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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P62805: Variant p.Lys92Gln

Histone H4
Gene: H4C16
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Variant information Variant position: help 92 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 Lysine (K) to Glutamine (Q) at position 92 (K92Q, p.Lys92Gln). 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 (K) 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 TEBIVANED1; results in severe early developmental defects when expressed in zebrafish embryos; results in defective cell cycle progression when expressed in zebrafish embryos. Any additional useful information about the variant.


Sequence information Variant position: help 92 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 103 The length of the canonical sequence.
Location on the sequence: help TYTEHAKRKTVTAMDVVYAL K RQGRTLYGFGG 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                         TYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG

Mouse                         TYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG

Rat                           TYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG

Pig                           TYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG

Bovine                        TYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG

Chicken                       TYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG

Xenopus laevis                TYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG

Xenopus tropicalis            TYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG

Caenorhabditis elegans        TYCEHAKRKTVTAMDVVYALKRQGRTLYGFGG

Drosophila                    TYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG

Slime mold                    AYTEHAGRRTVTAMDVVYALKRQGRTLYGFNS

Baker's yeast                 TYTEHAKRKTVTSLDVVYALKRQGRTLYGFGG

Fission yeast                 TYTEHAKRKTVTSLDVVYSLKRQGRTIYGFGG
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 – 103 Histone H4
Modified residue 78 – 78 N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue 78 – 78 N6-(beta-hydroxybutyryl)lysine; alternate
Modified residue 78 – 78 N6-butyryllysine; alternate
Modified residue 78 – 78 N6-glutaryllysine; alternate
Modified residue 78 – 78 N6-isonicotinyllysine; alternate
Modified residue 78 – 78 N6-lactoyllysine; alternate
Modified residue 78 – 78 N6-methacryllysine; alternate
Modified residue 78 – 78 N6-propionyllysine; alternate
Modified residue 78 – 78 N6-succinyllysine; alternate
Modified residue 80 – 80 N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue 80 – 80 N6-butyryllysine; alternate
Modified residue 80 – 80 N6-glutaryllysine; alternate
Modified residue 80 – 80 N6-isonicotinyllysine; alternate
Modified residue 80 – 80 N6-methacryllysine; alternate
Modified residue 80 – 80 N6-propionyllysine; alternate
Modified residue 80 – 80 N6-succinyllysine; alternate
Modified residue 81 – 81 Phosphothreonine
Modified residue 89 – 89 Phosphotyrosine
Modified residue 92 – 92 N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue 92 – 92 N6-(beta-hydroxybutyryl)lysine; alternate
Modified residue 92 – 92 N6-acetyllysine; alternate
Modified residue 92 – 92 N6-butyryllysine; alternate
Modified residue 92 – 92 N6-glutaryllysine; alternate
Modified residue 92 – 92 N6-isonicotinyllysine; alternate
Modified residue 92 – 92 N6-lactoyllysine; alternate
Modified residue 92 – 92 N6-methacryllysine; alternate
Modified residue 92 – 92 N6-propionyllysine; alternate
Modified residue 92 – 92 N6-succinyllysine; alternate
Cross 80 – 80 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Cross 92 – 92 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Cross 92 – 92 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Helix 84 – 97



Literature citations
Germline mutations affecting the histone H4 core cause a developmental syndrome by altering DNA damage response and cell cycle control.
Tessadori F.; Giltay J.C.; Hurst J.A.; Massink M.P.; Duran K.; Vos H.R.; van Es R.M.; Scott R.H.; van Gassen K.L.I.; Bakkers J.; van Haaften G.;
Nat. Genet. 49:1642-1646(2017)
Cited for: VARIANTS TEBIVANED1 ARG-92 AND GLN-92; CHARACTERIZATION OF VARIANTS TEBIVANED1 ARG-92 AND GLN-92; INVOLVEMENT IN TEBIVANED1;
Recurrent de novo missense variants across multiple histone H4 genes underlie a neurodevelopmental syndrome.
Tessadori F.; Duran K.; Knapp K.; Fellner M.; Smithson S.; Beleza Meireles A.; Elting M.W.; Waisfisz Q.; O'Donnell-Luria A.; Nowak C.; Douglas J.; Ronan A.; Brunet T.; Kotzaeridou U.; Svihovec S.; Saenz M.S.; Thiffault I.; Del Viso F.; Devine P.; Rego S.; Tenney J.; van Haeringen A.; Ruivenkamp C.A.L.; Koene S.; Robertson S.P.; Deshpande C.; Pfundt R.; Verbeek N.; van de Kamp J.M.; Weiss J.M.M.; Ruiz A.; Gabau E.; Banne E.; Pepler A.; Bottani A.; Laurent S.; Guipponi M.; Bijlsma E.; Bruel A.L.; Sorlin A.; Willis M.; Powis Z.; Smol T.; Vincent-Delorme C.; Baralle D.; Colin E.; Revencu N.; Calpena E.; Wilkie A.O.M.; Chopra M.; Cormier-Daire V.; Keren B.; Afenjar A.; Niceta M.; Terracciano A.; Specchio N.; Tartaglia M.; Rio M.; Barcia G.; Rondeau S.; Colson C.; Bakkers J.; Mace P.D.; Bicknell L.S.; van Haaften G.;
Am. J. Hum. Genet. 109:750-758(2022)
Cited for: VARIANTS TEBIVANED1 ALA-33; LEU-33 AND GLN-92; VARIANT TEBIVANED2 CYS-41; VARIANTS TEBIVANED3 THR-32; ARG-33; TRP-36; PRO-38; CYS-41; CYS-46 AND HIS-99; VARIANTS TEBIVANED4 LEU-41 AND ARG-76; CHARACTERIZATION OF VARIANT TEBIVANED1 GLN-92; CHARACTERIZATION OF VARIANT TEBIVANED2 CYS-41; CHARACTERIZATION OF VARIANTS TEBIVANED3 THR-32; ARG-33; TRP-36; PRO-38; CYS-41 AND HIS-99; CHARACTERIZATION OF VARIANTS TEBIVANED4 LEU-41 AND ARG-76; VARIANTS HIS-41 AND ARG-95; CHARACTERIZATION OF VARIANTS HIS-41 AND ARG-95; INVOLVEMENT IN TEBIVANED1; INVOLVEMENT IN TEBIVANED2; INVOLVEMENT IN TEBIVANED3; INVOLVEMENT IN TEBIVANED4;
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.