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Genetics Home Reference: your guide to understanding genetic conditions     A service of the U.S. National Library of Medicine®


Reviewed August 2013

What is the official name of the LMNA gene?

The official name of this gene is “lamin A/C.”

LMNA is the gene's official symbol. The LMNA gene is also known by other names, listed below.

What is the normal function of the LMNA gene?

The LMNA gene provides instructions for making several slightly different proteins called lamins. The two major proteins produced from this gene, lamin A and lamin C, are made in most of the body's cells. These proteins have a nearly identical sequence of protein building blocks (amino acids). The small difference in the sequence makes lamin A longer than lamin C.

Lamins A and C are structural proteins called intermediate filament proteins. Intermediate filaments provide stability and strength to cells. Lamins A and C are scaffolding (supporting) components of the nuclear envelope, which is a structure that surrounds the nucleus in cells. Specifically, these proteins are located in the nuclear lamina, a mesh-like layer of intermediate filaments and other proteins that is attached to the inner membrane of the nuclear envelope. The nuclear envelope regulates the movement of molecules into and out of the nucleus, and researchers believe it may play a role in regulating the activity (expression) of certain genes.

The lamin A protein must be processed within the cell before becoming part of the lamina. Its initial form, called prelamin A, undergoes a complex series of steps that are necessary for the protein to be inserted into the lamina. Lamin C does not have to undergo this processing before becoming part of the lamina.

Does the LMNA gene share characteristics with other genes?

The LMNA gene belongs to a family of genes called intermediate filaments type V, lamins (intermediate filaments type V, lamins).

A gene family is a group of genes that share important characteristics. Classifying individual genes into families helps researchers describe how genes are related to each other. For more information, see What are gene families? ( in the Handbook.

How are changes in the LMNA gene related to health conditions?

Charcot-Marie-Tooth disease - caused by mutations in the LMNA gene

At least one LMNA gene mutation has been identified in people with a form of Charcot-Marie-Tooth disease known as type 2B1. Charcot-Marie-Tooth disease is characterized by nerve damage, which can result in loss of sensation and wasting (atrophy) of muscles in the feet, legs, and hands. The mutation changes a single amino acid in the lamin A and lamin C proteins. Specifically, the amino acid arginine is replaced by the amino acid cysteine at protein position 298 (written as Arg298Cys or R298C). Although its effect is not fully understood, the Arg298Cys mutation alters a protein region important for interactions with other molecules. It is unclear how the altered proteins contribute to the signs and symptoms of type 2B1 Charcot-Marie-Tooth disease.

Emery-Dreifuss muscular dystrophy - caused by mutations in the LMNA gene

More than 100 mutations in the LMNA gene have been identified in people with Emery-Dreifuss muscular dystrophy, a condition characterized by weakness of the muscles used for movement (skeletal muscles) and the heart (cardiac) muscle. Most of these mutations change single amino acids in lamins A and C, which alters the structure of these proteins. The effect of LMNA mutations within cells remains unclear. Abnormal versions of lamins A and C may alter the activity of certain genes or weaken the structure of the nucleus, making cells more fragile. Researchers continue to investigate how LMNA mutations affect skeletal muscles and cardiac muscle, leading to the characteristic features of Emery-Dreifuss muscular dystrophy.

Hutchinson-Gilford progeria syndrome - caused by mutations in the LMNA gene

A specific mutation in the LMNA gene has been found in most patients with Hutchinson-Gilford progeria syndrome, which is a condition that causes the dramatic, rapid appearance of aging beginning in childhood. This mutation changes a single DNA building block (nucleotide) in the gene. Specifically, the mutation replaces the nucleotide cytosine with the nucleotide thymine at position 1824 (written as C1824T). This mutation is also sometimes noted as Gly608Gly or G608G, which refers to the position in the lamin A protein affected by the mutation. The C1824T mutation leads to an abnormal version of the lamin A protein called progerin, which is missing 50 amino acids near one end. The location of this mutation does not affect the production of lamin C. Other mutations in the LMNA gene have been identified in a small number of people with the features of Hutchinson-Gilford progeria syndrome.

The mutations responsible for this disorder result in an abnormal version of lamin A that cannot be processed correctly within the cell. When the altered protein is incorporated into the lamina, it can disrupt the shape of the nuclear envelope. Over time, a buildup of this altered protein appears to damage the structure and function of the nucleus, making cells more likely to die prematurely. Researchers are working to determine how these changes lead to the signs and symptoms of Hutchinson-Gilford progeria syndrome.

limb-girdle muscular dystrophy - caused by mutations in the LMNA gene

At least six mutations in the LMNA gene have been identified in people with limb-girdle muscular dystrophy type 1B. Limb-girdle muscular dystrophy is a group of related disorders characterized by muscle weakness and wasting, particularly in the shoulders, hips, and limbs.

