Variant position: 190 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 AKLEAALGEAKKQLQDEMLR RVDAENRLQTMKEELDFQKNI
Mouse AKLEAALGEAKKQLQDEMLR RVDAENRLQTLKEELDFQKNI
Rat AKLEAALGEAKKQLQDEMLR RVDAENRLQTLKEELDFQKNI
Pig AKLEAALGEAKKQLQDEMLR RVDAENRLQTLKEELDFQKNI
Chicken AKLEGALSEAKKQLQDEMLR RVDAENRLQTLKEELEFQKNI
Xenopus laevis AKLEASLADTKKQLQDEMLR RVDTENRNQTLKEELEFQKSI
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.
In vivo and in vitro examination of the functional significances of novel lamin gene mutations in heart failure patients.
Sylvius N.; Bilinska Z.T.; Veinot J.P.; Fidzianska A.; Bolongo P.M.; Poon S.; McKeown P.; Davies R.A.; Chan K.-L.; Tang A.S.L.; Dyack S.; Grzybowski J.; Ruzyllo W.; McBride H.; Tesson F.;
J. Med. Genet. 42:639-647(2005)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A); SUBCELLULAR LOCATION (ISOFORM C); VARIANTS CMD1A TRP-190; GLY-192 AND SER-541; CHARACTERIZATION OF VARIANTS CMD1A GLY-192 AND SER-541;
Autosomal dominant dilated cardiomyopathy with atrioventricular block: a lamin A/C defect-related disease.
Arbustini E.; Pilotto A.; Repetto A.; Grasso M.; Negri A.; Diegoli M.; Campana C.; Scelsi L.; Baldini E.; Gavazzi A.; Tavazzi L.;
J. Am. Coll. Cardiol. 39:981-990(2002)
Cited for: VARIANTS CMD1A GLU-97; TRP-190 AND LYS-317;
Familial dilated cardiomyopathy and isolated left ventricular noncompaction associated with lamin A/C gene mutations.
Hermida-Prieto M.; Monserrat L.; Castro-Beiras A.; Laredo R.; Soler R.; Peteiro J.; Rodriguez E.; Bouzas B.; Alvarez N.; Muniz J.; Crespo-Leiro M.;
Am. J. Cardiol. 94:50-54(2004)
Cited for: VARIANTS CMD1A TRP-190 AND LEU-349;
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.