Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P02545 (LMNA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 197. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prelamin-A/C

Cleaved into the following chain:

  1. Lamin-A/C
    Alternative name(s):
    70 kDa lamin
    Renal carcinoma antigen NY-REN-32
Gene names
Name:LMNA
Synonyms:LMN1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length664 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Plays an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics. Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation. Required for osteoblastogenesis and bone formation. Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone. Ref.28 Ref.30

Prelamin-A/C can accelerate smooth muscle cell senescence. It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence. Ref.28 Ref.30

Subunit structure

Homodimer of lamin A and lamin C. Interacts with lamin-associated polypeptides IA, IB and TMPO-alpha, RB1 and with emerin. Interacts with SREBF1, SREBF2, SUN2 and TMEM43 By similarity. Proteolytically processed isoform A interacts with NARF. Interacts with SUN1. Prelamin-A/C interacts with EMD. Interacts with MLIP; may regulate MLIP localization to the nucleus envelope. Interacts with DMPK; may regulate nuclear envelope stability. Interacts with SUV39H1; the interaction increases stability of SUV39H1. Ref.14 Ref.15 Ref.25 Ref.31 Ref.34 Ref.38 Ref.39

Subcellular location

Nucleus. Nucleus envelope. Nucleus lamina. Nucleusnucleoplasm. Note: Farnesylation of prelamin-A/C facilitates nuclear envelope targeting and subsequent cleaveage by ZMPSTE24/FACE1 to remove the farnesyl group produces mature lamin-A/C, which can then be inserted into the nuclear lamina. EMD is required for proper localization of non-farnesylated prelamin-A/C. Ref.3 Ref.20 Ref.25 Ref.26 Ref.29 Ref.37 Ref.38

Isoform C: Nucleus speckle Ref.3 Ref.20 Ref.25 Ref.26 Ref.29 Ref.37 Ref.38.

Tissue specificity

In the arteries, prelamin-A/C accumulation is not observed in young healthy vessels but is prevalent in medial vascular smooth muscle cells (VSMCs) from aged individuals and in atherosclerotic lesions, where it often colocalizes with senescent and degenerate VSMCs. Prelamin-A/C expression increases with age and disease. In normal aging, the accumulation of prelamin-A/C is caused in part by the down-regulation of ZMPSTE24/FACE1 in response to oxidative stress. Ref.30

Post-translational modification

Increased phosphorylation of the lamins occurs before envelope disintegration and probably plays a role in regulating lamin associations.

Proteolytic cleavage of the C-terminal of 18 residues of prelamin-A/C results in the production of lamin-A/C. The prelamin-A/C maturation pathway includes farnesylation of CAAX motif, ZMPSTE24/FACE1 mediated cleavage of the last three amino acids, methylation of the C-terminal cysteine and endoproteolytic removal of the last 15 C-terminal amino acids. Proteolytic cleavage requires prior farnesylation and methylation, and absence of these blocks cleavage.

Sumoylation is necessary for the localization to the nuclear envelope. Ref.20

Farnesylation of prelamin-A/C facilitates nuclear envelope targeting.

Involvement in disease

Emery-Dreifuss muscular dystrophy 2, autosomal dominant (EDMD2) [MIM:181350]: A form of Emery-Dreifuss muscular dystrophy, a degenerative myopathy characterized by weakness and atrophy of muscle without involvement of the nervous system, early contractures of the elbows, Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.31 Ref.37 Ref.43 Ref.47 Ref.48 Ref.52 Ref.53 Ref.55 Ref.63 Ref.72 Ref.74 Ref.80 Ref.84 Ref.94

Emery-Dreifuss muscular dystrophy 3, autosomal recessive (EDMD3) [MIM:181350]: A form of Emery-Dreifuss muscular dystrophy, a degenerative myopathy characterized by weakness and atrophy of muscle without involvement of the nervous system, early contractures of the elbows, Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.37 Ref.95

Cardiomyopathy, dilated 1A (CMD1A) [MIM:115200]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.20 Ref.29 Ref.37 Ref.44 Ref.54 Ref.55 Ref.57 Ref.62 Ref.67 Ref.71 Ref.72 Ref.75 Ref.76 Ref.92

Lipodystrophy, familial partial, 2 (FPLD2) [MIM:151660]: A disorder characterized by the loss of subcutaneous adipose tissue in the lower parts of the body (limbs, buttocks, trunk). It is accompanied by an accumulation of adipose tissue in the face and neck causing a double chin, fat neck, or cushingoid appearance. Adipose tissue may also accumulate in the axillae, back, labia majora, and intraabdominal region. Affected patients are insulin-resistant and may develop glucose intolerance and diabetes mellitus after age 20 years, hypertriglyceridemia, and low levels of high density lipoprotein cholesterol.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.26 Ref.37 Ref.45 Ref.49 Ref.51 Ref.55 Ref.61 Ref.64 Ref.69 Ref.87

Limb-girdle muscular dystrophy 1B (LGMD1B) [MIM:159001]: An autosomal dominant degenerative myopathy with age-related atrioventricular cardiac conduction disturbances, dilated cardiomyopathy, and the absence of early contractures. Characterized by slowly progressive skeletal muscle weakness of the hip and shoulder girdles. Muscle biopsy shows mild dystrophic changes.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.37 Ref.50 Ref.56 Ref.63 Ref.66 Ref.84 Ref.88

Charcot-Marie-Tooth disease 2B1 (CMT2B1) [MIM:605588]: A recessive axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.37 Ref.58

Hutchinson-Gilford progeria syndrome (HGPS) [MIM:176670]: Rare genetic disorder characterized by features reminiscent of marked premature aging.
Note: The disease is caused by mutations affecting the gene represented in this entry. HGPS is caused by the toxic accumulation of a truncated form of lamin-A/C. This mutant protein, called progerin (isoform 6) acts to deregulate mitosis and DNA damage signaling, leading to premature cell death and senescence. The mutant form is mainly generated by a silent or missense mutation at codon 608 of prelamin A that causes activation of a cryptic splice donor site, resulting in production of isoform 6 with a deletion of 50 amino acids near the C terminus. Progerin lacks the conserved ZMPSTE24/FACE1 cleavage site and therefore remains permanently farnesylated. Thus, although it can enter the nucleus and associate with the nuclear envelope, it cannot incorporate normally into the nuclear lamina (Ref.16). Ref.16 Ref.31 Ref.36 Ref.37 Ref.70 Ref.73 Ref.79 Ref.81 Ref.93

Cardiomyopathy, dilated, with hypergonadotropic hypogonadism (CMDHH) [MIM:212112]: A disorder characterized by the association of genital anomalies, hypergonadotropic hypogonadism and dilated cardiomyopathy. Patients can present other variable clinical manifestations including mental retardation, skeletal anomalies, scleroderma-like skin, graying and thinning of hair, osteoporosis. Dilated cardiomyopathy is characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.37 Ref.73 Ref.86 Ref.91

Mandibuloacral dysplasia with type A lipodystrophy (MADA) [MIM:248370]: A disorder characterized by mandibular and clavicular hypoplasia, acroosteolysis, delayed closure of the cranial suture, progeroid appearance, partial alopecia, soft tissue calcinosis, joint contractures, and partial lipodystrophy with loss of subcutaneous fat from the extremities. Adipose tissue in the face, neck and trunk is normal or increased.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.37 Ref.60 Ref.83 Ref.85

Lethal tight skin contracture syndrome (LTSCS) [MIM:275210]: Rare disorder mainly characterized by intrauterine growth retardation, tight and rigid skin with erosions, prominent superficial vasculature and epidermal hyperkeratosis, facial features (small mouth, small pinched nose and micrognathia), sparse/absent eyelashes and eyebrows, mineralization defects of the skull, thin dysplastic clavicles, pulmonary hypoplasia, multiple joint contractures and an early neonatal lethal course. Liveborn children usually die within the first week of life. The overall prevalence of consanguineous cases suggested an autosomal recessive inheritance.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.37 Ref.77

Heart-hand syndrome Slovenian type (HHS-Slovenian) [MIM:610140]: Heart-hand syndrome (HHS) is a clinically and genetically heterogeneous disorder characterized by the co-occurrence of a congenital cardiac disease and limb malformations.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.37

Muscular dystrophy congenital LMNA-related (MDCL) [MIM:613205]: A form of congenital muscular dystrophy. Patients present at birth, or within the first few months of life, with hypotonia, muscle weakness and often with joint contractures.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.37 Ref.89

Defects in LMNA may cause a late-onset cardiocutaneous progeria syndrome characterized by cutaneous manifestations of aging appearing in the third decade of life, cardiac valve calcification and dysfunction, prominent atherosclerosis, and cardiomyopathy, leading to death on average in the fourth decade. Ref.37

Miscellaneous

There are three types of lamins in human cells: A, B, and C.

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.

Sequence similarities

Belongs to the intermediate filament family.

Sequence caution

The sequence CAA27173.1 differs from that shown. Reason: Frameshift at position 582.

