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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9H165: Variant p.Cys48Phe

BCL11 transcription factor A
Gene: BCL11A
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Variant information Variant position: help 48 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance
Residue change: help From Cysteine (C) to Phenylalanine (F) at position 48 (C48F, p.Cys48Phe). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Change from medium size and polar (C) to large size and aromatic (F) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page
Variant description: help In IDPFH; de novo mutation; loss of function in transactivation of transcription; reduces the interaction between isoform 2 and isoform 3; disrupts the nuclear paraspeckle distribution of isoform 2 and isoform 3; does not affect the interaction of isoform 2 with TBR1. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 48 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 835 The length of the canonical sequence.
Location on the sequence: help DDEPDHGPLGAPEGDHDLLT C GQCQMNFPLGDILIFIEHKR 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         DDEPDHGPLGAPEGDHDLLTCGQCQMNFPLGDILIFIEHKR

Mouse                         DDEPDHGPLGAPEGDHDLLTCGQCQMNFPLGDILIFIEHKR
Sequence annotation in neighborhood: help 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.
TypePositionsDescription
Chain 1 – 835 BCL11 transcription factor A
Zinc finger 45 – 71 C2HC-type
Region 1 – 210 Required for nuclear body formation and for SUMO1 recruitment
Binding site 48 – 48
Binding site 51 – 51
Binding site 66 – 66
Mutagenesis 46 – 46 L -> A. Abolishes self-association; when associated with A-57, A-60, A-61 and A-63.
Mutagenesis 57 – 57 L -> A. Abolishes self-association; when associated with A-46, A-60, A-61 and A-63.
Mutagenesis 60 – 60 I -> A. Impairs self-association. Abolishes self-association; when associated with A-46, A-57, A-61 and A-63. Reduces expression in erythroid cells; when associated with A-61.
Mutagenesis 61 – 61 L -> A. Abolishes self-association; when associated with A-46, A-57, A-60 and A-63. Reduces expression in erythroid cells; when associated with A-60.
Mutagenesis 63 – 63 F -> A. Impairs self-association. Abolishes self-association; when associated with A-46, A-57, A-60 and A-61.



Literature citations
BCL11A haploinsufficiency causes an intellectual disability syndrome and dysregulates transcription.
Dias C.; Estruch S.B.; Grmaham S.A.; McRae J.; Sawiak S.J.; Hurst J.A.; Joss S.K.; Holder S.E.; Morton J.E.; Turner C.; Thevenon J.; Mellul K.; Sanchez-Andrade G.; Ibarra-Soria X.; Deriziotis P.; Santos R.F.; Lee S.C.; Faivre L.; Kleefstra T.; Liu P.; Hurles M.E.; Fisher S.E.; Logan D.W.;
Am. J. Hum. Genet. 99:253-274(2016)
Cited for: INVOLVEMENT IN IDPFH; VARIANTS IDPFH PRO-47; PHE-48 AND GLN-66; CHARACTERIZATION OF VARIANTS IDPFH PRO-47; PHE-48 AND GLN-66; FUNCTION; SUBCELLULAR LOCATION; Functional characterization of TBR1 variants in neurodevelopmental disorder.
den Hoed J.; Sollis E.; Venselaar H.; Estruch S.B.; Deriziotis P.; Fisher S.E.;
Sci. Rep. 8:14279-14279(2018)
Cited for: INTERACTION WITH TBR1; CHARACTERIZATION OF VARIANTS IDPFH PRO-47; PHE-48 AND GLN-66; DOMAIN;
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.