Sequence information
Variant position: 167 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 519 The length of the canonical sequence.
Location on the sequence:
CNQCGASFTQKGNLLRHIKL
H SGEKPFKCHLCNYACRRRDA
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 CNQCGASFTQKGNLLRHIKLH SGEKPFKCHLCNYACRRRDA
Mouse CNQCGASFTQKGNLLRHIKLH SGEKPFKCHLCNYACRRRDA
Chicken CNQCGASFTQKGNLLRHIKLH SGEKPFKCHLCNYACRRRDA
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 – 519
DNA-binding protein Ikaros
Zinc finger
145 – 167
C2H2-type 2
Site
159 – 159
Required for both pericentromeric heterochromatin localization and complete DNA binding
Site
162 – 162
Required for both pericentromeric heterochromatin localization and complete DNA binding
Modified residue
168 – 168
Phosphoserine
Alternative sequence
54 – 283
Missing. In isoform Ik6.
Alternative sequence
141 – 283
Missing. In isoform Ik5.
Mutagenesis
159 – 159
N -> A. Abolishes binding to DNA and has diffuse nuclear localization.
Helix
157 – 168
Literature citations
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.