Ontologies

Keywords
   Cellular componentIntermediate filament
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseCardiomyopathy
Charcot-Marie-Tooth disease
Congenital muscular dystrophy
Disease mutation
Emery-Dreifuss muscular dystrophy
Limb-girdle muscular dystrophy
Neurodegeneration
Neuropathy
   DomainCoiled coil
   PTMAcetylation
Isopeptide bond
Lipoprotein
Methylation
Phosphoprotein
Prenylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of signaling protein activity involved in unfolded protein response

Traceable author statement. Source: Reactome

apoptotic process

Traceable author statement. Source: Reactome

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

cellular response to hypoxia

Inferred from expression pattern PubMed 20810912. Source: UniProtKB

endoplasmic reticulum unfolded protein response

Traceable author statement. Source: Reactome

establishment or maintenance of microtubule cytoskeleton polarity

Inferred from sequence or structural similarity. Source: BHF-UCL

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic nuclear envelope disassembly

Traceable author statement. Source: Reactome

mitotic nuclear envelope reassembly

Traceable author statement. Source: Reactome

muscle organ development

Inferred from mutant phenotype Ref.43. Source: UniProtKB

negative regulation of extrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of release of cytochrome c from mitochondria

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell aging

Inferred from direct assay Ref.30. Source: UniProtKB

protein localization to nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell migration

Inferred from sequence or structural similarity. Source: BHF-UCL

sterol regulatory element binding protein import into nucleus

Inferred from electronic annotation. Source: Ensembl

ventricular cardiac muscle cell development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

intermediate filament

Traceable author statement PubMed 8344919PubMed 8344919. Source: UniProtKB

lamin filament

Inferred from electronic annotation. Source: Ensembl

nuclear envelope

Inferred from direct assay Ref.20. Source: UniProtKB

nuclear lamina

Traceable author statement PubMed 8344919PubMed 8344919. Source: UniProtKB

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 20810912. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay Ref.43. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 20580717. Source: IntAct

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ALOX12P180544EBI-351935,EBI-1633210
HIST2H3AQ71DI36EBI-351935,EBI-750650
PASKQ96RG22EBI-351935,EBI-1042651
UL31P102152EBI-351935,EBI-7183650From a different organism.
UL34P102182EBI-351935,EBI-7183680From a different organism.
YWHAZP631042EBI-351935,EBI-347088

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: P02545-1)

Also known as: Lamin A;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform C (identifier: P02545-2)

Also known as: Lamin C;

The sequence of this isoform differs from the canonical sequence as follows:
     567-572: GSHCSS → VSGSRR
     573-664: Missing.
Isoform ADelta10 (identifier: P02545-3)

Also known as: Lamin ADelta10;

The sequence of this isoform differs from the canonical sequence as follows:
     537-566: Missing.
Isoform 4 (identifier: P02545-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: METPSQR → MGNSEGC
     8-119: Missing.
     664-664: M → IQEMGMRWEVEEGRRKVSLSCLP
Note: No experimental confirmation available.
Isoform 5 (identifier: P02545-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-99: Missing.
     100-119: ARLQLELSKVREEFKELKAR → MDLEAWDPHLEPDAEAMVDG
Note: No experimental confirmation available.
Isoform 6 (identifier: P02545-6)

Also known as: Progerin;

The sequence of this isoform differs from the canonical sequence as follows:
     607-656: Missing.
Note: Disease-associated isoform. Polymorphism at codon 608 results in activation of a cryptic splice donor site within exon 11, resulting in a truncated protein product that lacks the site for endoproteolytic cleavage.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 661661Prelamin-A/C
PRO_0000398835
Chain1 – 646646Lamin-A/C
PRO_0000063810
Propeptide647 – 66115Removed in Lamin-A/C form
PRO_0000398836
Propeptide662 – 6643Removed in Prelamin-A/C form and in Lamin-A/C form
PRO_0000403442

Regions

Region1 – 130130Interaction with MLIP
Region1 – 3333Head
Region34 – 383350Rod
Region34 – 7037Coil 1A
Region71 – 8010Linker 1
Region81 – 218138Coil 1B
Region219 – 24224Linker 2
Region243 – 383141Coil 2
Region384 – 664281Tail
Motif417 – 4226Nuclear localization signal Potential

Sites

Site2661Heptad change of phase
Site3251Stutter By similarity
Site3301Heptad change of phase
Site646 – 6472Cleavage; by endoprotease

Amino acid modifications

Modified residue11N-acetylmethionine Ref.32
Modified residue31Phosphothreonine Ref.32
Modified residue121Phosphoserine Ref.23 Ref.32
Modified residue181Phosphoserine Ref.23
Modified residue191Phosphothreonine Ref.18 Ref.23 Ref.32
Modified residue221Phosphoserine Ref.9 Ref.18 Ref.23 Ref.32
Modified residue321N6-acetyllysine; alternate By similarity
Modified residue321N6-succinyllysine; alternate By similarity
Modified residue1081N6-acetyllysine Ref.27
Modified residue1231N6-acetyllysine By similarity
Modified residue1351N6-acetyllysine By similarity
Modified residue1551N6-acetyllysine By similarity
Modified residue1711N6-acetyllysine; alternate By similarity
Modified residue1711N6-succinyllysine; alternate By similarity
Modified residue2011N6-acetyllysine; alternate By similarity
Modified residue2121Phosphoserine Ref.32
Modified residue2601N6-acetyllysine By similarity
Modified residue2701N6-acetyllysine Ref.27
Modified residue2771Phosphoserine Ref.17 Ref.32
Modified residue3011Phosphoserine Ref.23 Ref.32
Modified residue3111N6-acetyllysine Ref.27
Modified residue3901Phosphoserine Ref.18 Ref.23 Ref.32 Ref.35
Modified residue3921Phosphoserine Ref.18 Ref.23 Ref.32 Ref.35
Modified residue3951Phosphoserine Ref.18 Ref.23 Ref.32
Modified residue4041Phosphoserine Ref.32 Ref.35
Modified residue4071Phosphoserine By similarity
Modified residue4141Phosphoserine Ref.32 Ref.35
Modified residue4311Phosphoserine Ref.32
Modified residue4501N6-acetyllysine Ref.27
Modified residue4571N6-acetyllysine By similarity
Modified residue4581Phosphoserine Ref.23 Ref.32 Ref.35
Modified residue4631Phosphoserine Ref.32
Modified residue4961Phosphothreonine By similarity
Modified residue5051Phosphothreonine Ref.32
Modified residue5101Phosphothreonine By similarity
Modified residue5461Phosphoserine By similarity
Modified residue6281Phosphoserine Ref.18 Ref.19 Ref.21 Ref.23 Ref.32
Modified residue6321Phosphoserine Ref.18 Ref.22 Ref.23 Ref.32
Modified residue6361Phosphoserine Ref.18 Ref.23 Ref.32 Ref.35
Modified residue6521Phosphoserine Ref.23 Ref.32
Modified residue6611Cysteine methyl ester Ref.11 Ref.12
Lipidation6611S-farnesyl cysteine Ref.11 Ref.12
Cross-link201Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Ref.20

