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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9UMX1: Variant p.His176Arg

Suppressor of fused homolog
Gene: SUFU
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Variant information Variant position: help 176 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 Histidine (H) to Arginine (R) at position 176 (H176R, p.His176Arg). 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 (H) to large size and basic (R) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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 JBTS32; decreased stability; no effect on nuclear and cytoplasmic localization; decreased interaction with GLI3; no effect on interaction with GLI1; decreased repression of the hedgehog/smoothened signaling pathway. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 176 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 484 The length of the canonical sequence.
Location on the sequence: help CSGDHVSWHSPLDNSESRIQ H MLLTEDPQMQPVQTPFGVVT 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                         CSGDHVSWHSPLDNSESRIQHMLLTEDPQMQPVQTPFGVVT

Mouse                         CSGDHVSWHSPLDNSESRIQHMLLTEDPQMQPVRTPFGVVT
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 – 484 Suppressor of fused homolog
Mutagenesis 159 – 159 D -> A. Abolishes down-regulation of GLI1 activity. Has only slight effect on GLI1 binding.
Mutagenesis 159 – 159 D -> R. Impairs interaction with GLI1 and GLI2. Abolishes interaction with GLI1 and GLI2; when associated with R-147 and R-380.
Mutagenesis 181 – 181 E -> A. No effect on down-regulation of GLI1 activity.
Beta strand 176 – 181



Literature citations
Hypomorphic Recessive Variants in SUFU Impair the Sonic Hedgehog Pathway and Cause Joubert Syndrome with Cranio-facial and Skeletal Defects.
De Mori R.; Romani M.; D'Arrigo S.; Zaki M.S.; Lorefice E.; Tardivo S.; Biagini T.; Stanley V.; Musaev D.; Fluss J.; Micalizzi A.; Nuovo S.; Illi B.; Chiapparini L.; Di Marcotullio L.; Issa M.Y.; Anello D.; Casella A.; Ginevrino M.; Leggins A.S.; Roosing S.; Alfonsi R.; Rosati J.; Schot R.; Mancini G.M.S.; Bertini E.; Dobyns W.B.; Mazza T.; Gleeson J.G.; Valente E.M.;
Am. J. Hum. Genet. 101:552-563(2017)
Cited for: FUNCTION; SUBCELLULAR LOCATION; INTERACTION WITH GLI1 AND GLI3; INVOLVEMENT IN JBTS32; VARIANTS JBTS32 ARG-176 AND THR-406; CHARACTERIZATION OF VARIANTS JBTS32 ARG-176 AND THR-406; VARIANTS VAL-19; VAL-37; MET-77; GLN-289; VAL-293; 299-ARG--HIS-484 DEL; LEU-382; ARG-442 AND ASN-481;
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.