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UniProtKB/Swiss-Prot Q12873: Variant p.Asp1120His

Chromodomain-helicase-DNA-binding protein 3
Gene: CHD3
Variant information

Variant position:  1120
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Disease [Disclaimer]
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Aspartate (D) to Histidine (H) at position 1120 (D1120H, p.Asp1120His).
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:  Change from medium size and acidic (D) to medium size and polar (H)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -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

Involvement in disease:  Snijders Blok-Campeau syndrome (SNIBCPS) [MIM:618205]: An autosomal dominant neurodevelopmental disorder characterized by intellectual disability with a wide range of severity, developmental delay, and impaired speech and language skills. Speech-related problems include dysarthria, speech apraxia, oromotor problems, and stuttering. Additional clinical features are macrocephaly, characteristic facial features such as prominent forehead and hypertelorism, hypotonia, and joint laxity. {ECO:0000269|PubMed:29463886, ECO:0000269|PubMed:30397230}. Note=The disease is caused by mutations affecting the gene represented in this entry.
The name and a short description of the disease associated with the variant. For more information about the disease, the user can refer to OMIM, following the link provided after the disease acronym.

Variant description:  In SNIBCPS; the patient also carries a truncating variant in CIC; both variants may contribute to disease phenotype.
Any additional useful information about the variant.



Sequence information

Variant position:  1120
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  2000
The length of the canonical sequence.

Location on the sequence:   GYKYERIDGGITGALRQEAI  D RFNAPGAQQFCFLLSTRAGG
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: 
The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         GYKYERIDGGITGALRQEAIDRFNAPGAQQFCFLLSTRAGG

Caenorhabditis elegans        GYKYERIDGSITGQQRQDAIDRYNAPGAKQFVFLLSTRAGG

Drosophila                    GYQYDRIDGSIKGDLRQKAIDRFNDPVSEHFVFLLSTRAGG

Sequence annotation in neighborhood:  
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 – 2000 Chromodomain-helicase-DNA-binding protein 3
Domain 1064 – 1229 Helicase C-terminal


Literature citations

CHD3 helicase domain mutations cause a neurodevelopmental syndrome with macrocephaly and impaired speech and language.
Snijders Blok L.; Rousseau J.; Twist J.; Ehresmann S.; Takaku M.; Venselaar H.; Rodan L.H.; Nowak C.B.; Douglas J.; Swoboda K.J.; Steeves M.A.; Sahai I.; Stumpel C.T.R.M.; Stegmann A.P.A.; Wheeler P.; Willing M.; Fiala E.; Kochhar A.; Gibson W.T.; Cohen A.S.A.; Agbahovbe R.; Innes A.M.; Au P.Y.B.; Rankin J.; Anderson I.J.; Skinner S.A.; Louie R.J.; Warren H.E.; Afenjar A.; Keren B.; Nava C.; Buratti J.; Isapof A.; Rodriguez D.; Lewandowski R.; Propst J.; van Essen T.; Choi M.; Lee S.; Chae J.H.; Price S.; Schnur R.E.; Douglas G.; Wentzensen I.M.; Zweier C.; Reis A.; Bialer M.G.; Moore C.; Koopmans M.; Brilstra E.H.; Monroe G.R.; van Gassen K.L.I.; van Binsbergen E.; Newbury-Ecob R.; Bownass L.; Bader I.; Mayr J.A.; Wortmann S.B.; Jakielski K.J.; Strand E.A.; Kloth K.; Bierhals T.; Roberts J.D.; Petrovich R.M.; Machida S.; Kurumizaka H.; Lelieveld S.; Pfundt R.; Jansen S.; Deriziotis P.; Faive L.; Thevenon J.; Assoum M.; Shriberg L.; Kleefstra T.; Brunner H.G.; Wade P.A.; Fisher S.E.; Campeau P.M.;
Nat. Commun. 9:4619-4619(2018)
Cited for: FUNCTION; CATALYTIC ACTIVITY; INVOLVEMENT IN SNIBCPS; VARIANTS SNIBCPS 457-GLU--ASP-2000 DEL; ARG-886; PHE-915; LYS-921; GLU-961; GLN-985; TRP-985; GLY-1109 DEL; HIS-1120; PRO-1121; ILE-1136; ARG-1158; LYS-1159; ARG-1161; TRP-1169; ARG-1171; GLN-1172; PRO-1187; PRO-1236; GLN-1342 AND LEU-1881; CHARACTERIZATION OF VARIANTS SNIBCPS PHE-915; PRO-1121; ARG-1158; LYS-1159; GLN-1172 AND PRO-1187;

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.