Natural variations

Alternative sequence1 – 9999Missing in isoform 5.
VSP_053503
Alternative sequence1 – 77METPSQR → MGNSEGC in isoform 4.
VSP_045977
Alternative sequence8 – 119112Missing in isoform 4.
VSP_045978
Alternative sequence100 – 11920ARLQL…ELKAR → MDLEAWDPHLEPDAEAMVDG in isoform 5.
VSP_053504
Alternative sequence537 – 56630Missing in isoform ADelta10.
VSP_002468
Alternative sequence567 – 5726GSHCSS → VSGSRR in isoform C.
VSP_002469
Alternative sequence573 – 66492Missing in isoform C.
VSP_002470
Alternative sequence607 – 65650Missing in isoform 6.
VSP_053505
Alternative sequence6641M → IQEMGMRWEVEEGRRKVSLS CLP in isoform 4.
VSP_045979
Natural variant101T → I in an atypical progeroid patient; diagnosed as Seip syndrome. Ref.78
Corresponds to variant rs57077886 [ dbSNP | Ensembl ].
VAR_039745
Natural variant251R → G in EDMD2. Ref.72
Corresponds to variant rs58327533 [ dbSNP | Ensembl ].
VAR_039746
Natural variant251R → P in EDMD2; mis-localized in the nucleus; causes nuclear deformations and LMNB1 redistribution. Ref.53 Ref.94
Corresponds to variant rs61578124 [ dbSNP | Ensembl ].
VAR_039747
Natural variant281R → W in FPLD2. Ref.61
Corresponds to variant rs59914820 [ dbSNP | Ensembl ].
VAR_039748
Natural variant321Missing in EDMD2. Ref.72
VAR_039749
Natural variant331E → D in CMT2; autosomal dominant form. Ref.80
Corresponds to variant rs57966821 [ dbSNP | Ensembl ].
VAR_039750
Natural variant331E → G in EDMD2. Ref.80
VAR_039751
Natural variant351L → V in EDMD2. Ref.72
Corresponds to variant rs56694480 [ dbSNP | Ensembl ].
VAR_039752
Natural variant391N → S in MDCL and EDMD2. Ref.89 Ref.94
VAR_063588
Natural variant431A → T in EDMD2. Ref.53
Corresponds to variant rs60446065 [ dbSNP | Ensembl ].
VAR_039753
Natural variant451Y → C in EDMD2. Ref.48 Ref.94
Corresponds to variant rs58436778 [ dbSNP | Ensembl ].
VAR_009971
Natural variant501R → P in EDMD2 and MDCL. Ref.48 Ref.89
Corresponds to variant rs60695352 [ dbSNP | Ensembl ].
VAR_009972
Natural variant501R → S in EDMD2. Ref.53
Corresponds to variant rs59931416 [ dbSNP | Ensembl ].
VAR_039754
Natural variant571A → P in CMDHH; phenotype originally designated as atypical Werner syndrome. Ref.73
Corresponds to variant rs28928903 [ dbSNP | Ensembl ].
VAR_017656
Natural variant591L → R in CMDHH. Ref.86 Ref.91
VAR_064055
Natural variant601R → G in CMD1A and FPLD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. Ref.44 Ref.55 Ref.64
Corresponds to variant rs28928900 [ dbSNP | Ensembl ].
VAR_034706
Natural variant621R → G in FPLD2. Ref.61
Corresponds to variant rs56793579 [ dbSNP | Ensembl ].
VAR_039755
Natural variant631I → N in EDMD2. Ref.74 Ref.84
VAR_039756
Natural variant631I → S in EDMD2. Ref.48
Corresponds to variant rs57793737 [ dbSNP | Ensembl ].
VAR_009974
Natural variant651E → G in EDMD2. Ref.72
VAR_039757
Natural variant851L → R in CMD1A; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. Ref.44 Ref.55
Corresponds to variant rs28933090 [ dbSNP | Ensembl ].
VAR_009975
Natural variant891R → L in CMD1A; dramatically aberrant localization with almost no nuclear rim staining and formation of intranuclear foci. Ref.29 Ref.67
Corresponds to variant rs59040894 [ dbSNP | Ensembl ].
VAR_039758
Natural variant921L → F in CMD1A. Ref.92
VAR_067257
Natural variant971K → E in CMD1A. Ref.62
Corresponds to variant rs59065411 [ dbSNP | Ensembl ].
VAR_039759
Natural variant1011R → P in CMD1A; dramatically aberrant localization with almost no nuclear rim staining and formation of intranuclear foci. Ref.29
VAR_070174
Natural variant1121Missing in EDMD2. Ref.48 Ref.72
VAR_009976
Natural variant1331R → L in FPLD2. Ref.69
VAR_016913
Natural variant1331R → P in EDMD2. Ref.53
Corresponds to variant rs60864230 [ dbSNP | Ensembl ].
VAR_017657
Natural variant1381E → K in HGPS; might be associated with early and severe strokes. Ref.93
VAR_070175
Natural variant1401L → P in EDMD2. Ref.74 Ref.84
VAR_039760
Natural variant1401L → R in HGPS; phenotype originally designated as atypical Werner syndrome. Ref.73
Corresponds to variant rs60652225 [ dbSNP | Ensembl ].
VAR_017658
Natural variant1431S → F in HGPS. Ref.81
Corresponds to variant rs58912633 [ dbSNP | Ensembl ].
VAR_034707
Natural variant1431S → P in CMD1A. Ref.76
Corresponds to variant rs61661343 [ dbSNP | Ensembl ].
VAR_039761
Natural variant1451E → K in HGPS; atypical. Ref.16
Corresponds to variant rs60310264 [ dbSNP | Ensembl ].
VAR_017659
Natural variant1501T → P in EDMD2. Ref.52 Ref.94
Corresponds to variant rs58917027 [ dbSNP | Ensembl ].
VAR_039762
Natural variant1611E → K in CMD1A. Ref.71 Ref.92
Corresponds to variant rs28933093 [ dbSNP | Ensembl ].
VAR_017660
Natural variant1661R → P in CMD1A; dramatically aberrant localization with almost no nuclear rim staining and formation of intranuclear foci. Ref.29
VAR_070176
Natural variant1891R → P in EDMD2; found also in a patient with limb-girdle muscular dystrophy; sporadic. Ref.94
VAR_064962
Natural variant1901R → Q in EDMD2 and CMD1A; aberrant localization with decreased nuclear rim staining and increased formation of intranuclear foci. Ref.29 Ref.84
VAR_039763
Natural variant1901R → RR in EDMD2. Ref.94
VAR_064963
Natural variant1901R → W in CMD1A. Ref.3 Ref.62 Ref.75
Corresponds to variant rs59026483 [ dbSNP | Ensembl ].
VAR_039764
Natural variant1921D → G in CMD1A; dramatically increases the size of intranuclear speckles and reduces their number; this phenotype is only partially reversed by coexpression of the G-192 mutation and wild-type lamin-C; precludes insertion of lamin-C into the nuclear envelope when co-transfected with the G-192 LMNA; G-192 lamin-C expression totally disrupts the SUMO1 pattern. Ref.3
Corresponds to variant rs57045855 [ dbSNP | Ensembl ].
VAR_039765
Natural variant1951N → K in CMD1A; dramatically aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; distribution of endogenous LMNA, LMNB1 and LMNB2 are altered in cells expressing this mutant; causes an increased loss of endogenous EMD from the nuclear envelope; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. Ref.44 Ref.55
Corresponds to variant rs28933091 [ dbSNP | Ensembl ].
VAR_009977
Natural variant196 – 1994RLQT → S in EDMD2.
VAR_039766
Natural variant2031E → G in CMD1A; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type; decreased sumoylation; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; associated with increased cell death. Ref.20 Ref.44 Ref.55
Corresponds to variant rs28933092 [ dbSNP | Ensembl ].
VAR_009978
Natural variant2031E → K in CMD1A; decreased sumoylation; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; associated with increased cell death. Ref.20 Ref.29 Ref.54
Corresponds to variant rs61195471 [ dbSNP | Ensembl ].
VAR_039767
Natural variant2061F → L in EDMD2. Ref.94
VAR_064964
Natural variant2081Missing in LGMD1B. Ref.50
VAR_034708
Natural variant2101I → S in CMD1A; dramatically aberrant localization with almost no nuclear rim staining and increased formation of intranuclear foci. Ref.29
VAR_070177
Natural variant2151L → P in CMD1A; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci. Ref.29 Ref.57
VAR_039768
Natural variant2221H → P in EDMD2. Ref.48
VAR_039769
Natural variant2221H → Y in EDMD2. Ref.47
Corresponds to variant rs28928901 [ dbSNP | Ensembl ].
VAR_009979
Natural variant2251R → Q in EDMD3. Ref.95
VAR_067697
Natural variant2301D → N in FPLD2. Ref.87
VAR_039770
Natural variant2321G → E in EDMD2. Ref.48
VAR_039771
Natural variant2481L → P in EDMD2. Ref.72
VAR_039772
Natural variant2491R → Q in EDMD2. Ref.47 Ref.48 Ref.53 Ref.63 Ref.72 Ref.74 Ref.84 Ref.94
VAR_009980
Natural variant2491R → W in MDCL and EDMD2; mislocalized in the nucleus; causes nuclear deformations and LMNB1 redistribution. Ref.89 Ref.94
VAR_063589
Natural variant2601K → N in CMDA1. Ref.82
VAR_039773
Natural variant2611Missing in EDMD2. Ref.48 Ref.52 Ref.53
VAR_009981
Natural variant2671Y → C in EDMD2. Ref.72
VAR_039774
Natural variant2681S → P in EDMD2. Ref.94
VAR_064965
Natural variant2711L → P in EDMD2. Ref.94
VAR_064966
Natural variant2941Q → P in EDMD2. Ref.48 Ref.94
VAR_009982
Natural variant2951S → P in EDMD2. Ref.94
VAR_064967
Natural variant2981R → C in CMT2B1. Ref.58
VAR_017661
Natural variant3001D → G Probable disease-associated mutation found in a patient with late-onset cardiocutaneous progeria syndrome; abnormal nuclear morphology with single or multple blebs, lobulation and occasional ringed or donut shaped nuclei. Ref.37
VAR_070178
Natural variant3021L → P in MDCL. Ref.89
VAR_063590
Natural variant3031S → P in EDMD2. Ref.94
VAR_064968
Natural variant3171E → K in CMD1A. Ref.62 Ref.92
VAR_039775
Natural variant3181A → T in CMD1A; no effect on nuclear morphology and lamin A localization. Ref.29
VAR_070179
Natural variant3361R → Q in EDMD2. Ref.47
VAR_009983
Natural variant3431R → Q in EDMD2.
VAR_009984
Natural variant3491R → L in CMD1A. Ref.75
VAR_039776
Natural variant3551Missing in EDMD2. Ref.94
VAR_064969
Natural variant3581E → K in EDMD2 and MDCL; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; distribution of endogenous LMNA, LMNB1 and LMNB2 are altered in cells expressing this mutant; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. Ref.48 Ref.53 Ref.55 Ref.89 Ref.94
VAR_009985
Natural variant3611E → K in EDMD2. Ref.94
VAR_064970
Natural variant3711M → K in EDMD2; dramatically aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; distribution of endogenous LMNA, LMNB1 and LMNB2 are altered in cells expressing this mutant; causes an increased loss of endogenous EMD from the nuclear envelope; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. Ref.48 Ref.55
VAR_009986
Natural variant3771R → H in LGMD1B. Ref.50 Ref.66 Ref.67 Ref.84 Ref.88
VAR_016205
Natural variant3771R → L in EDMD2 and LGMD1B. Ref.63 Ref.74
VAR_039777
Natural variant3801L → S in MDCL. Ref.89
VAR_063591
Natural variant3861R → K in EDMD2; dramatically aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; distribution of endogenous LMNA, LMNB1 and LMNB2 are altered in cells expressing this mutant; causes an increased loss of endogenous EMD from the nuclear envelope; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. Ref.48 Ref.55 Ref.74 Ref.94
VAR_009987
Natural variant3881R → H in CMD1A; no effect on nuclear morphology but restricts lamin A to the cytoplasm. Ref.29
VAR_070180
Natural variant3991R → C in FPLD2 and CMD1A; no effect on nuclear morphology and lamin A localization. Ref.29 Ref.87
VAR_039778
Natural variant4351R → C in CMD1A. Ref.72
VAR_039779
Natural variant4391R → C in FPLD2; increase in nuclear blebbing and formation of honeycomb-like structures in the nuclei with no accumulation of prelamin A in skin fibroblasts; causes oligomerization of the C-terminal globular domain of lamins A and C under no-reducing conditions and increases binding affinity for DNA; increases sensitivity to oxidative stress; no significant differences in stability and structure compared with the wild-type. Ref.26
VAR_070181
Natural variant4461D → V in EDMD2. Ref.72
VAR_039780
Natural variant4491G → D in EDMD2. Ref.94
VAR_064971
Natural variant4531R → P in MDCL. Ref.89
VAR_063592
Natural variant4531R → W in EDMD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. Ref.43 Ref.47 Ref.48 Ref.53 Ref.55 Ref.72 Ref.94
VAR_009988
Natural variant4541L → P in EDMD2. Ref.94
VAR_064972
Natural variant4551R → P in MDCL. Ref.89
VAR_063593
Natural variant4561N → D in MDCL. Ref.89
VAR_063594
Natural variant4561N → I in EDMD2; mislocalized in the nucleus; does not alter nuclear size or shape. Ref.53 Ref.94
VAR_039781
Natural variant4561N → K in EDMD2. Ref.48
VAR_039782
Natural variant4611D → Y in EDMD2. Ref.94
VAR_064973
Natural variant4651G → D in FPLD2. Ref.45
VAR_009989
Natural variant4671W → R in EDMD2. Ref.94
VAR_064974
Natural variant4691I → T in EDMD2. Ref.47
VAR_009990
Natural variant4711R → C in HGPS. Ref.70
Corresponds to variant rs28928902 [ dbSNP | Ensembl ].
VAR_017662
Natural variant4711R → H in CMD1A; no effect on nuclear morphology and lamin A localization. Ref.29
VAR_070182
Natural variant4811Y → H in LGMD1B. Ref.56
VAR_039783
Natural variant4821R → L in FPLD2. Ref.51
VAR_009991
Natural variant4821R → Q in FPLD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. Ref.45 Ref.49 Ref.55
Corresponds to variant rs11575937 [ dbSNP | Ensembl ].
VAR_009992
Natural variant4821R → W in FPLD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type; decreases binding affinity for DNA; increases sensitivity to oxidative stress. Ref.26 Ref.45 Ref.51 Ref.55
VAR_009993
Natural variant4861K → N in FPLD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. Ref.55
VAR_009994
Natural variant5201W → S in EDMD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. Ref.48 Ref.55
VAR_039784
Natural variant5231G → R in CMD1A. Ref.92
VAR_067258
Natural variant5271R → C in HGPS. Ref.70
VAR_017663
Natural variant5271R → H in MADA. Ref.60
VAR_018727
Natural variant5271R → P in EDMD2 and FPLD2; interacts with itself and with wild-type LMNA and LMNB1; reduced binding to SUN1; no decrease in the stability compared with wild-type. Ref.31 Ref.43 Ref.47 Ref.48 Ref.53 Ref.55 Ref.64 Ref.74 Ref.84 Ref.94
VAR_009995
Natural variant5281T → K in EDMD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. Ref.47 Ref.48 Ref.55 Ref.94
VAR_009996
Natural variant5281T → R in EDMD2. Ref.72 Ref.94
VAR_039785
Natural variant5291A → V in MADA. Ref.83
VAR_034709
Natural variant5301L → P in EDMD2; interacts with itself and with wild-type LMNA and LMNB1; reduced binding to SUN1; no decrease in the stability compared with wild-type. Ref.31 Ref.43 Ref.55
VAR_009997
Natural variant5411R → C in apical left ventricular aneurysm. Ref.65
VAR_039786
Natural variant5411R → H in EDMD2. Ref.72
VAR_039787
Natural variant5411R → P in EDMD2; mis-localized in the nucleus; does not alter nuclear size or shape. Ref.94
VAR_064975
Natural variant5411R → S in EDMD2 and CMD1A; modest and non-specific nuclear membrane alterations; the phenotype is entirely reversed by coexpression of the S-541 mutation and wild-type lamin-C. Ref.3 Ref.94
VAR_039788
Natural variant5421K → N in HGPS. Ref.79
VAR_034710
Natural variant5731S → L in CMD1A, FPLD2 and MADA. Ref.67 Ref.85 Ref.87
VAR_039789
Natural variant5781E → V in an atypical progeroid patient; diagnosed as Werner syndrome. Ref.78
VAR_039790
Natural variant5821R → H in FPLD2. Ref.45
Corresponds to variant rs57830985 [ dbSNP | Ensembl ].
VAR_009998
Natural variant6021G → S in EDMD2. Ref.94
Corresponds to variant rs60662302 [ dbSNP | Ensembl ].
VAR_064976
Natural variant6081G → S in HGPS; reduced binding to SUN1; may affect splicing by activating a cryptic splice donor site. Ref.16 Ref.31 Ref.70
VAR_017664
Natural variant6241R → H in EDMD2. Ref.53
VAR_039791
Natural variant6441R → C in an atypical progeroid patient; diagnosed as Hutchinson-Gilford progeria syndrome; partially inhibits tail cleavage. Ref.36 Ref.78 Ref.94
VAR_039792

