Variant position: 417 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 CPKCQYQAPDMDTLQIHVME CIE--
Mouse CPKCQYQAPDMDTLQIHVME CIE
Rat CPKCQYQAPDMDTLQIHVME CIE
Pig CPKCQYQAPDMDTLQIHVME CIE
Bovine CPKCQYQAPDIDTLQIHVME CIE
Drosophila CPICSKSFNALSVLQSHVND CLD
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
389 – 419 CCHC NOA-type
251 – 419 Required for interaction with TNFAIP3
382 – 419 Interaction with CYLD
399 – 399 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
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.
414 – 414 V -> S. Abolishes binding to polyubiquitin.
415 – 415 M -> S. Impairs binding to polyubiquitin.
Solution structure of NEMO zinc finger and impact of an anhidrotic ectodermal dysplasia with immunodeficiency-related point mutation.
Cordier F.; Vinolo E.; Veron M.; Delepierre M.; Agou F.;
J. Mol. Biol. 377:1419-1432(2008)
Cited for: STRUCTURE BY NMR OF 394-419 OF WILD-TYPE AND MUTANT PHE-417; DOMAIN ZINC-FINGER;
A novel X-linked disorder of immune deficiency and hypohidrotic ectodermal dysplasia is allelic to incontinentia pigmenti and due to mutations in IKK-gamma (NEMO).
Zonana J.; Elder M.E.; Schneider L.C.; Orlow S.J.; Moss C.; Golabi M.; Shapira S.K.; Farndon P.A.; Wara D.W.; Emmal S.A.; Ferguson B.M.;
Am. J. Hum. Genet. 67:1555-1562(2000)
Cited for: VARIANTS EDAID ARG-417 AND PHE-417;
X-linked anhidrotic ectodermal dysplasia with immunodeficiency is caused by impaired NF-kappa B signaling.
Doeffinger R.; Smahi A.; Bessia C.; Geissmann F.; Feinberg J.; Durandy A.; Bodemer C.; Kenwrick S.J.; Dupuis-Girod S.; Blanche S.; Wood P.; Rabia S.H.; Headon D.J.; Overbeek P.A.; Le Deist F.; Holland S.M.; Belani K.; Kumararatne D.S.; Fischer A.; Shapiro R.; Conley M.E.; Reimund E.; Kalhoff H.; Abinun M.; Munnich A.; Israael A.; Courtois G.; Casanova J.-L.;
Nat. Genet. 27:277-285(2001)
Cited for: INVOLVEMENT IN OLEDAID; INVOLVEMENT IN EDAID; VARIANTS EDAID PRO-175; PRO-227; GLY-288; ASN-311; ARG-417 AND PHE-417;
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.