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:
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 YEKKIFEYETQRRRLSPPSS SAAS-SYSFSDLNSTRGDADMY
Mouse YEKKIFEYETQRRRLLPPNS SSSSFSYQFSDLDSAAVDSDM
Rat YEKKIFEYETQRRRLSPPSS SSSSFSYRFSDLDSASVDSDM
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.
Type Positions Description
1 – 254 Emerin
46 – 222 Interaction with F-actin
49 – 49 Phosphoserine; by PKA
54 – 54 Phosphoserine
60 – 60 Phosphoserine
49 – 49 S -> A. Abolishes phosphorylation. No effect on targeting to nuclear envelope nor on interaction with LMNA.
49 – 49 S -> E. Mimics phosphorylation. No effect on targeting to nuclear envelope nor on interaction with LMNA.
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;
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.