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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P84243: Variant p.Pro122Leu

Histone H3.3
Gene: H3-3B
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Variant information Variant position: help 122 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 Proline (P) to Leucine (L) at position 122 (P122L, p.Pro122Leu). 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 Similar physico-chemical property. Both residues are medium size and hydrophobic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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. Any additional useful information about the variant.


Sequence information Variant position: help 122 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 VGLFEDTNLCAIHAKRVTIM P KDIQLARRIRGERA 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 108 – 108 Phosphothreonine
Modified residue 116 – 116 N6-acetyllysine; alternate
Modified residue 116 – 116 N6-glutaryllysine; alternate
Modified residue 123 – 123 N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue 123 – 123 N6-(beta-hydroxybutyryl)lysine; alternate
Modified residue 123 – 123 N6-acetyllysine; alternate
Modified residue 123 – 123 N6-glutaryllysine; alternate
Modified residue 123 – 123 N6-methyllysine; alternate
Modified residue 123 – 123 N6-succinyllysine; alternate
Helix 122 – 131



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; De novo variants in H3-3A and H3-3B are associated with neurodevelopmental delay, dysmorphic features, and structural brain abnormalities.
Okur V.; Chen Z.; Vossaert L.; Peacock S.; Rosenfeld J.; Zhao L.; Du H.; Calamaro E.; Gerard A.; Zhao S.; Kelsay J.; Lahr A.; Mighton C.; Porter H.M.; Siemon A.; Silver J.; Svihovec S.; Fong C.T.; Grant C.L.; Lerner-Ellis J.; Manickam K.; Madan-Khetarpal S.; McCandless S.E.; Morel C.F.; Schaefer G.B.; Berry-Kravis E.M.; Gates R.; Gomez-Ospina N.; Qiu G.; Zhang T.J.; Wu Z.; Meng L.; Liu P.; Scott D.A.; Lupski J.R.; Eng C.M.; Wu N.; Yuan B.;
NPJ Genom. Med. 6:104-104(2021)
Cited for: VARIANTS BRYLIB1 CYS-41; LYS-56; ARG-91; ILE-121; LEU-122 AND HIS-129; VARIANTS BRYLIB2 VAL-8; CYS-9; GLU-10; LYS-23 AND ASN-52; CHARACTERIZATION OF VARIANTS BRYLIB1 CYS-41; LYS-56; ARG-91; ILE-121; LEU-122 AND HIS-129; CHARACTERIZATION OF VARIANTS BRYLIB2 VAL-8; GLU-10; LYS-23 AND ASN-52; SUBCELLULAR LOCATION; INTERACTION WITH DAXX; 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.