Sequence information
Variant position: 407 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:
SPPEEPPDFCCPKCQYQAPD
M DTLQIHVMECIE
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 SPPEEPPDFCCPKCQYQAPDM DTLQIHVMECIE--
Mouse SPPEEPPDFCCPKCQYQAPDM DTLQIHVMECIE
Rat SPPEEPPDFCCPKCQYQAPDM DTLQIHVMECIE
Pig SPPEEPPNFCCPKCQYQAPDM DTLQIHVMECIE
Bovine SPPDEPPKFCCPKCQYQAPDI DTLQIHVMECIE
Drosophila SSRTSDTTLRCPICSKSFNAL SVLQSHVNDCLD
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 – 419
NF-kappa-B essential modulator
Zinc finger
389 – 419
CCHC NOA-type
Region
251 – 419
Required for interaction with TNFAIP3
Region
382 – 419
Interaction with CYLD
Modified residue
387 – 387
Phosphoserine
Cross
399 – 399
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Mutagenesis
399 – 399
K -> R. Abolishes BCL10-mediated but not RIPK2-mediated ubiquitination. Important decrease in the ubiquitination level; when associated with R-285. No change in the ubiquitination level; when associated with R-115 or R-224.
Mutagenesis
414 – 414
V -> S. Abolishes binding to polyubiquitin.
Mutagenesis
415 – 415
M -> S. Impairs binding to polyubiquitin.
Helix
407 – 416
Literature citations
Genomic rearrangement in NEMO impairs NF-kappaB activation and is a cause of incontinentia pigmenti.
Smahi A.; Courtois G.; Vabres P.; Yamaoka S.; Heuertz S.; Munnich A.; Israel A.; Heiss N.S.; Klauck S.M.; Kioschis P.; Wiemann S.; Poustka A.; Esposito T.; Bardaro T.; Gianfrancesco F.; Ciccodicola A.; D'Urso M.; Woffendin H.; Jakins T.; Donnai D.; Stewart H.; Kenwrick S.J.; Aradhya S.; Yamagata T.; Levy M.; Lewis R.A.; Nelson D.L.;
Nature 405:466-472(2000)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANT IP VAL-407;
The zinc finger of NEMO is a functional ubiquitin-binding domain.
Cordier F.; Grubisha O.; Traincard F.; Veron M.; Delepierre M.; Agou F.;
J. Biol. Chem. 284:2902-2907(2009)
Cited for: UBIQUITIN-BINDING; MUTAGENESIS OF VAL-414 AND MET-415; CHARACTERIZATION OF VARIANT IP VAL-407;
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;
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.