and KPNA6 and increases strongly its cytoplasmic localization; when associated with A-320; A-341; A-346; A-349 and A-350.
Helix 312 – 323



Literature citations
Genetic and functional analyses of ZIC3 variants in congenital heart disease.
Cowan J.; Tariq M.; Ware S.M.;
Hum. Mutat. 35:66-75(2014)
Cited for: VARIANTS CHTD1 CYS-17; ALA-53 INS; CYS-109; ALA-217 AND GLY-447; VARIANTS HTX1 CYS-17 AND ALA-217; VARIANT VACTERLX ASN-318; CHARACTERIZATION OF VARIANTS CHTD1 ALA-53 INS; CYS-109; ALA-217 AND GLY-447; CHARACTERIZATION OF VARIANTS HTX1 CYS-17 AND ALA-217; CHARACTERIZATION OF VARIANT VACTERLX ASN-318;
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.