Experimental info

Mutagenesis2011K → L: Decreased sumoylation; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; associated with increased cell death. Ref.20
Mutagenesis6441R → A: Does not affect tail cleavage. Ref.36
Mutagenesis6471L → R: Completely inhibits tail cleavage. Ref.36
Mutagenesis6481L → A: Completely inhibits tail cleavage. Ref.36
Mutagenesis6501N → A: Partially inhibits tail cleavage. Ref.36
Mutagenesis6611C → S: Loss of interaction with NARF. Abolishes farnesylation. Ref.14 Ref.36
Sequence conflict3401E → K in BAG58344. Ref.5
Isoform 4:
Sequence conflict5561G → R in BAG58344. Ref.5

Secondary structure

........................... 664
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform A (Lamin A) [UniParc].

Last modified March 20, 1987. Version 1.
Checksum: E0855F7699F0318B

FASTA66474,139
        10         20         30         40         50         60 
METPSQRRAT RSGAQASSTP LSPTRITRLQ EKEDLQELND RLAVYIDRVR SLETENAGLR 

        70         80         90        100        110        120 
LRITESEEVV SREVSGIKAA YEAELGDARK TLDSVAKERA RLQLELSKVR EEFKELKARN 

       130        140        150        160        170        180 
TKKEGDLIAA QARLKDLEAL LNSKEAALST ALSEKRTLEG ELHDLRGQVA KLEAALGEAK 

       190        200        210        220        230        240 
KQLQDEMLRR VDAENRLQTM KEELDFQKNI YSEELRETKR RHETRLVEID NGKQREFESR 

       250        260        270        280        290        300 
LADALQELRA QHEDQVEQYK KELEKTYSAK LDNARQSAER NSNLVGAAHE ELQQSRIRID 

       310        320        330        340        350        360 
SLSAQLSQLQ KQLAAKEAKL RDLEDSLARE RDTSRRLLAE KEREMAEMRA RMQQQLDEYQ 

       370        380        390        400        410        420 
ELLDIKLALD MEIHAYRKLL EGEEERLRLS PSPTSQRSRG RASSHSSQTQ GGGSVTKKRK 

       430        440        450        460        470        480 
LESTESRSSF SQHARTSGRV AVEEVDEEGK FVRLRNKSNE DQSMGNWQIK RQNGDDPLLT 

       490        500        510        520        530        540 
YRFPPKFTLK AGQVVTIWAA GAGATHSPPT DLVWKAQNTW GCGNSLRTAL INSTGEEVAM 

       550        560        570        580        590        600 
RKLVRSVTVV EDDEDEDGDD LLHHHHGSHC SSSGDPAEYN LRSRTVLCGT CGQPADKASA 

       610        620        630        640        650        660 
SGSGAQVGGP ISSGSSASSV TVTRSYRSVG GSGGGSFGDN LVTRSYLLGN SSPRTQSPQN 


CSIM 

« Hide

Isoform C (Lamin C) [UniParc].

