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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P49336: Variant p.Arg178Gln

Cyclin-dependent kinase 8
Gene: CDK8
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Variant information Variant position: help 178 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 Arginine (R) to Glutamine (Q) at position 178 (R178Q, p.Arg178Gln). 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 large size and basic (R) to medium size and polar (Q) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 1 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 IDDHBA; decreased protein kinase activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 178 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 464 The length of the canonical sequence.
Location on the sequence: help LVMGEGPERGRVKIADMGFA R LFNSPLKPLADLDPVVVTFW 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                         LVMGEGPE--RGRVKIADMGFARLFNSPLKPLADLDPVVVTFW

Mouse                         LVMGEGPE--RGRVKIADMGFARLFNSPLKPLADLDPVVVT

Xenopus laevis                LVMGEGPE--RGRVKIADMGFARLFNSPLKPLADLDPVVVT

Xenopus tropicalis            LVMGEGPE--RGRVKIADMGFARLFNSPLKPLADLDPVVVT

Zebrafish                     LVMGEGPE--RGRVKIADMGFARLSNSPLKPLADLDPVVVT

Caenorhabditis elegans        LLMGDGPPDMRGRVKIADLGFSRIYANPLKPMAELDPVVVT

Drosophila                    LVMGDGNE--RGRVKIADMGFARLFNAPLKPLADLDPVVVT

Slime mold                    LVMGEGKE--CGTVKIGDFGLARIFQSPLKPLNE-NGVVVT

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 – 464 Cyclin-dependent kinase 8
Domain 21 – 335 Protein kinase
Mutagenesis 173 – 173 D -> A. Abrogates kinase activity and TFIIH-dependent transcriptional repression.
Turn 174 – 178



Literature citations
De Novo Missense Substitutions in the Gene Encoding CDK8, a Regulator of the Mediator Complex, Cause a Syndromic Developmental Disorder.
Calpena E.; Hervieu A.; Kaserer T.; Swagemakers S.M.A.; Goos J.A.C.; Popoola O.; Ortiz-Ruiz M.J.; Barbaro-Dieber T.; Bownass L.; Brilstra E.H.; Brimble E.; Foulds N.; Grebe T.A.; Harder A.V.E.; Lees M.M.; Monaghan K.G.; Newbury-Ecob R.A.; Ong K.R.; Osio D.; Reynoso Santos F.J.; Ruzhnikov M.R.Z.; Telegrafi A.; van Binsbergen E.; van Dooren M.F.; van der Spek P.J.; Blagg J.; Twigg S.R.F.; Mathijssen I.M.J.; Clarke P.A.; Wilkie A.O.M.;
Am. J. Hum. Genet. 104:709-720(2019)
Cited for: INVOLVEMENT IN IDDHBA; VARIANTS IDDHBA LEU-27; GLY-29; SER-30; LEU-62; LEU-97; GLN-178; GLY-193 AND MET-223; CHARACTERIZATION OF VARIANTS IDDHBA LEU-27; GLY-29; SER-30; LEU-62; GLN-178; GLY-193 AND MET-223; FUNCTION; MUTAGENESIS OF ASP-173;
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.