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UniProtKB/Swiss-Prot P50402: Variant p.Ser54Phe

Emerin
Gene: EMD
Variant information

Variant position:  54
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Serine (S) to Phenylalanine (F) at position 54 (S54F, p.Ser54Phe).
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:  Change from small size and polar (S) to large size and aromatic (F)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -2
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:  In EDMD1; no loss of binding to F-actin, enhanced rate of actin polymerization and loss of binding to BCLAF1.
Any additional useful information about the variant.



Sequence information

Variant position:  54
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  254
The length of the canonical sequence.

Location on the sequence:   YEKKIFEYETQRRRLSPPSS  S AASSYSFSDLNSTRGDADMY
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: 
The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         YEKKIFEYETQRRRLSPPSSSAAS-SYSFSDLNSTRGDADMY

Mouse                         YEKKIFEYETQRRRLLPPNSSSSSFSYQFSDLDSAAVDSDM

Rat                           YEKKIFEYETQRRRLSPPSSSSSSFSYRFSDLDSASVDSDM

Sequence annotation in neighborhood:  
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 – 254 Emerin
Region 46 – 222 Interaction with F-actin
Modified residue 49 – 49 Phosphoserine; by PKA
Modified residue 54 – 54 Phosphoserine
Modified residue 60 – 60 Phosphoserine
Mutagenesis 49 – 49 S -> A. Abolishes phosphorylation. No effect on targeting to nuclear envelope nor on interaction with LMNA.
Mutagenesis 49 – 49 S -> E. Mimics phosphorylation. No effect on targeting to nuclear envelope nor on interaction with LMNA.


Literature citations

Emerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by a missense mutation that causes Emery-Dreifuss muscular dystrophy.
Haraguchi T.; Holaska J.M.; Yamane M.; Koujin T.; Hashiguchi N.; Mori C.; Wilson K.L.; Hiraoka Y.;
Eur. J. Biochem. 271:1035-1045(2004)
Cited for: INTERACTION WITH BCLAF1; CHARACTERIZATION OF VARIANT EDMD1 PHE-54;

Emerin caps the pointed end of actin filaments: evidence for an actin cortical network at the nuclear inner membrane.
Holaska J.M.; Kowalski A.K.; Wilson K.L.;
PLoS Biol. 2:1354-1362(2004)
Cited for: FUNCTION; INTERACTION WITH ACTB; SPTAN1 AND F-ACTIN; MUTAGENESIS OF SER-196 AND SER-197; CHARACTERIZATION OF VARIANTS EDMD1 PHE-54; HIS-133 AND HIS-183;

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.