Checksum: CFF0FE0F230FCDE2
Show »

FASTA57265,135
Isoform ADelta10 (Lamin ADelta10) [UniParc].

Checksum: 4ED0A48922D0A9F7
Show »

FASTA63470,661
Isoform 4 [UniParc].

Checksum: 194BC5E15265F657
Show »

FASTA57463,893
Isoform 5 [UniParc].

Checksum: 6C95CF2145496D6F
Show »

FASTA56562,853
Isoform 6 (Progerin) [UniParc].

Checksum: CF89C559FAE39BC4
Show »

FASTA61469,249

References

« Hide 'large scale' references
[1]"Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins."
McKeon F.D., Kirschner M.W., Caput D.
Nature 319:463-468(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND C).
[2]"cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins."
Fisher D.Z., Chaudhary N., Blobel G.
Proc. Natl. Acad. Sci. U.S.A. 83:6450-6454(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND C), PROTEIN SEQUENCE OF 583-644.
[3]"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) [PubMed] [Europe PMC] [Abstract]
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.
[4]"The progerin allele of lamin A disrupts chromatin organization."
Csoka A.B.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Corpus callosum.
[6]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND C).
Tissue: Kidney, Lung and Skin.
[9]Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W., Norman J.C.
Submitted (OCT-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 12-25; 29-90; 102-117; 120-166; 172-189; 197-216; 226-233; 241-260; 281-316; 320-329; 352-386; 440-453; 456-482; 472-482; 516-542; 585-624 AND 628-644, PHOSPHORYLATION AT SER-22, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[10]"An alternative splicing product of the lamin A/C gene lacks exon 10."
Machiels B.M., Zorenc A.H., Endert J.M., Kuijpers H.J., van Eys G.J., Ramaekers F.C., Broers J.L.
J. Biol. Chem. 271:9249-9253(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 375-664 (ISOFORM ADELTA10).
Tissue: Colon.
[11]"The processing pathway of prelamin A."
Sinensky M., Fantle K., Trujillo M., McLain T., Kupfer A., Dalton M.
J. Cell Sci. 107:61-67(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC CLEAVAGE, ISOPRENYLATION AT CYS-661, METHYLATION AT CYS-661.
[12]"In vitro assay and characterization of the farnesylation-dependent prelamin A endoprotease."
Kilic F., Dalton M.B., Burrell S.K., Mayer J.P., Patterson S.D., Sinensky M.
J. Biol. Chem. 272:5298-5304(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC CLEAVAGE, ISOPRENYLATION AT CYS-661, METHYLATION AT CYS-661.
[13]"Antigens recognized by autologous antibody in patients with renal-cell carcinoma."
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J.
Int. J. Cancer 83:456-464(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
Tissue: Renal cell carcinoma.
[14]"Prenylated prelamin A interacts with Narf, a novel nuclear protein."
Barton R.M., Worman H.J.
J. Biol. Chem. 274:30008-30018(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NARF, MUTAGENESIS OF CYS-661.
[15]"Lamin A/C binding protein LAP2alpha is required for nuclear anchorage of retinoblastoma protein."
Markiewicz E., Dechat T., Foisner R., Quinlan R.A., Hutchison C.J.
Mol. Biol. Cell 13:4401-4413(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TMPO-ALPHA AND RB1.
[16]"Recurrent de novo point mutations in lamin A cause Hutchinson-Gilford progeria syndrome."
Eriksson M., Brown W.T., Gordon L.B., Glynn M.W., Singer J., Scott L., Erdos M.R., Robbins C.M., Moses T.Y., Berglund P., Dutra A., Pak E., Durkin S., Csoka A.B., Boehnke M., Glover T.W., Collins F.S.
Nature 423:293-298(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING, INVOLVEMENT IN HGPS (ISOFORM 6), VARIANTS HGPS LYS-145 AND SER-608.
[17]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-22; SER-390; SER-392; SER-395; SER-628; SER-632 AND SER-636, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-628, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, SUMOYLATION AT LYS-201, MUTAGENESIS OF LYS-201, CHARACTERIZATION OF VARIANTS CMD1A GLY-203 AND LYS-203.
[21]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-628, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-18; THR-19; SER-22; SER-301; SER-390; SER-392; SER-395; SER-458; SER-628; SER-632; SER-636 AND SER-652, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"Emerin-prelamin A interplay in human fibroblasts."
Capanni C., Del Coco R., Mattioli E., Camozzi D., Columbaro M., Schena E., Merlini L., Squarzoni S., Maraldi N.M., Lattanzi G.
Biol. Cell 101:541-554(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH EMD.
[26]"The R439C mutation in LMNA causes lamin oligomerization and susceptibility to oxidative stress."
Verstraeten V.L., Caputo S., van Steensel M.A., Duband-Goulet I., Zinn-Justin S., Kamps M., Kuijpers H.J., Ostlund C., Worman H.J., Briede J.J., Le Dour C., Marcelis C.L., van Geel M., Steijlen P.M., van den Wijngaard A., Ramaekers F.C., Broers J.L.
J. Cell. Mol. Med. 13:959-971(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS FPLD2 CYS-439 AND TRP-482.
[27]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-108; LYS-270; LYS-311 AND LYS-450, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"Increased plasticity of the nuclear envelope and hypermobility of telomeres due to the loss of A-type lamins."
De Vos W.H., Houben F., Hoebe R.A., Hennekam R., van Engelen B., Manders E.M., Ramaekers F.C., Broers J.L., Van Oostveldt P.
Biochim. Biophys. Acta 1800:448-458(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[29]"Morphological analysis of 13 LMNA variants identified in a cohort of 324 unrelated patients with idiopathic or familial dilated cardiomyopathy."
Cowan J., Li D., Gonzalez-Quintana J., Morales A., Hershberger R.E.
Circ. Cardiovasc. Genet. 3:6-14(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, VARIANTS CMD1A LEU-89; PRO-101; PRO-166; GLN-190; LYS-203; SER-210; PRO-215; THR-318; HIS-388; CYS-399 AND HIS-471.
[30]"Prelamin A acts to accelerate smooth muscle cell senescence and is a novel biomarker of human vascular aging."
Ragnauth C.D., Warren D.T., Liu Y., McNair R., Tajsic T., Figg N., Shroff R., Skepper J., Shanahan C.M.
Circulation 121:2200-2210(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PROTEOLYTIC PROCESSING, TISSUE SPECIFICITY.
[31]"Mammalian SUN protein interaction networks at the inner nuclear membrane and their role in laminopathy disease processes."
Haque F., Mazzeo D., Patel J.T., Smallwood D.T., Ellis J.A., Shanahan C.M., Shackleton S.
J. Biol. Chem. 285:3487-3498(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SUN1, CHARACTERIZATION OF VARIANTS EDMD2 PRO-527 AND PRO-530, CHARACTERIZATION OF VARIANT HGPS SER-608.
[32]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3; SER-12; THR-19; SER-22; SER-212; SER-277; SER-301; SER-390; SER-392; SER-395; SER-404; SER-414; SER-431; SER-458; SER-463; THR-505; SER-628; SER-632; SER-636 AND SER-652, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[33]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[34]"Identification of a novel muscle enriched A-type Lamin interacting protein (MLIP)."
Ahmady E., Deeke S.A., Rabaa S., Kouri L., Kenney L., Stewart A.F., Burgon P.G.
J. Biol. Chem. 286:19702-19713(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MLIP.
[35]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390; SER-392; SER-404; SER-414; SER-458 AND SER-636, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[36]"Requirements for efficient proteolytic cleavage of prelamin A by ZMPSTE24."
Barrowman J., Hamblet C., Kane M.S., Michaelis S.
PLoS ONE 7:E32120-E32120(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ARG-644; LEU-647; LEU-648; ASN-650 AND CYS-661, CHARACTERIZATION OF VARIANT HGPS CYS-644.
[37]"LMNA-associated cardiocutaneous progeria: An inherited autosomal dominant premature aging syndrome with late onset."
Kane M.S., Lindsay M.E., Judge D.P., Barrowman J., Ap Rhys C., Simonson L., Dietz H.C., Michaelis S.
Am. J. Med. Genet. A 161:1599-1611(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, DISEASE, VARIANT GLY-300.
[38]"Depleting the methyltransferase Suv39h1 improves DNA repair and extends lifespan in a progeria mouse model."
Liu B., Wang Z., Zhang L., Ghosh S., Zheng H., Zhou Z.
Nat. Commun. 4:1868-1868(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SUV39H1.
[39]"Myotonic dystrophy protein kinase is critical for nuclear envelope integrity."
Harmon E.B., Harmon M.L., Larsen T.D., Yang J., Glasford J.W., Perryman M.B.
J. Biol. Chem. 286:40296-40306(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DMPK.
[40]"Structure of the globular tail of nuclear lamin."
Dhe-Paganon S., Werner E.D., Chi Y.I., Shoelson S.E.
J. Biol. Chem. 277:17381-17384(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 435-552.
[41]"The Ig-like structure of the C-terminal domain of lamin A/C, mutated in muscular dystrophies, cardiomyopathy, and partial lipodystrophy."
Krimm I., Ostlund C., Gilquin B., Couprie J., Hossenlopp P., Mornon J.-P., Bonne G., Courvalin J.-C., Worman H.J., Zinn-Justin S.
Structure 10:811-823(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 428-549.
[42]"Crystal structure of the human lamin A coil 2B dimer: implications for the head-to-tail association of nuclear lamins."
Strelkov S.V., Schumacher J., Burkhard P., Aebi U., Herrmann H.
J. Mol. Biol. 343:1067-1080(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 305-387.
[43]"Mutations in the gene encoding lamin A/C cause autosomal dominant Emery-Dreifuss muscular dystrophy."
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.
