[1]
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SEQUENCE FROM NUCLEIC ACID (ISOFORMS A AND C).
MEDLINE=86118697; PubMed=3453101; [NCBI, ExPASy, EBI, Israel, Japan]
McKeon F.D.,
Kirschner M.W.,
Caput D.;
"Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins.";
Nature 319:463-468(1986).
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[2]
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SEQUENCE FROM NUCLEIC ACID (ISOFORMS A AND C), AND SEQUENCE OF 583-644.
MEDLINE=86313596; PubMed=3462705; [NCBI, ExPASy, EBI, Israel, Japan]
Fisher D.Z.,
Chaudhary N.,
Blobel G.;
"cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins.";
Proc. Natl. Acad. Sci. U.S.A. 83:6450-6454(1986).
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[3]
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SEQUENCE FROM NUCLEIC ACID (ISOFORM C).
TISSUE=Kidney, and Lung;
Strausberg R.;
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
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[4]
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SEQUENCE OF 375-664 FROM NUCLEIC ACID (ISOFORM ADELTA10).
TISSUE=Colon;
MEDLINE=96199170; PubMed=8621584; [NCBI, ExPASy, EBI, Israel, Japan]
Machiels B.M.,
Zorenc A.H.,
Endert J.M.,
Kuijpers H.J.,
van Eys G.J.,
Ramaekers F.C.,
Broers J.L.;
"An alternative splicing product of the lamin A/C gene lacks exon 10.";
J. Biol. Chem. 271:9249-9253(1996).
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[5]
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VARIANTS EDMD TRP-453; PRO-527 AND PRO-530.
MEDLINE=99178265; PubMed=10080180; [NCBI, ExPASy, EBI, Israel, Japan]
Bonne G.,
Di Barletta M.R.,
Varnous S.,
Becane H.-M.,
Hammouda E.-H.,
Merlini L.,
Muntoni F.,
Greenberg C.R.,
Gary F.,
Urtizberea J.-A.,
Duboc D.,
Fardeau M.,
Toniolo D.,
Schwartz K.;
"Mutations in the gene encoding lamin A/C cause autosomal dominant Emery-Dreifuss muscular dystrophy.";
Nat. Genet. 21:285-288(1999).
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[6]
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VARIANTS CMD1A GLY-60; ARG-85; LYS-195 AND GLY-203.
MEDLINE=20037766; PubMed=10580070; [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Missense mutations in the rod domain of the lamin A/C gene as causes of dilated cardiomyopathy and conduction-system disease.";
New Engl. J. Med. 341:1715-1724(1999).
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[7]
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VARIANT EDMD TYR-222.
MEDLINE=20206333; PubMed=10739764; [NCBI, ExPASy, EBI, Israel, Japan]
Raffaele di Barletta M.,
Ricci E.,
Galluzzi G.,
Tonali P.,
Mora M.,
Morandi L.,
Romorini A.,
Voit T.,
Orstavik K.H.,
Merlini L.,
Trevisan C.,
Biancalana V.,
Housmanowa-Petrusewicz I.,
Bione S.,
Ricotti R.,
Schwartz K.,
Bonne G.,
Toniolo D.;
"Different mutations in the LMNA gene cause autosomal dominant and autosomal recessive Emery-Dreifuss muscular dystrophy.";
Am. J. Hum. Genet. 66:1407-1412(2000).
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[8]
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VARIANT FPLD GLN-482.
MEDLINE=20056129; PubMed=10587585; [NCBI, ExPASy, EBI, Israel, Japan]
Cao H.,
Hegele R.A.;
"Nuclear lamin A/C R482Q mutation in Canadian kindreds with Dunnigan-type familial partial lipodystrophy.";
Hum. Mol. Genet. 9:109-112(2000).
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[9]
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VARIANTS FPLD LEU-482 AND TRP-482.
