Variant position: 57 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 419 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 AMLHLPSEQGAPETLQRCLE ENQELRDAIRQSNQILRERCE
Mouse AMLHLPSEQGTPETLQRCLE ENQELRDAIRQSNQMLRERCE
Rat AMLHLPSEQGTPETLQRCLE ENQELRDAIRQSNQMLRERCE
Pig TMLHLPSEQGAPETFQRCLE ENQELRDAIRQSNQMLRERCE
Bovine AMLHVPSEQGTPETFQRCLE ENQELRDAIRQSNQMLRERCE
Drosophila TVNCIPVSITASQQQHKSLD SGSSQQQSLATSFIMGEIQSD
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 – 419 NF-kappa-B essential modulator
44 – 111 Interaction with CHUK/IKBKB
49 – 356
43 – 43 Phosphoserine; by IKKB
68 – 68 Phosphoserine
54 – 54 Interchain
68 – 68 S -> A. Increases formation of homodimers.
68 – 68 S -> E. Abolishes interaction with IKBKB; abolishes TNF-alpha induced NF-kappa-B activity.
38 – 129
A recurrent deletion in the ubiquitously expressed NEMO (IKK-gamma) gene accounts for the vast majority of incontinentia pigmenti mutations.
Aradhya S.; Woffendin H.; Jakins T.; Bardaro T.; Esposito T.; Smahi A.; Shaw C.; Levy M.; Munnich A.; D'Urso M.; Lewis R.A.; Kenwrick S.; Nelson D.L.;
Hum. Mol. Genet. 10:2171-2179(2001)
Cited for: VARIANTS IP LYS-57 AND VAL-407;
Molecular analysis of the genetic defect in a large cohort of IP patients and identification of novel NEMO mutations interfering with NF-kappaB activation.
Fusco F.; Bardaro T.; Fimiani G.; Mercadante V.; Miano M.G.; Falco G.; Israeel A.; Courtois G.; D'Urso M.; Ursini M.V.;
Hum. Mol. Genet. 13:1763-1773(2004)
Cited for: VARIANTS IP LYS-57; LYS-90 DEL AND TRP-123; VARIANT ASN-113; CHARACTERIZATION OF VARIANTS IP LYS-57; LYS-90 DEL AND TRP-123; CHARACTERIZATION OF VARIANT ASN-113;
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.