Nat. Genet. 21:285-288(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EDMD2 TRP-453; PRO-527 AND PRO-530.
[44]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CMD1A GLY-60; ARG-85; LYS-195 AND GLY-203.
[45]"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."
Speckman R.A., Garg A., Du F., Bennett L., Veile R., Arioglu E., Taylor S.I., Lovett M., Bowcock A.M.
Am. J. Hum. Genet. 66:1192-1198(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FPLD2 ASP-465; GLN-482; TRP-482 AND HIS-582.
[46]Erratum
Speckman R.A., Garg A., Du F., Bennett L., Veile R., Arioglu E., Taylor S.I., Lovett M., Bowcock A.M.
Am. J. Hum. Genet. 67:775-775(2000)
[47]"Different mutations in the LMNA gene cause autosomal dominant and autosomal recessive Emery-Dreifuss muscular dystrophy."
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.
Am. J. Hum. Genet. 66:1407-1412(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EDMD2 TYR-222; GLN-249; GLN-336; TRP-453; THR-469; PRO-527 AND LYS-528.
[48]"Clinical and molecular genetic spectrum of autosomal dominant Emery-Dreifuss muscular dystrophy due to mutations of the lamin A/C gene."
Bonne G., Mercuri E., Muchir A., Urtizberea A., Becane H.M., Recan D., Merlini L., Wehnert M., Boor R., Reuner U., Vorgerd M., Wicklein E.M., Eymard B., Duboc D., Penisson-Besnier I., Cuisset J.M., Ferrer X., Desguerre I. expand/collapse author list , Lacombe D., Bushby K., Pollitt C., Toniolo D., Fardeau M., Schwartz K., Muntoni F.
Ann. Neurol. 48:170-180(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EDMD2 CYS-45; PRO-50; SER-63; GLU-112 DEL; PRO-222; GLU-232; GLN-249; LYS-261 DEL; PRO-294; LYS-358; LYS-371; LYS-386; TRP-453; LYS-456; SER-520; PRO-527 AND LYS-528.
[49]"Nuclear lamin A/C R482Q mutation in Canadian kindreds with Dunnigan-type familial partial lipodystrophy."
Cao H., Hegele R.A.
Hum. Mol. Genet. 9:109-112(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FPLD2 GLN-482.
[50]"Identification of mutations in the gene encoding lamins A/C in autosomal dominant limb girdle muscular dystrophy with atrioventricular conduction disturbances (LGMD1B)."
Muchir A., Bonne G., van der Kooi A.J., van Meegen M., Baas F., Bolhuis P.A., de Visser M., Schwartz K.
Hum. Mol. Genet. 9:1453-1459(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LGMD1B LYS-208 DEL AND HIS-377.
[51]"LMNA, encoding lamin A/C, is mutated in partial lipodystrophy."
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.
Nat. Genet. 24:153-156(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FPLD2 LEU-482 AND TRP-482.
[52]"Autosomal dominant Emery-Dreifuss dystrophy due to mutations in rod domain of the lamin A/C gene."
Felice K.J., Schwartz R.C., Brown C.A., Leicher C.R., Grunnet M.L.
Neurology 55:275-280(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EDMD2 PRO-150 AND LYS-261 DEL.
[53]"Novel and recurrent mutations in lamin A/C in patients with Emery-Dreifuss muscular dystrophy."
Brown C.A., Lanning R.W., McKinney K.Q., Salvino A.R., Cherniske E., Crowe C.A., Darras B.T., Gominak S., Greenberg C.R., Grosmann C., Heydemann P., Mendell J.R., Pober B.R., Sasaki T., Shapiro F., Simpson D.A., Suchowersky O., Spence J.E.
Am. J. Med. Genet. 102:359-367(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EDMD2 PRO-25; THR-43; SER-50; PRO-133; 196-ARG--THR-199 DELINS SER; GLN-249; LYS-261 DEL; LYS-358; TRP-453; ILE-456; PRO-527 AND HIS-624.
[54]"Novel lamin A/C mutations in two families with dilated cardiomyopathy and conduction system disease."
Jakobs P.M., Hanson E.L., Crispell K.A., Toy W., Keegan H., Schilling K., Icenogle T.B., Litt M., Hershberger R.E.
J. Card. Fail. 7:249-256(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMD1A LYS-203.
[55]"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) [PubMed] [Europe PMC] [Abstract]
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.
[56]"A missense mutation in the exon 8 of lamin A/C gene in a Japanese case of autosomal dominant limb-girdle muscular dystrophy and cardiac conduction block."
Kitaguchi T., Matsubara S., Sato M., Miyamoto K., Hirai S., Schwartz K., Bonne G.
Neuromuscul. Disord. 11:542-546(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LGMD1B HIS-481.
[57]"A novel lamin A/C mutation in a family with dilated cardiomyopathy, prominent conduction system disease, and need for permanent pacemaker implantation."
Hershberger R.E., Hanson E.L., Jakobs P.M., Keegan H., Coates K., Bousman S., Litt M.
Am. Heart J. 144:1081-1086(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMD1A PRO-215.
[58]"Homozygous defects in LMNA, encoding lamin A/C nuclear-envelope proteins, cause autosomal recessive axonal neuropathy in human (Charcot-Marie-Tooth disorder type 2) and mouse."
De Sandre-Giovannoli A., Chaouch M., Kozlov S., Vallat J.-M., Tazir M., Kassouri N., Szepetowski P., Hammadouche T., Vandenberghe A., Stewart C.L., Grid D., Levy N.
Am. J. Hum. Genet. 70:726-736(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMT2B1 CYS-298.
[59]Erratum
De Sandre-Giovannoli A., Chaouch M., Kozlov S., Vallat J.-M., Tazir M., Kassouri N., Szepetowski P., Hammadouche T., Vandenberghe A., Stewart C.L., Grid D., Levy N.
Am. J. Hum. Genet. 70:1075-1075(2002)
[60]"Mandibuloacral dysplasia is caused by a mutation in LMNA-encoding lamin A/C."
Novelli G., Muchir A., Sangiuolo F., Helbling-Leclerc A., D'Apice M.R., Massart C., Capon F., Sbraccia P., Federici M., Lauro R., Tudisco C., Pallotta R., Scarano G., Dallapiccola B., Merlini L., Bonne G.
Am. J. Hum. Genet. 71:426-431(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MADA HIS-527.
[61]"Multisystem dystrophy syndrome due to novel missense mutations in the amino-terminal head and alpha-helical rod domains of the lamin A/C gene."
Garg A., Speckman R.A., Bowcock A.M.
Am. J. Med. 112:549-555(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FPLD2 TRP-28 AND GLY-62.
[62]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CMD1A GLU-97; TRP-190 AND LYS-317.
[63]"Identification of lamin A/C (LMNA) gene mutations in Korean patients with autosomal dominant Emery-Dreifuss muscular dystrophy and limb-girdle muscular dystrophy 1B."
Ki C.-S., Hong J.S., Jeong G.-Y., Ahn K.J., Choi K.-M., Kim D.-K., Kim J.-W.
J. Hum. Genet. 47:225-228(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EDMD2 GLN-249, VARIANT LGMD1B LEU-377.
[64]"Lamin A/C mutations with lipodystrophy, cardiac abnormalities, and muscular dystrophy."
van der Kooi A.J., Bonne G., Eymard B., Duboc D., Talim B., Van der Valk M., Reiss P., Richard P., Demay L., Merlini L., Schwartz K., Busch H.F.M., de Visser M.
Neurology 59:620-623(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FPLD2 GLY-60 AND PRO-527.
[65]"Apical left ventricular aneurysm without atrio-ventricular block due to a lamin A/C gene mutation."
Forissier J.-F., Bonne G., Bouchier C., Duboscq-Bidot L., Richard P., Wisnewski C., Briault S., Moraine C., Dubourg O., Schwartz K., Komajda M.
Eur. J. Heart Fail. 5:821-825(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT APICAL LEFT VENTRICULAR ANEURYSM CYS-541.
[66]"Functional consequences of an LMNA mutation associated with a new cardiac and non-cardiac phenotype."
Charniot J.-C., Pascal C., Bouchier C., Sebillon P., Salama J., Duboscq-Bidot L., Peuchmaurd M., Desnos M., Artigou J.-Y., Komajda M.
Hum. Mutat. 21:473-481(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LGMD1B HIS-377.
[67]"Natural history of dilated cardiomyopathy due to lamin A/C gene mutations."
Familial dilated cardiomyopathy registry research group
Taylor M.R.G., Fain P.R., Sinagra G., Robinson M.L., Robertson A.D., Carniel E., Di Lenarda A., Bohlmeyer T.J., Ferguson D.A., Brodsky G.L., Boucek M.M., Lascor J., Moss A.C., Li W.-L.P., Stetler G.L., Muntoni F., Bristow M.R., Mestroni L.
J. Am. Coll. Cardiol. 41:771-780(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CMD1A LEU-89; HIS-377 AND LEU-573.
[68]Erratum
Familial dilated cardiomyopathy registry research group
Taylor M.R.G., Fain P.R., Sinagra G., Robinson M.L., Robertson A.D., Carniel E., Di Lenarda A., Bohlmeyer T.J., Ferguson D.A., Brodsky G.L., Boucek M.M., Lascor J., Moss A.C., Li W.-L.P., Stetler G.L., Muntoni F., Bristow M.R., Mestroni L.
J. Am. Coll. Cardiol. 42:590-590(2003)
[69]"A new clinical condition linked to a novel mutation in lamins A and C with generalized lipoatrophy, insulin-resistant diabetes, disseminated leukomelanodermic papules, liver steatosis, and cardiomyopathy."
Caux F., Dubosclard E., Lascols O., Buendia B., Chazouilleres O., Cohen A., Courvalin J.-C., Laroche L., Capeau J., Vigouroux C., Christin-Maitre S.
J. Clin. Endocrinol. Metab. 88:1006-1013(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FPLD2 LEU-133.
[70]"LMNA is mutated in Hutchinson-Gilford progeria (MIM 176670) but not in Wiedemann-Rautenstrauch progeroid syndrome (MIM 264090)."
Cao H., Hegele R.A.
J. Hum. Genet. 48:271-274(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HGPS CYS-471; CYS-527 AND SER-608.
[71]"Expanding the phenotype of LMNA mutations in dilated cardiomyopathy and functional consequences of these mutations."
Sebillon P., Bouchier C., Bidot L.D., Bonne G., Ahamed K., Charron P., Drouin-Garraud V., Millaire A., Desrumeaux G., Benaiche A., Charniot J.-C., Schwartz K., Villard E., Komajda M.
J. Med. Genet. 40:560-567(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMD1A LYS-161.
[72]"Mutation analysis of the lamin A/C gene (LMNA) among patients with different cardiomuscular phenotypes."
Vytopil M., Benedetti S., Ricci E., Galluzzi G., Dello Russo A., Merlini L., Boriani G., Gallina M., Morandi L., Politano L., Moggio M., Chiveri L., Hausmanova-Petrusewicz I., Ricotti R., Vohanka S., Toman J., Toniolo D.
