Variant position: 224 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 565 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 PVRCRNISGTLYKNRLGSGG RGRCIKQGENWYSPTEFEAMA
Chimpanzee PVRCRNISGTLYKNRLGSGG RGRCIKQGENWYSPTEFEAMA
Mouse PVRCRNISGTLYKSRLGSGG RGRCIKQGENWYSPTEFEAMA
Rat PVRCRNISGTLYKSRLGSGG RGRCIKQGENWYSPTEFEAMA
Drosophila QIRCKTTCAELYRSKLGSGG RGRCVKYKDKWHTPSEFEHVC
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 – 565 Deformed epidermal autoregulatory factor 1 homolog
193 – 273 SAND
223 – 333 GRGRCIKQGENWYSPTEFEAMAGRASSKDWKRSIRYAGRPLQCLIQDGILNPHAASCTCAACCDDMTLSGPVRLFVPYKRRKKENELPTTPVKKDSPKNITLLPATAATTF -> WDLKPSRCLLHLCCLLRRHDLI. In isoform 4.
215 – 215 Y -> Q. Reduces transcription activation.
226 – 226 R -> A. Reduces transcription activation.
Mutations affecting the SAND domain of DEAF1 cause intellectual disability with severe speech impairment and behavioral problems.
Vulto-van Silfhout A.T.; Rajamanickam S.; Jensik P.J.; Vergult S.; de Rocker N.; Newhall K.J.; Raghavan R.; Reardon S.N.; Jarrett K.; McIntyre T.; Bulinski J.; Ownby S.L.; Huggenvik J.I.; McKnight G.S.; Rose G.M.; Cai X.; Willaert A.; Zweier C.; Endele S.; de Ligt J.; van Bon B.W.; Lugtenberg D.; de Vries P.F.; Veltman J.A.; van Bokhoven H.; Brunner H.G.; Rauch A.; de Brouwer A.P.; Carvill G.L.; Hoischen A.; Mefford H.C.; Eichler E.E.; Vissers L.E.; Menten B.; Collard M.W.; de Vries B.B.;
Am. J. Hum. Genet. 94:649-661(2014)
Cited for: FUNCTION; INTERACTION WITH XRCC6; DNA-BINDING; TISSUE SPECIFICITY; INVOLVEMENT IN MRD24; VARIANTS MRD24 TRP-224; SER-228; SER-254 AND PRO-264; CHARACTERIZATION OF VARIANTS MRD24 TRP-224; SER-228; SER-254 AND PRO-264; MUTAGENESIS OF LYS-250 AND LYS-253;
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.