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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P02545: Variant p.Leu530Pro

Prelamin-A/C
Gene: LMNA
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Variant information Variant position: help 530 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 Leucine (L) to Proline (P) at position 530 (L530P, p.Leu530Pro). 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 Similar physico-chemical property. Both residues are medium size and hydrophobic. 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; interacts with itself and with wild-type LMNA and LMNB1; reduced binding to SUN1; no decrease in the stability compared with wild-type. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 530 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 TDLVWKAQNTWGCGNSLRTA L INSTGEEVAMRKLVRSVTVV 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                         TDLVWKAQNTWGCGNSLRTALINSTGEEVAMRKLVRSVTVV

Mouse                         TDLVWKAQNTWGCGSSLRTALINSTGEEVAMRKLVRSLTMV

Rat                           TDLVWKAQNTWGCGTSLRTALINATGEEVAMRKLVRSLTMV

Pig                           ADLVWKSQNTWGCGNSLRTALINSTGEEVAMRKLVRSVTMI

Chicken                       SDVVWKAQSSWGSGDSLRTALINSNGEEVAMRKLVRTVIIN

Xenopus laevis                SDLVWKAQSSWGTGDSIRTALLTSSNEEVAMRKLVRTVVIN
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 510 – 510 Phosphothreonine
Modified residue 533 – 533 Phosphoserine
Modified residue 546 – 546 Phosphoserine
Modified residue 548 – 548 Phosphothreonine
Beta strand 526 – 531



Literature citations
Mammalian SUN protein interaction networks at the inner nuclear membrane and their role in laminopathy disease processes.
Haque F.; Mazzeo D.; Patel J.T.; Smallwood D.T.; Ellis J.A.; Shanahan C.M.; Shackleton S.;
J. Biol. Chem. 285:3487-3498(2010)
Cited for: INTERACTION WITH SUN1; CHARACTERIZATION OF VARIANTS EDMD2 PRO-527 AND PRO-530; CHARACTERIZATION OF VARIANT HGPS SER-608; Mutations in the gene encoding lamin A/C cause autosomal dominant Emery-Dreifuss muscular dystrophy.
Bonne G.; Di Barletta M.R.; Varnous S.; Becane H.-M.; Hammouda E.-H.; Merlini L.; Muntoni F.; Greenberg C.R.; Gary F.; Urtizberea J.-A.; Duboc D.; Fardeau M.; Toniolo D.; Schwartz K.;
Nat. Genet. 21:285-288(1999)
Cited for: VARIANTS EDMD2 TRP-453; PRO-527 AND PRO-530; FUNCTION; SUBCELLULAR LOCATION; Properties of lamin A mutants found in Emery-Dreifuss muscular dystrophy, cardiomyopathy and Dunnigan-type partial lipodystrophy.
Oestlund C.; Bonne G.; Schwartz K.; Worman H.J.;
J. Cell Sci. 114:4435-4445(2001)
Cited for: CHARACTERIZATION OF VARIANTS CMD1A GLY-60; ARG-85; LYS-195 AND GLY-203; CHARACTERIZATION OF VARIANTS EDMD2 LYS-358; LYS-371; LYS-386; TRP-453; SER-520; PRO-527; LYS-528 AND PRO-530; CHARACTERIZATION OF VARIANTS FPLD2 GLN-482; TRP-482 AND ASN-486;
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.