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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P02545: Variant p.Arg50Ser

Prelamin-A/C
Gene: LMNA
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Variant information Variant position: help 50 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 Arginine (R) to Serine (S) at position 50 (R50S, p.Arg50Ser). 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 (R) 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 EDMD2. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 50 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 664 The length of the canonical sequence.
Location on the sequence: help QEKEDLQELNDRLAVYIDRV R SLETENAGLRLRITESEEVV 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                         QEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVV

Mouse                         QEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVV

Rat                           QEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVV

Pig                           QEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVV

Chicken                       QEKEDLQELNDRLAVYIDKVRSLELENAGLRLRITESEEVV

Xenopus laevis                QEKEDLQGLNDRLAVYIDKVRSLELENARLRLRITESEDVI
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 – 661 Prelamin-A/C
Chain 1 – 646 Lamin-A/C
Domain 31 – 387 IF rod
Region 1 – 130 Interaction with MLIP
Region 34 – 70 Coil 1A
Modified residue 32 – 32 N6-acetyllysine; alternate
Modified residue 32 – 32 N6-succinyllysine; alternate
Modified residue 51 – 51 Phosphoserine
Modified residue 66 – 66 Phosphoserine
Cross 32 – 32 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Alternative sequence 1 – 99 Missing. In isoform 5.
Alternative sequence 8 – 119 Missing. In isoform 4.
Mutagenesis 32 – 32 K -> Q. Impaired lamin assembly.
Mutagenesis 41 – 41 R -> H. Impaired lamin assembly.
Helix 28 – 70



Literature citations
Novel and recurrent mutations in lamin A/C in patients with Emery-Dreifuss muscular dystrophy.
Brown C.A.; Lanning R.W.; McKinney K.Q.; Salvino A.R.; Cherniske E.; Crowe C.A.; Darras B.T.; Gominak S.; Greenberg C.R.; Grosmann C.; Heydemann P.; Mendell J.R.; Pober B.R.; Sasaki T.; Shapiro F.; Simpson D.A.; Suchowersky O.; Spence J.E.;
Am. J. Med. Genet. 102:359-367(2001)
Cited for: VARIANTS EDMD2 PRO-25; THR-43; SER-50; PRO-133; 196-ARG--THR-199 DELINS SER; GLN-249; LYS-261 DEL; LYS-358; TRP-453; ILE-456; PRO-527 AND HIS-624;
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.