Variant position: 189 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 VAKLEAALGEAKKQLQDEML RRVDAENRLQTMKEELDFQKN
Mouse VAKLEAALGEAKKQLQDEML RRVDAENRLQTLKEELDFQKN
Rat VAKLEAALGEAKKQLQDEML RRVDAENRLQTLKEELDFQKN
Pig VAKLEAALGEAKKQLQDEML RRVDAENRLQTLKEELDFQKN
Chicken VAKLEGALSEAKKQLQDEML RRVDAENRLQTLKEELEFQKN
Xenopus laevis IAKLEASLADTKKQLQDEML RRVDTENRNQTLKEELEFQKS
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
31 – 387 IF rod
81 – 218 Coil 1B
171 – 171 N6-acetyllysine; alternate
171 – 171 N6-succinyllysine; alternate
201 – 201 N6-acetyllysine; alternate
171 – 171 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
201 – 201 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
201 – 201 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
208 – 208 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
201 – 201 K -> L. Decreased sumoylation; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; associated with increased cell death.
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.