Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P84243: Variant p.Gly35Arg

Histone H3.3
Gene: H3-3B
Feedback?
Variant information Variant position: help 35 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 Arginine (R) at position 35 (G35R, p.Gly35Arg). 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 large size and basic (R) 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 GLM; glioblastoma multiforme samples; somatic mutation; also found in osteosarcoma samples; results in global decrease of H3K36me2 and H3K36me3 levels; has no effect on H3K27me3 levels. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 35 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 136 The length of the canonical sequence.
Location on the sequence: help KAPRKQLATKAARKSAPSTG G VKKPHRYRPGTVALREIRRY 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.
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 – 136 Histone H3.3
Region 1 – 43 Disordered
Site 32 – 32 Interaction with ZMYND11
Modified residue 15 – 15 N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue 15 – 15 N6-(beta-hydroxybutyryl)lysine; alternate
Modified residue 15 – 15 N6-acetyllysine; alternate
Modified residue 15 – 15 N6-glutaryllysine; alternate
Modified residue 15 – 15 N6-lactoyllysine; alternate
Modified residue 15 – 15 N6-succinyllysine; alternate
Modified residue 18 – 18 Asymmetric dimethylarginine; by CARM1; alternate
Modified residue 18 – 18 Citrulline; alternate
Modified residue 19 – 19 N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue 19 – 19 N6-(beta-hydroxybutyryl)lysine; alternate
Modified residue 19 – 19 N6-acetyllysine; alternate
Modified residue 19 – 19 N6-butyryllysine; alternate
Modified residue 19 – 19 N6-crotonyllysine; alternate
Modified residue 19 – 19 N6-glutaryllysine; alternate
Modified residue 19 – 19 N6-lactoyllysine; alternate
Modified residue 19 – 19 N6-methyllysine; alternate
Modified residue 24 – 24 N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue 24 – 24 N6-(beta-hydroxybutyryl)lysine; alternate
Modified residue 24 – 24 N6-acetyllysine; alternate
Modified residue 24 – 24 N6-butyryllysine; alternate
Modified residue 24 – 24 N6-crotonyllysine; alternate
Modified residue 24 – 24 N6-glutaryllysine; alternate
Modified residue 24 – 24 N6-lactoyllysine; alternate
Modified residue 24 – 24 N6-methyllysine; alternate
Modified residue 27 – 27 Citrulline
Modified residue 28 – 28 N6,N6,N6-trimethyllysine; alternate
Modified residue 28 – 28 N6,N6-dimethyllysine; alternate
Modified residue 28 – 28 N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue 28 – 28 N6-(beta-hydroxybutyryl)lysine; alternate
Modified residue 28 – 28 N6-acetyllysine; alternate
Modified residue 28 – 28 N6-crotonyllysine; alternate
Modified residue 28 – 28 N6-glutaryllysine; alternate
Modified residue 28 – 28 N6-lactoyllysine; alternate
Modified residue 28 – 28 N6-methyllysine; alternate
Modified residue 29 – 29 ADP-ribosylserine; alternate
Modified residue 29 – 29 Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5
Modified residue 32 – 32 Phosphoserine
Modified residue 37 – 37 N6,N6,N6-trimethyllysine; alternate
Modified residue 37 – 37 N6,N6-dimethyllysine; alternate
Modified residue 37 – 37 N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue 37 – 37 N6-acetyllysine; alternate
Modified residue 37 – 37 N6-methyllysine; alternate
Modified residue 38 – 38 N6-methyllysine
Modified residue 42 – 42 Phosphotyrosine
Lipidation 19 – 19 N6-decanoyllysine
Mutagenesis 43 – 43 R -> K. Reduced binding of histone H1 to histone H3.3-containing nucleosomes.
Beta strand 35 – 37



Literature citations
Driver mutations in histone H3.3 and chromatin remodelling genes in paediatric glioblastoma.
Schwartzentruber J.; Korshunov A.; Liu X.Y.; Jones D.T.; Pfaff E.; Jacob K.; Sturm D.; Fontebasso A.M.; Quang D.A.; Toenjes M.; Hovestadt V.; Albrecht S.; Kool M.; Nantel A.; Konermann C.; Lindroth A.; Jaeger N.; Rausch T.; Ryzhova M.; Korbel J.O.; Hielscher T.; Hauser P.; Garami M.; Klekner A.; Bognar L.; Ebinger M.; Schuhmann M.U.; Scheurlen W.; Pekrun A.; Fruehwald M.C.; Roggendorf W.; Kramm C.; Duerken M.; Atkinson J.; Lepage P.; Montpetit A.; Zakrzewska M.; Zakrzewski K.; Liberski P.P.; Dong Z.; Siegel P.; Kulozik A.E.; Zapatka M.; Guha A.; Malkin D.; Felsberg J.; Reifenberger G.; von Deimling A.; Ichimura K.; Collins V.P.; Witt H.; Milde T.; Witt O.; Zhang C.; Castelo-Branco P.; Lichter P.; Faury D.; Tabori U.; Plass C.; Majewski J.; Pfister S.M.; Jabado N.;
Nature 482:226-231(2012)
Cited for: VARIANTS GLM MET-28; ARG-35 AND VAL-35; INVOLVEMENT IN GLM; Inhibition of PRC2 activity by a gain-of-function H3 mutation found in pediatric glioblastoma.
Lewis P.W.; Mueller M.M.; Koletsky M.S.; Cordero F.; Lin S.; Banaszynski L.A.; Garcia B.A.; Muir T.W.; Becher O.J.; Allis C.D.;
Science 340:857-861(2013)
Cited for: CHARACTERIZATION OF VARIANTS GLM MET-28; ARG-35 AND VAL-35;
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.