LMNA gene mutations that cause limb-girdle muscular dystrophy may impair the function of lamin proteins. Impaired lamin protein function may lead to a fragile, easily-damaged cell nucleus or improperly regulated genes that affect a variety of cell activities. It is not known how the effects of LMNA gene mutations relate to the specific signs and symptoms of limb-girdle muscular dystrophy.

mandibuloacral dysplasia - caused by mutations in the LMNA gene

At least four mutations in the LMNA gene cause a form of mandibuloacral dysplasia called mandibuloacral dysplasia with type A lipodystrophy (MADA). This condition is characterized by a variety of signs and symptoms, which can include bone abnormalities; mottled or patchy skin coloring; and loss of fatty tissue under the skin, particularly affecting the limbs (type A lipodystrophy). The LMNA gene mutations that cause this condition change single protein building blocks (amino acids) in the lamin A and lamin C proteins. The most common mutation replaces the amino acid arginine at position 527 with the amino acid histidine (written as Arg527His or R527H).

The effects of LMNA gene mutations are not well understood. The amino acid changes may affect the structure of the lamin A or lamin C protein or both and alter how they interact with other proteins in the nuclear lamina. Some researchers speculate that these changes disrupt the nuclear envelope, making cells more fragile; however, it is unclear how the altered lamin proteins contribute to the signs and symptoms of MADA.

other disorders - caused by mutations in the LMNA gene

Mutations in the LMNA gene have been found to cause several other inherited conditions. Because the conditions result from mutations that affect lamin proteins, they are known as laminopathies. Familial dilated cardiomyopathy with conduction defects has severe effects on cardiac muscle that result in life-threatening heart problems. The features of this disorder, and also those of limb-girdle muscular dystrophy type 1B, overlap with those of the autosomal dominant form of Emery-Dreifuss muscular dystrophy. Because certain LMNA mutations may be responsible for any of these conditions, researchers suspect that limb-girdle muscular dystrophy type 1B and familial dilated cardiomyopathy with conduction defects may be variants of Emery-Dreifuss muscular dystrophy instead of separate disorders.

As in mandibuloacral dysplasia (described above), laminopathies can affect the amount and distribution of fat in the body. Dunnigan-type partial lipodystrophy is characterized by a loss of fatty tissue from the torso and limbs and a buildup of fat around the neck and shoulders.

Mutations in the LMNA gene also cause atypical progeroid syndrome (APS); the features of this condition are similar to those of Hutchinson-Gilford progeria syndrome and mandibuloacral dysplasia (described above). As in Hutchinson-Gilford progeria syndrome, children with APS look as though they are aging prematurely, although the signs and symptoms of APS usually begin slightly later in life. APS can also cause similar abnormalities in bone development and fat distribution as mandibuloacral dysplasia, although they are typically milder in APS.

Mutations in the LMNA gene have been identified in newborns with a disorder called lethal restrictive dermopathy. Infants with this disorder have tight, rigid skin; underdeveloped lungs; and other abnormalities. They do not usually survive past the first week of life.

Researchers have not determined how mutations in the LMNA gene result in this diverse group of disorders, but the multiple roles of the nuclear lamina in cells may help explain the wide variety of signs and symptoms.

Where is the LMNA gene located?

Cytogenetic Location: 1q22

Molecular Location on chromosome 1: base pairs 156,082,546 to 156,140,089

(Homo sapiens Annotation Release 107, GRCh38.p2) (NCBI (

The LMNA gene is located on the long (q) arm of chromosome 1 at position 22.

The LMNA gene is located on the long (q) arm of chromosome 1 at position 22.

More precisely, the LMNA gene is located from base pair 156,082,546 to base pair 156,140,089 on chromosome 1.

See How do geneticists indicate the location of a gene? ( in the Handbook.

Where can I find additional information about LMNA?

You and your healthcare professional may find the following resources about LMNA helpful.

You may also be interested in these resources, which are designed for genetics professionals and researchers.

What other names do people use for the LMNA gene or gene products?

  • HGPS
  • LMN1
  • LMNC

See How are genetic conditions and genes named? ( in the Handbook.

What glossary definitions help with understanding LMNA?

acids ; amino acid ; arginine ; atrophy ; atypical ; autosomal ; autosomal dominant ; cardiac ; cardiomyopathy ; cell ; cell nucleus ; cysteine ; cytosine ; dilated ; DNA ; dysplasia ; familial ; fatty tissue ; gene ; histidine ; inherited ; intermediate filaments ; lamin ; lipodystrophy ; muscular dystrophy ; mutation ; nuclear envelope ; nucleotide ; nucleus ; protein ; syndrome ; thymine ; tissue ; wasting

You may find definitions for these and many other terms in the Genetics Home Reference Glossary.


