Sequence information
Variant position: 1169 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:
DTVIIFDSDWNPHNDIQAFS
R AHRIGQANKVMIYRFVTRAS
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 DTVIIFDSDWNPHNDIQAFSR AHRIGQANKVMIYRFVTRAS
Caenorhabditis elegans DTVIIYDSDWNPHNDIQAFSR AHRLGQKHKVMIYRFVTKGS
Drosophila DTVIIFDSDWNPHNDVQAFSR AHRMGQKKKVMIYRFVTHNS
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.
Type Positions Description
Chain
1 – 2000
Chromodomain-helicase-DNA-binding protein 3
Domain
1064 – 1229
Helicase C-terminal
Literature citations
A set of regulatory genes co-expressed in embryonic human brain is implicated in disrupted speech development.
Eising E.; Carrion-Castillo A.; Vino A.; Strand E.A.; Jakielski K.J.; Scerri T.S.; Hildebrand M.S.; Webster R.; Ma A.; Mazoyer B.; Francks C.; Bahlo M.; Scheffer I.E.; Morgan A.T.; Shriberg L.D.; Fisher S.E.;
Mol. Psychiatry 24:1065-1078(2019)
Cited for: INVOLVEMENT IN SNIBCPS; VARIANT SNIBCPS TRP-1169;
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.