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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O95999: Variant p.Lys45Gln

B-cell lymphoma/leukemia 10
Gene: BCL10
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Variant information Variant position: help 45 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LB/B 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 45 (K45Q, p.Lys45Gln). 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



Sequence information Variant position: help 45 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 233 The length of the canonical sequence.
Location on the sequence: help RVYLCEKIIAERHFDHLRAK K ILSREDTEEISCRTSSRKRA 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                         RVYLCEKIIAERHFDHLRAKKILSREDTEEISCRTSSRKRA

Mouse                         RVYLCEKIIAERHFDHLRAKKILSREDTEEISCRTSSRKRA

Rat                           RVYLCEKIIAERHFDHLRAKKILSREDTEEISCRTSSRKRA

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 1 – 233 B-cell lymphoma/leukemia 10
Domain 13 – 101 CARD
Cross 31 – 31 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross 63 – 63 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Mutagenesis 28 – 28 L -> A. Abolishes cell death-inducing capability.
Mutagenesis 31 – 31 K -> R. Decreased ubiquitination and ability to bind NEMO; when associated with 63-R--R-67. Decreased ubiquitination and ability to bind NEMO, impaired ability to activate NF-kappa-B; when associated with R-63. Decreased linear ubiquitination and impaired ability to activate NF-kappa-B; when associated with R-17 and R-63.
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.



Literature citations
Absence of BCL10 mutations in human malignant mesothelioma.
Apostolou S.; de Rienzo A.; Murthy S.S.; Jhanwar S.C.; Testa J.R.;
Cell 97:684-686(1999)
Cited for: VARIANTS SER-5; GLN-45; GLN-58; SER-93; VAL-153; GLU-213 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.