Variant position: 288 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 QQAEEALVAKQEVIDKLKEE AEQHKIVMETVPVLKAQADIY
Mouse QQAEEALVAKQELIDKLKEE AEQHKIVMETVPVLKAQADIY
Rat QQAEEALVAKQELIDKLKEE AEQHKIVMETVPVLKAQADIY
Bovine QQAEEALVAKQEVIDKLKEE AEQHKIVMETVPVLKAQADIY
Drosophila -------------INELKAR DIQKQ---EVIKGLQIQNDIY
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
242 – 350 Ubiquitin-binding (UBD)
246 – 365 Self-association
251 – 419 Required for interaction with TNFAIP3
49 – 356
277 – 277 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
277 – 277 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
283 – 283 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
285 – 285 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
292 – 292 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
302 – 302 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
257 – 304 Missing. In isoform 3.
277 – 277 K -> A. Partial abolition of sumoylation. Abolishes sumoylation and IKK activation; when associated with A-309.
285 – 285 K -> R. Important decrease in the ubiquitination level; when associated with R-399.
296 – 296 E -> A. No effet on oligomerization,impairs binding of 'Lys-63'-linked ubiuitin and linear tetra-ubiquitin, impairs TNF-induced NF-kappa-B activation.
300 – 300 V -> D. Greatly impairs tandem ubiquitin binding.
301 – 301 L -> A. Impairs tandem ubiquitin binding.
304 – 304 Q -> A. Impairs tandem ubiquitin binding.
307 – 307 I -> N. Greatly impairs tandem ubiquitin binding.
308 – 308 Y -> A. Greatly impairs tandem ubiquitin binding.
271 – 295
No reference for the current variant in UniProtKB/Swiss-Prot.
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.