J. Med. Genet. 40:E132-E132(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EDMD2 GLY-25; LYS-32 DEL; VAL-35; GLY-65; GLU-112 DEL; PRO-248; GLN-249; CYS-267; VAL-446; TRP-453; ARG-528 AND HIS-541, VARIANT CMD1A CYS-435.
[73]"LMNA mutations in atypical Werner's syndrome."
Chen L., Lee L., Kudlow B.A., Dos Santos H.G., Sletvold O., Shafeghati Y., Botha E.G., Garg A., Hanson N.B., Martin G.M., Mian I.S., Kennedy B.K., Oshima J.
Lancet 362:440-445(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMDHH PRO-57, VARIANT HGPS ARG-140.
[74]"Clinical relevance of atrial fibrillation/flutter, stroke, pacemaker implant, and heart failure in Emery-Dreifuss muscular dystrophy: a long-term longitudinal study."
Boriani G., Gallina M., Merlini L., Bonne G., Toniolo D., Amati S., Biffi M., Martignani C., Frabetti L., Bonvicini M., Rapezzi C., Branzi A.
Stroke 34:901-908(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EDMD2 ASN-63; PRO-140; GLN-249; LEU-377; LYS-386 AND PRO-527.
[75]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CMD1A TRP-190 AND LEU-349.
[76]"A novel mutation, Ser143Pro, in the lamin A/C gene is common in Finnish patients with familial dilated cardiomyopathy."
Kaerkkaeinen S., Helioe T., Miettinen R., Tuomainen P., Peltola P., Rummukainen J., Ylitalo K., Kaartinen M., Kuusisto J., Toivonen L., Nieminen M.S., Laakso M., Peuhkurinen K.
Eur. Heart J. 25:885-893(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMD1A PRO-143.
[77]"Lamin A and ZMPSTE24 (FACE-1) defects cause nuclear disorganization and identify restrictive dermopathy as a lethal neonatal laminopathy."
Navarro C.L., De Sandre-Giovannoli A., Bernard R., Boccaccio I., Boyer A., Genevieve D., Hadj-Rabia S., Gaudy-Marqueste C., Smitt H.S., Vabres P., Faivre L., Verloes A., Van Essen T., Flori E., Hennekam R., Beemer F.A., Laurent N., Le Merrer M., Cau P., Levy N.
Hum. Mol. Genet. 13:2493-2503(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN LTSCS.
[78]"Novel lamin A/C gene (LMNA) mutations in atypical progeroid syndromes."
Csoka A.B., Cao H., Sammak P.J., Constantinescu D., Schatten G.P., Hegele R.A.
J. Med. Genet. 41:304-308(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ILE-10; VAL-578 AND CYS-644.
[79]"Homozygous missense mutation in the lamin A/C gene causes autosomal recessive Hutchinson-Gilford progeria syndrome."
Plasilova M., Chattopadhyay C., Pal P., Schaub N.A., Buechner S.A., Mueller H., Miny P., Ghosh A., Heinimann K.
J. Med. Genet. 41:609-614(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HGPS ASN-542.
[80]"A new mutation of the lamin A/C gene leading to autosomal dominant axonal neuropathy, muscular dystrophy, cardiac disease, and leuconychia."
Goizet C., Yaou R.B., Demay L., Richard P., Bouillot S., Rouanet M., Hermosilla E., Le Masson G., Lagueny A., Bonne G., Ferrer X.
J. Med. Genet. 41:E29-E29(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMT2 ASP-33, VARIANT EDMD2 GLY-33.
[81]"p.S143F mutation in lamin A/C: a new phenotype combining myopathy and progeria."
Kirschner J., Brune T., Wehnert M., Denecke J., Wasner C., Feuer A., Marquardt T., Ketelsen U.-P., Wieacker P., Boennemann C.G., Korinthenberg R.
Ann. Neurol. 57:148-151(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HGPS PHE-143.
[82]"Gene symbol: LMNA. Disease: cardiomyopathy, dilated, with conduction defect 1."
Arbustini Eloisa A.E., Pilotto A., Pasotti M., Grasso M., Diegoli M., Campana C., Gavazzi A., Alessandra R., Tavazzi L.
Hum. Genet. 117:298-298(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMDA1 ASN-260.
[83]"A novel homozygous Ala529Val LMNA mutation in Turkish patients with mandibuloacral dysplasia."
Garg A., Cogulu O., Ozkinay F., Onay H., Agarwal A.K.
J. Clin. Endocrinol. Metab. 90:5259-5264(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MADA VAL-529.
[84]"Lamin A N-terminal phosphorylation is associated with myoblast activation: impairment in Emery-Dreifuss muscular dystrophy."
Cenni V., Sabatelli P., Mattioli E., Marmiroli S., Capanni C., Ognibene A., Squarzoni S., Maraldi N.M., Bonne G., Columbaro M., Merlini L., Lattanzi G.
J. Med. Genet. 42:214-220(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LGMD1B HIS-377, VARIANTS EDMD2 ASN-63; PRO-140; GLN-190; GLN-249 AND PRO-527.
[85]"A homozygous mutation in the lamin A/C gene associated with a novel syndrome of arthropathy, tendinous calcinosis, and progeroid features."
Van Esch H., Agarwal A.K., Debeer P., Fryns J.-P., Garg A.
J. Clin. Endocrinol. Metab. 91:517-521(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MADA LEU-573.
[86]"Collagen expression in fibroblasts with a novel LMNA mutation."
Nguyen D., Leistritz D.F., Turner L., MacGregor D., Ohson K., Dancey P., Martin G.M., Oshima J.
Biochem. Biophys. Res. Commun. 352:603-608(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMDHH ARG-59.
[87]"Novel LMNA mutations seen in patients with familial partial lipodystrophy subtype 2 (FPLD2; MIM 151660)."
Lanktree M., Cao H., Rabkin S.W., Hanna A., Hegele R.A.
Clin. Genet. 71:183-186(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FPLD2 ASN-230; CYS-399 AND LEU-573.
[88]"Mutations of the LMNA gene can mimic autosomal dominant proximal spinal muscular atrophy."
Rudnik-Schoeneborn S., Botzenhart E., Eggermann T., Senderek J., Schoser B.G.H., Schroeder R., Wehnert M., Wirth B., Zerres K.
Neurogenetics 8:137-142(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LGMD1B HIS-377.
[89]"De novo LMNA mutations cause a new form of congenital muscular dystrophy."
Quijano-Roy S., Mbieleu B., Bonnemann C.G., Jeannet P.Y., Colomer J., Clarke N.F., Cuisset J.M., Roper H., De Meirleir L., D'Amico A., Ben Yaou R., Nascimento A., Barois A., Demay L., Bertini E., Ferreiro A., Sewry C.A., Romero N.B. expand/collapse author list , Ryan M., Muntoni F., Guicheney P., Richard P., Bonne G., Estournet B.
Ann. Neurol. 64:177-186(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MDCL SER-39; PRO-50; TRP-249; PRO-302; LYS-358; SER-380; PRO-453; PRO-455 AND ASP-456.
[90]"Heart-hand syndrome of Slovenian type: a new kind of laminopathy."
Renou L., Stora S., Yaou R.B., Volk M., Sinkovec M., Demay L., Richard P., Peterlin B., Bonne G.
J. Med. Genet. 45:666-671(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HHS-SLOVENIAN.
[91]"Ovarian failure and dilated cardiomyopathy due to a novel lamin mutation."
McPherson E., Turner L., Zador I., Reynolds K., Macgregor D., Giampietro P.F.
Am. J. Med. Genet. A 149:567-572(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMDHH ARG-59.
[92]"Clinical and mutational spectrum in a cohort of 105 unrelated patients with dilated cardiomyopathy."
Millat G., Bouvagnet P., Chevalier P., Sebbag L., Dulac A., Dauphin C., Jouk P.S., Delrue M.A., Thambo J.B., Le Metayer P., Seronde M.F., Faivre L., Eicher J.C., Rousson R.
Eur. J. Med. Genet. 54:E570-E575(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CMD1A PHE-92; LYS-161; LYS-317 AND ARG-523.
[93]"LMNA mutation in progeroid syndrome in association with strokes."
Gonzalez-Quereda L., Delgadillo V., Juan-Mateu J., Verdura E., Rodriguez M.J., Baiget M., Pineda M., Gallano P.
Eur. J. Med. Genet. 54:E576-E579(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HGPS LYS-138.
[94]"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) [PubMed] [Europe PMC] [Abstract]
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.
[95]"Autosomal recessive Emery-Dreifuss muscular dystrophy caused by a novel mutation (R225Q) in the lamin A/C gene identified by exome sequencing."
Jimenez-Escrig A., Gobernado I., Garcia-Villanueva M., Sanchez-Herranz A.
Muscle Nerve 45:605-610(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EDMD3 GLN-225.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03444 mRNA. Translation: CAA27173.1. Frameshift.
X03445 mRNA. Translation: CAA27174.1.
M13451 mRNA. Translation: AAA36164.1.
M13452 mRNA. Translation: AAA36160.1.
AY847597 mRNA. Translation: AAW32540.1.
AY847595 mRNA. Translation: AAW32538.1.
AY357727 mRNA. Translation: AAR29466.1.
AK295390 mRNA. Translation: BAG58344.1.
AL135927 Genomic DNA. Translation: CAI15521.1.
AL135927 Genomic DNA. Translation: CAI15522.1.
AL355388 Genomic DNA. No translation available.
AL356734 Genomic DNA. No translation available.
CH471121 Genomic DNA. Translation: EAW52997.1.
CH471121 Genomic DNA. Translation: EAW52999.1.
BC000511 mRNA. Translation: AAH00511.1.
BC003162 mRNA. Translation: AAH03162.1.
BC014507 mRNA. Translation: AAH14507.1.
AF381029 mRNA. Translation: AAK59326.1.
CCDSCCDS1129.1. [P02545-1]
CCDS1131.1. [P02545-2]
CCDS58038.1. [P02545-4]
PIRVEHULA. A02961.
VEHULC. A02962.
RefSeqNP_001244303.1. NM_001257374.2. [P02545-4]
NP_001269553.1. NM_001282624.1.
NP_001269554.1. NM_001282625.1. [P02545-2]
NP_001269555.1. NM_001282626.1. [P02545-6]
NP_005563.1. NM_005572.3. [P02545-2]
NP_733821.1. NM_170707.3. [P02545-1]
NP_733822.1. NM_170708.3. [P02545-3]
UniGeneHs.594444.
Hs.706897.
Hs.733671.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IFRX-ray1.40A436-552[»]
1IVTNMR-A428-549[»]
1X8YX-ray2.20A305-387[»]
2XV5X-ray2.40A/B328-398[»]
2YPTX-ray3.80F/G/H/I661-664[»]
3GEFX-ray1.50A/B/C/D436-552[»]
3V4QX-ray3.06A313-386[»]
3V4WX-ray3.70A313-386[»]
3V5BX-ray3.00A313-386[»]
DisProtDP00716.
ProteinModelPortalP02545.
SMRP02545. Positions 27-119, 313-386, 435-544.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110186. 195 interactions.
DIPDIP-32948N.
DIP-58162N.
IntActP02545. 44 interactions.
MINTMINT-5003995.
STRING9606.ENSP00000357283.

