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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q12948: Variant p.Cys135Tyr

Forkhead box protein C1
Gene: FOXC1
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Variant information Variant position: help 135 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 Tyrosine (Y) at position 135 (C135Y, p.Cys135Tyr). 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 (Y) 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 RIEG3; decreased protein abundance; decreased protein stability; decreased location at nucleus; loss of transcription regulatory region DNA binding; loss of sequence-specific DNA binding transcription factor activity. Any additional useful information about the variant.


Sequence information Variant position: help 135 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 553 The length of the canonical sequence.
Location on the sequence: help YRDNKQGWQNSIRHNLSLNE C FVKVPRDDKKPGKGSYWTLD 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                         YRDNKQGWQNSIRHNLSLNECFVKVPRDDKKPGKGSYWTLD

Mouse                         YRDNKQGWQNSIRHNLSLNECFVKVPRDDKKPGKGSYWTLD

Xenopus tropicalis            YRDNKQGWQNSIRHNLSLNECFVKVPRDDKKPGKGSYWTLD
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 – 553 Forkhead box protein C1
DNA binding 77 – 168 Fork-head
Mutagenesis 126 – 126 I -> A. Decreased nuclear localization. Decreased DNA-binding activity. Decreased transcriptional activity.
Mutagenesis 126 – 126 I -> E. Decreased nuclear localization. Decreased DNA-binding activity. Decreased transcriptional activity.
Mutagenesis 126 – 126 I -> K. Decreased nuclear localization. Decreased DNA-binding activity. Decreased transcriptional activity.
Mutagenesis 127 – 127 R -> A. Decreased nuclear localization. Decreased DNA-binding activity. Decreased transcriptional activity.
Mutagenesis 127 – 127 R -> E. Decreased nuclear localization. Decreased DNA-binding activity. Decreased transcriptional activity.
Mutagenesis 127 – 127 R -> K. Decreased nuclear localization. Decreased DNA-binding activity. Decreased transcriptional activity.



Literature citations
Comparison of bioinformatics prediction, molecular modeling, and functional analyses of FOXC1 mutations in patients with Axenfeld-Rieger syndrome.
Seifi M.; Footz T.; Taylor S.A.; Walter M.A.;
Hum. Mutat. 38:169-179(2017)
Cited for: VARIANTS RIEG3 ARG-128; TYR-135 AND VAL-161; VARIANT ASN-368; CHARACTERIZATION OF VARIANTS RIEG3 ARG-128; TYR-135 AND VAL-161; CHARACTERIZATION OF VARIANT ASN-368; FUNCTION; SUBCELLULAR LOCATION;
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.