Sequence information
Variant position: 1021 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 1044 The length of the canonical sequence.
Location on the sequence:
SLALGKTEEEALKHFRVKFN
E ALRESWKTKVNWLAHNVSKD
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 SLALGKTEEEALKHFRVKFNE ALRESWKTKVNWLAHNVSKD
Mouse SLALGKTEEEALKHFRVKFNE ALRESWKTKVNWLAHNVSKD
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 – 1044
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform
Domain
745 – 1027
PI3K/PI4K catalytic
Modified residue
1039 – 1039
Phosphoserine; by autocatalysis
Alternative sequence
302 – 1044
Missing. In isoform 2.
Mutagenesis
1039 – 1039
S -> A. Abolishes autophosphorylation, no effect on lipid kinase activity.
Mutagenesis
1039 – 1039
S -> DE. Abolishes autophosphorylation, reduced lipid kinase activity.
Helix
1008 – 1031
Literature citations
Phosphoinositide 3-kinase delta gene mutation predisposes to respiratory infection and airway damage.
Angulo I.; Vadas O.; Garcon F.; Banham-Hall E.; Plagnol V.; Leahy T.R.; Baxendale H.; Coulter T.; Curtis J.; Wu C.; Blake-Palmer K.; Perisic O.; Smyth D.; Maes M.; Fiddler C.; Juss J.; Cilliers D.; Markelj G.; Chandra A.; Farmer G.; Kielkowska A.; Clark J.; Kracker S.; Debre M.; Picard C.; Pellier I.; Jabado N.; Morris J.A.; Barcenas-Morales G.; Fischer A.; Stephens L.; Hawkins P.; Barrett J.C.; Abinun M.; Clatworthy M.; Durandy A.; Doffinger R.; Chilvers E.R.; Cant A.J.; Kumararatne D.; Okkenhaug K.; Williams R.L.; Condliffe A.; Nejentsev S.;
Science 342:866-871(2013)
Cited for: INVOLVEMENT IN IMD14A; VARIANT IMD14A LYS-1021; CHARACTERIZATION OF VARIANT IMD14A LYS-1021;
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.