Variant position: 264 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 AGRASSKDWKRSIRYAGRPL QCLIQDGILNPHAASCTCAAC
Chimpanzee AGRASSKDWKRSIRYAGRPL QCLIQDGILNPHAASCTCAAC
Mouse AGRASSKDWKRSIRYAGRPL QCLIQDGILNPHAASCTCAAC
Rat AGRASSKDWKRSIRYAGRPL QCLIQDGILNPHAASCTCAAC
Drosophila CGRGSSKDWKRSIKYGGKSL QSLIDEGTLTPHATNCSCTVC
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.
246 – 246 R -> A. Reduces transcription activation.
250 – 250 K -> A. Abolishes DNA-binding. Loss of DEAF1-promoter repression; when associated with A-253. Loss of transcriptional activation of EIF4G3; when associated with A-253. Loss of interaction with XRCC6; when associated with A-253. Loss of DNA binding; when associated with A-253.
252 – 252 W -> Q. Abolishes DNA-binding.
253 – 253 K -> A. Abolishes DNA-binding. oss of DEAF1-promoter repression; when associated with A-250. Loss of transcriptional activation of EIF4G3; when associated with A-250. Loss of interaction with XRCC6; when associated with A-250. Loss of DNA binding; when associated with A-250.
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.