UniProtKB/Swiss-Prot P84243: Variant p.Ile52Asn

• Variant information
• Sequence information
• Literature citations
• All

Variant information

Variant position: 52 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: 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: From Isoleucine (I) to Asparagine (N) at position 52 (I52N, p.Ile52Asn). 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: Change from medium size and hydrophobic (I) to medium size and polar (N) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: -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: In BRYLIB2; uncertain significance; decreased protein abundance. Any additional useful information about the variant.

Sequence information

Variant position: 52 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 136 The length of the canonical sequence.
Location on the sequence: STGGVKKPHRYRPGTVALRE I RRYQKSTELLIRKLPFQRLV 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: 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	2 – 136	Histone H3.3
Site	32 – 32	Interaction with ZMYND11
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
Modified residue	57 – 57	N6,N6,N6-trimethyllysine; alternate
Modified residue	57 – 57	N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue	57 – 57	N6-(beta-hydroxybutyryl)lysine; alternate
Modified residue	57 – 57	N6-acetyllysine; alternate
Modified residue	57 – 57	N6-crotonyllysine; alternate
Modified residue	57 – 57	N6-glutaryllysine; alternate
Modified residue	57 – 57	N6-lactoyllysine; alternate
Modified residue	57 – 57	N6-methyllysine; by EHMT2; alternate
Modified residue	57 – 57	N6-succinyllysine; alternate
Modified residue	58 – 58	Phosphoserine
Modified residue	65 – 65	N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue	65 – 65	N6-methyllysine; alternate
Mutagenesis	43 – 43	R -> K. Reduced binding of histone H1 to histone H3.3-containing nucleosomes.
Helix	49 – 59

Literature citations

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;