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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P14678: Variant p.Asn55Ser

Small nuclear ribonucleoprotein-associated proteins B and B'
Gene: SNRPB
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Variant information Variant position: help 55 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 Asparagine (N) to Serine (S) at position 55 (N55S, p.Asn55Ser). 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 polar (N) to small size and polar (S) 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 CCMS; expression of the protein is reduced. Any additional useful information about the variant.


Sequence information Variant position: help 55 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 240 The length of the canonical sequence.
Location on the sequence: help DKHMNLILCDCDEFRKIKPK N SKQAEREEKRVLGLVLLRGE 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                         DKHMNLILCDCDEFR-------KIKPKN-SKQ----AEREEKRVLGLVLLRGE

Mouse                         DKHMNLILCDCDEFR-------KIKPKN-SKQ----AEREE

Rat                           DKHMNLILCDCDEFR-------KIKPKN-SKQ----AEREE

Bovine                        DKHMNLILCDCDEFR-------KIKPKN-SKQ----AEREE

Chicken                       DKHMNLILCDCDEFR-------KIKPKN-SKQ----PEREE

Caenorhabditis elegans        DKHMNILLAECEEHR-------QIKPKA-GKK----TDGEE

Drosophila                    DKHMNLILGDCEEFR-------KIRSKN-SKV----PEREE

Slime mold                    DKHMNVVICDAEEFR-------RIRQK--GKE-----DREE

Baker's yeast                 DKHMNLVLNECIEERVPKTQLDKLRPRKDSKDGTTLNIKVE

Fission yeast                 DGFMNLVLSDCQEYR-------HIKKQNVPSN----SVYEE
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 – 240 Small nuclear ribonucleoprotein-associated proteins B and B'
Domain 4 – 86 Sm
Beta strand 54 – 58



Literature citations
Disrupted auto-regulation of the spliceosomal gene SNRPB causes cerebro-costo-mandibular syndrome.
Lynch D.C.; Revil T.; Schwartzentruber J.; Bhoj E.J.; Innes A.M.; Lamont R.E.; Lemire E.G.; Chodirker B.N.; Taylor J.P.; Zackai E.H.; McLeod D.R.; Kirk E.P.; Hoover-Fong J.; Fleming L.; Savarirayan R.; Majewski J.; Jerome-Majewska L.A.; Parboosingh J.S.; Bernier F.P.;
Nat. Commun. 5:4483-4483(2014)
Cited for: INVOLVEMENT IN CCMS; VARIANTS CCMS SER-55; ARG-56 AND TRP-56; CHARACTERIZATION OF VARIANTS CCMS SER-55; Mutations in SNRPB, encoding components of the core splicing machinery, cause cerebro-costo-mandibular syndrome.
Bacrot S.; Doyard M.; Huber C.; Alibeu O.; Feldhahn N.; Lehalle D.; Lacombe D.; Marlin S.; Nitschke P.; Petit F.; Vazquez M.P.; Munnich A.; Cormier-Daire V.;
Hum. Mutat. 36:187-190(2015)
Cited for: INVOLVEMENT IN CCMS; VARIANTS CCMS SER-55; THR-55 AND ARG-56;
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.