UniProtKB/Swiss-Prot O95999: Variant p.Thr52Ile

B-cell lymphoma/leukemia 10
Gene: BCL10
Feedback?

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 Threonine (T) to Isoleucine (I) at position 52 (T52I, p.Thr52Ile). 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 polar (T) to medium size and hydrophobic (I) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-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:

Found in a mesothelioma sample; uncertain significance. 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:

233 The length of the canonical sequence.
Location on the sequence:

IIAERHFDHLRAKKILSRED T EEISCRTSSRKRAGKLLDYL 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:

The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         IIAERHFDHLRAKKILSREDTEEISCRTSSRKRAGKLLDYL

Mouse                         IIAERHFDHLRAKKILSREDTEEISCRTSSRKRAGKLLDYL

Rat                           IIAERHFDHLRAKKILSREDTEEISCRTSSRKRAGKLLDYL

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	1 – 233	B-cell lymphoma/leukemia 10
Domain	13 – 101	CARD
Cross	63 – 63	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Mutagenesis	36 – 36	R -> E. Abolished homomultimerization and formation of a CBM complex, abolished ability to activate NF-kappa-B.
Mutagenesis	41 – 41	L -> A. Abolishes cell death-inducing capability.
Mutagenesis	41 – 41	L -> Q. Abolishes NF-kappa-B activation and homo/heterodimerization.
Mutagenesis	46 – 46	I -> A. Abolishes cell death-inducing capability.
Mutagenesis	47 – 47	L -> A. Abolishes cell death-inducing capability.
Mutagenesis	50 – 50	E -> R. Abolished homomultimerization and formation of a CBM complex, abolished ability to activate NF-kappa-B.
Mutagenesis	53 – 53	E -> A. Abolishes cell death-inducing capability.
Mutagenesis	53 – 53	E -> R. Abolished homomultimerization and formation of a CBM complex, abolished ability to activate NF-kappa-B.
Mutagenesis	55 – 55	I -> A. Abolishes cell death-inducing capability.
Mutagenesis	63 – 63	K -> R. Decreased ubiquitination and ability to bind NEMO, impaired ability to activate NF-kappa-B; when associated with R-31. Decreased linear ubiquitination and impaired ability to activate NF-kappa-B; when associated with R-17 and R-31.
Helix	49 – 53

Literature citations
Bcl10 is involved in t(1;14)(p22;q32) of MALT B cell lymphoma and mutated in multiple tumor types.
Willis T.G.; Jadayel D.M.; Du M.-Q.; Peng H.; Perry A.R.; Abdul-Rauf M.; Price H.; Karran L.; Majekodunmi O.; Wlodarska I.; Pan L.; Crook T.; Hamoudi R.; Isaacson P.; Dyer M.J.S.;
Cell 96:35-45(1999)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; TISSUE SPECIFICITY; INVOLVEMENT IN MALTOMA; VARIANTS ILE-52; GLY-58; GLU-210 DEL AND PHE-218;

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.