Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q13422: Variant p.Tyr210Cys

DNA-binding protein Ikaros
Gene: IKZF1
Feedback?
Variant information Variant position: help 210 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 Tyrosine (Y) to Cysteine (C) at position 210 (Y210C, p.Tyr210Cys). 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 large size and aromatic (Y) to medium size and polar (C) 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 CVID13; decreases binding to pericentromeric heterochromatin DNA; has diffuse nuclear localization. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 210 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 519 The length of the canonical sequence.
Location on the sequence: help GHLRTHSVGKPHKCGYCGRS Y KQRSSLEEHKERCHNYLESM 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                         GHLRTHSVGKPHKCGYCGRSYKQRSSLEEHKERCHNYLESM

Mouse                         GHLRTHSVGKPHKCGYCGRSYKQRSSLEEHKERCHNYLESM

Chicken                       GHLRTHSVGKPHKCGYCGRSYKQRSSLEEHKERCHNYLQTM
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 – 519 DNA-binding protein Ikaros
Zinc finger 201 – 224 C2H2-type 4
Modified residue 196 – 196 Phosphoserine
Alternative sequence 54 – 283 Missing. In isoform Ik6.
Alternative sequence 141 – 283 Missing. In isoform Ik5.
Alternative sequence 197 – 283 Missing. In isoform Ik3 and isoform Ik4.
Alternative sequence 197 – 238 Missing. In isoform Ik7 and isoform Ikx.
Mutagenesis 191 – 191 H -> R. Abolishes binding to DNA and has diffuse nuclear localization.



Literature citations
Congenital pancytopenia and absence of B lymphocytes in a neonate with a mutation in the Ikaros gene.
Goldman F.D.; Gurel Z.; Al-Zubeidi D.; Fried A.J.; Icardi M.; Song C.; Dovat S.;
Pediatr. Blood Cancer 58:591-597(2012)
Cited for: INVOLVEMENT IN CVID13; VARIANT CVID13 CYS-210; CHARACTERIZATION OF VARIANT CVID13 CYS-210; SUBCELLULAR LOCATION; Loss of B Cells in Patients with Heterozygous Mutations in IKAROS.
Kuehn H.S.; Boisson B.; Cunningham-Rundles C.; Reichenbach J.; Stray-Pedersen A.; Gelfand E.W.; Maffucci P.; Pierce K.R.; Abbott J.K.; Voelkerding K.V.; South S.T.; Augustine N.H.; Bush J.S.; Dolen W.K.; Wray B.B.; Itan Y.; Cobat A.; Sorte H.S.; Ganesan S.; Prader S.; Martins T.B.; Lawrence M.G.; Orange J.S.; Calvo K.R.; Niemela J.E.; Casanova J.L.; Fleisher T.A.; Hill H.R.; Kumanovics A.; Conley M.E.; Rosenzweig S.D.;
N. Engl. J. Med. 374:1032-1043(2016)
Cited for: VARIANTS CVID13 GLN-162; LEU-162; ARG-167 AND GLN-184; CHARACTERIZATION OF VARIANTS CVID13 GLN-162; LEU-162; ARG-167; GLN-184 AND CYS-210; MUTAGENESIS OF ASN-159 AND HIS-191;
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.