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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P02545: Variant p.Thr150Pro

Prelamin-A/C
Gene: LMNA
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Variant information Variant position: help 150 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 Threonine (T) to Proline (P) at position 150 (T150P, p.Thr150Pro). 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 (T) to medium size and hydrophobic (P) 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 150 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 AQARLKDLEALLNSKEAALS T ALSEKRTLEGELHDLRGQVA 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                         AQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVA

Mouse                         AQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVA

Rat                           AQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVA

Pig                           AQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVA

Chicken                       AQARLKDLEALLNSKEAALSTALGEKRNLENEVRDLRAQVA

Xenopus laevis                AQARLKDLEALLNSKDAALTTALGEKRNLENEIRELKAHIA
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 81 – 218 Coil 1B
Modified residue 135 – 135 N6-acetyllysine
Modified residue 155 – 155 N6-acetyllysine



Literature citations
Autosomal dominant Emery-Dreifuss dystrophy due to mutations in rod domain of the lamin A/C gene.
Felice K.J.; Schwartz R.C.; Brown C.A.; Leicher C.R.; Grunnet M.L.;
Neurology 55:275-280(2000)
Cited for: VARIANTS EDMD2 PRO-150 AND LYS-261 DEL; Novel LMNA mutations in patients with Emery-Dreifuss muscular dystrophy and functional characterization of four LMNA mutations.
Scharner J.; Brown C.A.; Bower M.; Iannaccone S.T.; Khatri I.A.; Escolar D.; Gordon E.; Felice K.; Crowe C.A.; Grosmann C.; Meriggioli M.N.; Asamoah A.; Gordon O.; Gnocchi V.F.; Ellis J.A.; Mendell J.R.; Zammit P.S.;
Hum. Mutat. 32:152-167(2011)
Cited for: VARIANTS EDMD2 SER-39; CYS-45; PRO-150; PRO-189; ARG-190 INS; LEU-206; TRP-249; GLN-249; PRO-268; PRO-271; PRO-294; PRO-295; PRO-303; GLN-355 DEL; LYS-358; LYS-361; LYS-386; ASP-449; TRP-453; PRO-454; TYR-461; ARG-467; PRO-527; LYS-528; ARG-528; SER-541; PRO-541; SER-602 AND CYS-644; CHARACTERIZATION OF VARIANTS EDMD2 PRO-25; TRP-249; ILE-456 AND PRO-541;
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.