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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P02545: Variant p.Asp446Val

Prelamin-A/C
Gene: LMNA
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Variant information Variant position: help 446 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 Aspartate (D) to Valine (V) at position 446 (D446V, p.Asp446Val). 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 acidic (D) to medium size and hydrophobic (V) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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: 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 446 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 SRSSFSQHARTSGRVAVEEV D EEGKFVRLRNKSNEDQSMGN 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                         SR-SSFSQHARTSGRVAVEEVDEEGKFVRLRNKSNEDQSMGN

Mouse                         SR-SSFSQHARTSGRVAVEEVDEEGKFVRLRNKSNEDQSMG

Rat                           SR-SSFSQHARTSGRVAVEEVDEEGKFVRLRNKSNEDQSMG

Pig                           SR-SSFSQHARTSGRVAVEEVDEEGKFVRLRNKSNEDQSMG

Chicken                       GR-TSFSHHARTSGRVGVEEVDLEGRFVRLRNKSNEDQALG

Xenopus laevis                SRSSSFTQHARTTGKVSVEEVDPEGKYVRLRNKSNEDQSLG
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 428 – 545 LTD
Region 384 – 664 Tail
Modified residue 426 – 426 Phosphoserine
Modified residue 429 – 429 Phosphoserine
Modified residue 431 – 431 Phosphoserine
Modified residue 450 – 450 N6-acetyllysine
Modified residue 457 – 457 N6-acetyllysine
Modified residue 458 – 458 Phosphoserine
Modified residue 463 – 463 Phosphoserine
Cross 450 – 450 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate



Literature citations
Mutation analysis of the lamin A/C gene (LMNA) among patients with different cardiomuscular phenotypes.
Vytopil M.; Benedetti S.; Ricci E.; Galluzzi G.; Dello Russo A.; Merlini L.; Boriani G.; Gallina M.; Morandi L.; Politano L.; Moggio M.; Chiveri L.; Hausmanova-Petrusewicz I.; Ricotti R.; Vohanka S.; Toman J.; Toniolo D.;
J. Med. Genet. 40:E132-E132(2003)
Cited for: VARIANTS EDMD2 GLY-25; LYS-32 DEL; VAL-35; GLY-65; GLU-112 DEL; PRO-248; GLN-249; CYS-267; VAL-446; TRP-453; ARG-528 AND HIS-541; VARIANT CMD1A CYS-435;
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.