Variant position: 162 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:
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 ERPFQCNQCGASFTQKGNLL RHIKLHSGEKPFKCHLCNYAC
Mouse ERPFQCNQCGASFTQKGNLL RHIKLHSGEKPFKCHLCNYAC
Chicken ERPFQCNQCGASFTQKGNLL RHIKLHSGEKPFKCHLCNYAC
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 – 519 DNA-binding protein Ikaros
145 – 167 C2H2-type 2
154 – 163 Required for both high-affinity DNA binding and pericentromeric heterochromatin localization
159 – 159 Required for both pericentromeric heterochromatin localization and complete DNA binding
162 – 162 Required for both pericentromeric heterochromatin localization and complete DNA binding
168 – 168 Phosphoserine
54 – 283 Missing. In isoform Ik6.
141 – 283 Missing. In isoform Ik5.
159 – 159 N -> A. Abolishes binding to DNA and has diffuse nuclear localization.
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;
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.