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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P50402: Variant p.Pro183His

Emerin
Gene: EMD
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Variant information Variant position: help 183 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 Proline (P) to Histidine (H) at position 183 (P183H, p.Pro183His). 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 hydrophobic (P) to medium size and polar (H) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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: help In EDMD1; no loss of binding to F-actin and enhanced rate of actin polymerization. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 183 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 254 The length of the canonical sequence.
Location on the sequence: help SITHYRPVSASRSSLDLSYY P TSSSTSFMSSSSSSSSWLTR 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                         SITHYRPVS-ASRSSLDLSYYPTSSSTSFMSSSSSSSSWLTR

Mouse                         SIAHYRPISNVSRSSLGLSYYPTSSTSSVSSSSSSPSSWLT

Rat                           SIAEYRPISNVSRSSLGLSYYPRSSTSSVSSSSSSPSSWLT
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 – 254 Emerin
Region 46 – 222 Interaction with F-actin
Region 168 – 186 Interaction with CTNNB1
Modified residue 171 – 171 Phosphoserine
Modified residue 173 – 173 Phosphoserine
Modified residue 175 – 175 Phosphoserine
Mutagenesis 196 – 196 S -> A. No loss of binding to F-actin; when associated with A-197.
Mutagenesis 197 – 197 S -> A. No loss of binding to F-actin; when associated with A-196.



Literature citations
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; Changes at P183 of emerin weaken its protein-protein interactions resulting in X-linked Emery-Dreifuss muscular dystrophy.
Ellis J.A.; Yates J.R.W.; Kendrick-Jones J.; Brown C.A.;
Hum. Genet. 104:262-268(1999)
Cited for: VARIANTS EDMD1 HIS-183 AND THR-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.