Variant position: 203 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 LQDEMLRRVDAENRLQTMKE ELDFQKNIYSEELRETKRRHE
Mouse LQDEMLRRVDAENRLQTLKE ELDFQKNIYSEELRETKRRHE
Rat LQDEMLRRVDAENRLQTLKE ELDFQKNIYSEELRETKRRHE
Pig LQDEMLRRVDAENRLQTLKE ELDFQKNIYSEELRETKRRHE
Chicken LQDEMLRRVDAENRLQTLKE ELEFQKNIYSEELRETKRRHE
Xenopus laevis LQDEMLRRVDTENRNQTLKE ELEFQKSIYNEEMRETKRRHE
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
201 – 201 N6-acetyllysine; alternate
212 – 212 Phosphoserine
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)
219 – 219 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.
65 – 218
Sumoylation regulates lamin A function and is lost in lamin A mutants associated with familial cardiomyopathies.
Zhang Y.Q.; Sarge K.D.;
J. Cell Biol. 182:35-39(2008)
Cited for: SUBCELLULAR LOCATION; SUMOYLATION AT LYS-201; MUTAGENESIS OF LYS-201; CHARACTERIZATION OF VARIANTS CMD1A GLY-203 AND LYS-203;
Missense mutations in the rod domain of the lamin A/C gene as causes of dilated cardiomyopathy and conduction-system disease.
Fatkin D.; MacRae C.; Sasaki T.; Wolff M.R.; Porcu M.; Frenneaux M.; Atherton J.; Vidaillet H.J. Jr.; Spudich S.; De Girolami U.; Seidman J.G.; Seidman C.E.;
N. Engl. J. Med. 341:1715-1724(1999)
Cited for: VARIANTS CMD1A GLY-60; ARG-85; LYS-195 AND GLY-203; FUNCTION;
Properties of lamin A mutants found in Emery-Dreifuss muscular dystrophy, cardiomyopathy and Dunnigan-type partial lipodystrophy.
Oestlund C.; Bonne G.; Schwartz K.; Worman H.J.;
J. Cell Sci. 114:4435-4445(2001)
Cited for: CHARACTERIZATION OF VARIANTS CMD1A GLY-60; ARG-85; LYS-195 AND GLY-203; CHARACTERIZATION OF VARIANTS EDMD2 LYS-358; LYS-371; LYS-386; TRP-453; SER-520; PRO-527; LYS-528 AND PRO-530; CHARACTERIZATION OF VARIANTS FPLD2 GLN-482; TRP-482 AND ASN-486;
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.