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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9UKF6: Variant p.Gly468Glu

Cleavage and polyadenylation specificity factor subunit 3
Gene: CPSF3
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Variant information Variant position: help 468 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 Glycine (G) to Glutamate (E) at position 468 (G468E, p.Gly468Glu). 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 glycine (G) to medium size and acidic (E) 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 NEDMHS. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 468 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 684 The length of the canonical sequence.
Location on the sequence: help PRNTEAVTLNFRGEKLAKVM G FLADKKPEQGQRVSGILVKR 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                         PRNTEAVTLNFRGEKLAKVMGFLADKKPEQGQRVSGILVKR

Mouse                         PRNTEAVTLNFRGEKLAKVMGFLADKKPEQGQRVSGILVKR

Bovine                        PRNTEAVTLNFRGEKLAKVMGFLADKKPEQGQRVSGILVKR

Drosophila                    PRNTHAVDLYFRGEKTAKVMGSLAAKNSEVGSKLSGVLVKR

Slime mold                    PKNAMSVALEFRPEKVAKTLGSIITNPPKQNDIIQGILVTK
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 2 – 684 Cleavage and polyadenylation specificity factor subunit 3
Cross 462 – 462 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross 465 – 465 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Mutagenesis 462 – 462 K -> R. Reduced sumoylation; when associated with R-465 and R-545.
Mutagenesis 465 – 465 K -> R. Reduced sumoylation; when associated with R-462 and R-545.



Literature citations
Population-level deficit of homozygosity unveils CPSF3 as an intellectual disability syndrome gene.
Arnadottir G.A.; Oddsson A.; Jensson B.O.; Gisladottir S.; Simon M.T.; Arnthorsson A.O.; Katrinardottir H.; Fridriksdottir R.; Ivarsdottir E.V.; Jonasdottir A.; Jonasdottir A.; Barrick R.; Saemundsdottir J.; le Roux L.; Oskarsson G.R.; Asmundsson J.; Steffensen T.; Gudmundsson K.R.; Ludvigsson P.; Jonsson J.J.; Masson G.; Jonsdottir I.; Holm H.; Jonasson J.G.; Magnusson O.T.; Thorarensen O.; Abdenur J.; Norddahl G.L.; Gudbjartsson D.F.; Bjornsson H.T.; Thorsteinsdottir U.; Sulem P.; Stefansson K.;
Nat. Commun. 13:705-705(2022)
Cited for: VARIANTS NEDMHS THR-354 AND GLU-468; INVOLVEMENT IN NEDMHS;
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.