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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P84243: Variant p.Asp78Asn

Histone H3.3
Gene: H3-3B
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Variant information Variant position: help 78 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help US 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 Aspartate (D) to Asparagine (N) at position 78 (D78N, p.Asp78Asn). 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 medium size and acidic (D) to medium size and polar (N) 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 BRYLIB1; uncertain significance. Any additional useful information about the variant.


Sequence information Variant position: help 78 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 STELLIRKLPFQRLVREIAQ D FKTDLRFQSAAIGALQEASE 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
Modified residue 58 – 58 Phosphoserine
Modified residue 65 – 65 N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue 65 – 65 N6-methyllysine; alternate
Modified residue 80 – 80 N6,N6,N6-trimethyllysine; alternate
Modified residue 80 – 80 N6,N6-dimethyllysine; alternate
Modified residue 80 – 80 N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue 80 – 80 N6-(beta-hydroxybutyryl)lysine; alternate
Modified residue 80 – 80 N6-acetyllysine; alternate
Modified residue 80 – 80 N6-glutaryllysine; alternate
Modified residue 80 – 80 N6-lactoyllysine; alternate
Modified residue 80 – 80 N6-methyllysine; alternate
Modified residue 80 – 80 N6-succinyllysine; alternate
Modified residue 81 – 81 Phosphothreonine
Modified residue 87 – 87 Phosphoserine



Literature citations
Histone H3.3 beyond cancer: Germline mutations in Histone 3 Family 3A and 3B cause a previously unidentified neurodegenerative disorder in 46 patients.
Bryant L.; Li D.; Cox S.G.; Marchione D.; Joiner E.F.; Wilson K.; Janssen K.; Lee P.; March M.E.; Nair D.; Sherr E.; Fregeau B.; Wierenga K.J.; Wadley A.; Mancini G.M.S.; Powell-Hamilton N.; van de Kamp J.; Grebe T.; Dean J.; Ross A.; Crawford H.P.; Powis Z.; Cho M.T.; Willing M.C.; Manwaring L.; Schot R.; Nava C.; Afenjar A.; Lessel D.; Wagner M.; Klopstock T.; Winkelmann J.; Catarino C.B.; Retterer K.; Schuette J.L.; Innis J.W.; Pizzino A.; Luettgen S.; Denecke J.; Strom T.M.; Monaghan K.G.; Yuan Z.F.; Dubbs H.; Bend R.; Lee J.A.; Lyons M.J.; Hoefele J.; Guenthner R.; Reutter H.; Keren B.; Radtke K.; Sherbini O.; Mrokse C.; Helbig K.L.; Odent S.; Cogne B.; Mercier S.; Bezieau S.; Besnard T.; Kury S.; Redon R.; Reinson K.; Wojcik M.H.; Ounap K.; Ilves P.; Innes A.M.; Kernohan K.D.; Costain G.; Meyn M.S.; Chitayat D.; Zackai E.; Lehman A.; Kitson H.; Martin M.G.; Martinez-Agosto J.A.; Nelson S.F.; Palmer C.G.S.; Papp J.C.; Parker N.H.; Sinsheimer J.S.; Vilain E.; Wan J.; Yoon A.J.; Zheng A.; Brimble E.; Ferrero G.B.; Radio F.C.; Carli D.; Barresi S.; Brusco A.; Tartaglia M.; Thomas J.M.; Umana L.; Weiss M.M.; Gotway G.; Stuurman K.E.; Thompson M.L.; McWalter K.; Stumpel C.T.R.M.; Stevens S.J.C.; Stegmann A.P.A.; Tveten K.; Voello A.; Prescott T.; Fagerberg C.; Laulund L.W.; Larsen M.J.; Byler M.; Lebel R.R.; Hurst A.C.; Dean J.; Schrier Vergano S.A.; Norman J.; Mercimek-Andrews S.; Neira J.; Van Allen M.I.; Longo N.; Sellars E.; Louie R.J.; Cathey S.S.; Brokamp E.; Heron D.; Snyder M.; Vanderver A.; Simon C.; de la Cruz X.; Padilla N.; Crump J.G.; Chung W.; Garcia B.; Hakonarson H.H.; Bhoj E.J.;
Sci. Adv. 6:0-0(2020)
Cited for: VARIANTS BRYLIB1 GLY-9; SER-9; GLY-16; GLY-18; ILE-23; THR-30; PHE-32; GLU-37; TYR-40; ILE-46; ARG-62; ASN-78; HIS-82; CYS-84; ARG-91; SER-109; LEU-113; VAL-113; LEU-118; ILE-121; LYS-121; ARG-122; LEU-122; ARG-126 AND CYS-129; VARIANTS BRYLIB2 CYS-9; PRO-11; ARG-14; PRO-30; VAL-35; ARG-40; ARG-49; SER-109; VAL-121; ARG-122 AND ARG-126; INVOLVEMENT IN BRYLIB1; INVOLVEMENT IN BRYLIB2;
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.