  • Bouhouche A, Birouk N, Azzedine H, Benomar A, Durosier G, Ente D, Muriel MP, Ruberg M, Slassi I, Yahyaoui M, Dubourg O, Ouazzani R, LeGuern E. Autosomal recessive axonal Charcot-Marie-Tooth disease (ARCMT2): phenotype-genotype correlations in 13 Moroccan families. Brain. 2007 Apr;130(Pt 4):1062-75. Epub 2007 Mar 8. (
  • Broers JL, Ramaekers FC, Bonne G, Yaou RB, Hutchison CJ. Nuclear lamins: laminopathies and their role in premature ageing. Physiol Rev. 2006 Jul;86(3):967-1008. Review. (
  • Brown CA, Lanning RW, McKinney KQ, Salvino AR, Cherniske E, Crowe CA, Darras BT, Gominak S, Greenberg CR, Grosmann C, Heydemann P, Mendell JR, Pober BR, Sasaki T, Shapiro F, Simpson DA, Suchowersky O, Spence JE. Novel and recurrent mutations in lamin A/C in patients with Emery-Dreifuss muscular dystrophy. Am J Med Genet. 2001 Sep 1;102(4):359-67. (
  • Cao K, Capell BC, Erdos MR, Djabali K, Collins FS. A lamin A protein isoform overexpressed in Hutchinson-Gilford progeria syndrome interferes with mitosis in progeria and normal cells. Proc Natl Acad Sci U S A. 2007 Mar 20;104(12):4949-54. Epub 2007 Mar 14. (
  • De Sandre-Giovannoli A, Bernard R, Cau P, Navarro C, Amiel J, Boccaccio I, Lyonnet S, Stewart CL, Munnich A, Le Merrer M, Lévy N. Lamin a truncation in Hutchinson-Gilford progeria. Science. 2003 Jun 27;300(5628):2055. Epub 2003 Apr 17. (
  • Doubaj Y, De Sandre-Giovannoli A, Vera EV, Navarro CL, Elalaoui SC, Tajir M, Lévy N, Sefiani A. An inherited LMNA gene mutation in atypical Progeria syndrome. Am J Med Genet A. 2012 Nov;158A(11):2881-7. doi: 10.1002/ajmg.a.35557. Epub 2012 Sep 18. (
  • Eriksson M, Brown WT, Gordon LB, Glynn MW, Singer J, Scott L, Erdos MR, Robbins CM, Moses TY, Berglund P, Dutra A, Pak E, Durkin S, Csoka AB, Boehnke M, Glover TW, Collins FS. Recurrent de novo point mutations in lamin A cause Hutchinson-Gilford progeria syndrome. Nature. 2003 May 15;423(6937):293-8. Epub 2003 Apr 25. (
  • Goldman RD, Shumaker DK, Erdos MR, Eriksson M, Goldman AE, Gordon LB, Gruenbaum Y, Khuon S, Mendez M, Varga R, Collins FS. Accumulation of mutant lamin A causes progressive changes in nuclear architecture in Hutchinson-Gilford progeria syndrome. Proc Natl Acad Sci U S A. 2004 Jun 15;101(24):8963-8. Epub 2004 Jun 7. (
  • Mounkes L, Kozlov S, Burke B, Stewart CL. The laminopathies: nuclear structure meets disease. Curr Opin Genet Dev. 2003 Jun;13(3):223-30. Review. (
  • Muchir A, Bonne G, van der Kooi AJ, van Meegen M, Baas F, Bolhuis PA, de Visser M, Schwartz K. Identification of mutations in the gene encoding lamins A/C in autosomal dominant limb girdle muscular dystrophy with atrioventricular conduction disturbances (LGMD1B). Hum Mol Genet. 2000 May 22;9(9):1453-9. (
  • Muchir A, Worman HJ. The nuclear envelope and human disease. Physiology (Bethesda). 2004 Oct;19:309-14. Review. (
  • Navarro CL, De Sandre-Giovannoli A, Bernard R, Boccaccio I, Boyer A, Geneviève D, Hadj-Rabia S, Gaudy-Marqueste C, Smitt HS, Vabres P, Faivre L, Verloes A, Van Essen T, Flori E, Hennekam R, Beemer FA, Laurent N, Le Merrer M, Cau P, Lévy N. Lamin A and ZMPSTE24 (FACE-1) defects cause nuclear disorganization and identify restrictive dermopathy as a lethal neonatal laminopathy. Hum Mol Genet. 2004 Oct 15;13(20):2493-503. Epub 2004 Aug 18. (
  • NCBI Gene (
  • Niemann A, Berger P, Suter U. Pathomechanisms of mutant proteins in Charcot-Marie-Tooth disease. Neuromolecular Med. 2006;8(1-2):217-42. Review. (
  • Novelli G, Muchir A, Sangiuolo F, Helbling-Leclerc A, D'Apice MR, Massart C, Capon F, Sbraccia P, Federici M, Lauro R, Tudisco C, Pallotta R, Scarano G, Dallapiccola B, Merlini L, Bonne G. Mandibuloacral dysplasia is caused by a mutation in LMNA-encoding lamin A/C. Am J Hum Genet. 2002 Aug;71(2):426-31. Epub 2002 Jun 19. (
  • Rankin J, Ellard S. The laminopathies: a clinical review. Clin Genet. 2006 Oct;70(4):261-74. Review. Erratum in: Clin Genet. 2007 Mar;71(3):293. (


The resources on this site should not be used as a substitute for professional medical care or advice. Users seeking information about a personal genetic disease, syndrome, or condition should consult with a qualified healthcare professional. See How can I find a genetics professional in my area? ( in the Handbook.

Reviewed: August 2013
Published: February 8, 2016