MEDLINE=20120714; PubMed=10655060; [NCBI, ExPASy, EBI, Israel, Japan]
Shackleton S.,
Lloyd D.J.,
Jackson S.N.J.,
Evans R.,
Niermeijer M.F.,
Singh B.M.,
Schmidt H.,
Brabant G.,
Kumar S.,
Durrington P.N.,
Gregory S.,
O'Rahilly S.,
Trembath R.C.;
"LMNA, encoding lamin A/C, is mutated in partial lipodystrophy.";
Nat. Genet. 24:153-156(2000).
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[10]
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VARIANTS FPLD ASP-465; GLN-482; TRP-482 AND HIS-582.
MEDLINE=20206314; PubMed=10739751; [NCBI, ExPASy, EBI, Israel, Japan]
Speckman R.A.,
Garg A.,
Du F.,
Bennett L.,
Veile R.,
Arioglu E.,
Taylor S.I.,
Lovett M.,
Bowcock A.M.;
"Mutational and haplotype analyses of families with familial partial lipodystrophy (Dunnigan variety) reveal recurrent missense mutations in the globular C-terminal domain of lamin A/C.";
Am. J. Hum. Genet. 66:1192-1198(2000).
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- FUNCTION: LAMINS ARE COMPONENTS OF THE NUCLEAR LAMINA, A FIBROUS LAYER ON THE NUCLEOPLASMIC SIDE OF THE INNER NUCLEAR MEMBRANE, WHICH IS THOUGHT TO PROVIDE A FRAMEWORK FOR THE NUCLEAR ENVELOPE AND MAY ALSO INTERACT WITH CHROMATIN. LAMIN A AND C ARE PRESENT IN EQUAL AMOUNTS IN THE LAMINA OF MAMMALS.
- SUBUNIT: HOMODIMER OF LAMIN A AND LAMIN C. INTERACTS WITH LAMIN-ASSOCIATED POLYPEPTIDES IA AND IB AND WITH EMERIN.
- SUBCELLULAR LOCATION: Nuclear.
- ALTERNATIVE PRODUCTS: 3 isoforms; Lamin A (shown here), Lamin C and ADelta10/Lamin ADelta10; are produced by alternative splicing.
- PTM: INCREASED PHOSPHORYLATION OF THE LAMINS OCCURS BEFORE ENVELOPE DISINTEGRATION AND PROBABLY PLAYS A ROLE IN REGULATING LAMIN ASSOCIATIONS.
- DISEASE: DEFECTS IN LMNA ARE A CAUSE OF EMERY-DREIFUSS MUSCULAR DYSTROPHY (EDMD), AN AUTOSOMAL RECESSIVE OR DOMINANT DISEASE CHARACTERIZED BY CARDIOMYOPATHY WITH CONDUCTION DEFECTS.
- DISEASE: DEFECTS IN LMNA ARE A CAUSE OF DILATED CARDIOMYOPATHY 1A (CMD1A).
- DISEASE: DEFECTS IN LMNA ARE A CAUSE OF FAMILIAL PARTIAL LIPODYSTROPHY (DUNNIGAN VARIETY) (FPLD), AN AUTOSOMAL DOMINANT DISORDER CHARACTERIZED BY MARKED LOSS OF SUBCUTANEOUS ADIPOSE TISSUE FROM THE EXTREMITIES AND TRUNK BUT BY EXCESS FAT DEPOSITION IN THE HEAD AND NECK. FREQUENTLY ASSOCIATED WITH PROFOUND INSULIN RESISTANCE, DYSLIPIDEMIA, AND DIABETES.
- MISCELLANEOUS: THERE ARE THREE TYPES OF LAMINS IN HUMAN CELLS: A, B, AND C.
- MISCELLANEOUS: THE STRUCTURAL INTEGRITY OF THE LAMINA IS STRICTLY CONTROLLED BY THE CELL CYCLE, AS SEEN BY THE DISINTEGRATION AND FORMATION OF THE NUCLEAR ENVELOPE IN PROPHASE AND TELOPHASE, RESPECTIVELY.
- SIMILARITY: BELONGS TO THE INTERMEDIATE FILAMENT FAMILY.
- CAUTION: Ref.1 (CAA27173) sequence differs from that shown due to a frameshift in position 582.
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