Variant position: 25 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 664 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 SQRRATRSGAQASSTPLSPT RITRLQEKEDLQELNDRLAVY
Mouse SQRRATRSGAQASSTPLSPT RITRLQEKEDLQELNDRLAVY
Rat SQRRPTRSGAQASSTPLSPT RITRLQEKEDLQELNDRLAVY
Pig SQRRATRSGAQASSTPLSPT RITRLQEKEDLQELNDRLAVY
Chicken SQRRSGRGGG-PSGTPLSPT RITRLQEKEDLQELNDRLAVY
Xenopus laevis GQKRATR----STHTPLSPT RITRLQEKEDLQGLNDRLAVY
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 – 661 Prelamin-A/C
1 – 646 Lamin-A/C
1 – 130 Interaction with MLIP
1 – 33 Head
12 – 12 Phosphoserine
18 – 18 Phosphoserine
19 – 19 Phosphothreonine
22 – 22 Phosphoserine
32 – 32 N6-acetyllysine; alternate
32 – 32 N6-succinyllysine; alternate
32 – 32 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
1 – 99 Missing. In isoform 5.
8 – 119 Missing. In isoform 4.
22 – 22 S -> A. Decreased accumulation to the double-strand break (DSB) sites.
22 – 22 S -> D. Increased accumulation to the double-strand break (DSB) sites.
Novel and recurrent mutations in lamin A/C in patients with Emery-Dreifuss muscular dystrophy.
Brown C.A.; Lanning R.W.; McKinney K.Q.; Salvino A.R.; Cherniske E.; Crowe C.A.; Darras B.T.; Gominak S.; Greenberg C.R.; Grosmann C.; Heydemann P.; Mendell J.R.; Pober B.R.; Sasaki T.; Shapiro F.; Simpson D.A.; Suchowersky O.; Spence J.E.;
Am. J. Med. Genet. 102:359-367(2001)
Cited for: VARIANTS EDMD2 PRO-25; THR-43; SER-50; PRO-133; 196-ARG--THR-199 DELINS SER; GLN-249; LYS-261 DEL; LYS-358; TRP-453; ILE-456; PRO-527 AND HIS-624;
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;
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.