Chemistry

ChEMBLCHEMBL1293235.

PTM databases

PhosphoSiteP02545.

Polymorphism databases

DMDM125962.

2D gel databases

REPRODUCTION-2DPAGEIPI00021405.
IPI00216952.
P02545.
SWISS-2DPAGEP02545.

Proteomic databases

MaxQBP02545.
PaxDbP02545.
PeptideAtlasP02545.
PRIDEP02545.

Protocols and materials databases

DNASU4000.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000347559; ENSP00000292304; ENSG00000160789. [P02545-3]
ENST00000361308; ENSP00000355292; ENSG00000160789. [P02545-2]
ENST00000368299; ENSP00000357282; ENSG00000160789. [P02545-6]
ENST00000368300; ENSP00000357283; ENSG00000160789. [P02545-1]
ENST00000368301; ENSP00000357284; ENSG00000160789. [P02545-2]
ENST00000448611; ENSP00000395597; ENSG00000160789. [P02545-4]
ENST00000473598; ENSP00000421821; ENSG00000160789. [P02545-5]
ENST00000508500; ENSP00000424977; ENSG00000160789.
GeneID4000.
KEGGhsa:4000.
UCSCuc001fnf.1. human. [P02545-2]
uc001fnh.3. human. [P02545-3]
uc001fni.3. human. [P02545-1]
uc009wro.2. human.

Organism-specific databases

CTD4000.
GeneCardsGC01P156053.
GeneReviewsLMNA.
HGNCHGNC:6636. LMNA.
HPACAB004022.
HPA006660.
HPA012078.
MIM115200. phenotype.
150330. gene.
151660. phenotype.
159001. phenotype.
176670. phenotype.
181350. phenotype.
212112. phenotype.
248370. phenotype.
275210. phenotype.
605588. phenotype.
610140. phenotype.
613205. phenotype.
neXtProtNX_P02545.
Orphanet79474. Atypical Werner syndrome.
280365. Autosomal codominant severe lipodystrophic laminopathy.
98853. Autosomal dominant Emery-Dreifuss muscular dystrophy.
264. Autosomal dominant limb-girdle muscular dystrophy type 1B.
98855. Autosomal recessive Emery-Dreifuss muscular dystrophy.
98856. Charcot-Marie-Tooth disease type 2B1.
157973. Congenital muscular dystrophy due to LMNA mutation.
2229. Dilated cardiomyopathy - hypergonadotropic hypogonadism.
300751. Familial dilated cardiomyopathy with conduction defect due to LMNA mutation.
293899. Familial isolated arrhythmogenic ventricular dysplasia, biventricular form.
293888. Familial isolated arrhythmogenic ventricular dysplasia, left dominant form.
293910. Familial isolated arrhythmogenic ventricular dysplasia, right dominant form.
2348. Familial partial lipodystrophy, Dunnigan type.
79084. Familial partial lipodystrophy, Kobberling type.
168796. Heart-hand syndrome, Slovenian type.
740. Hutchinson-Gilford progeria syndrome.
137871. Laminopathy type Decaudain-Vigouroux.
54260. Left ventricular noncompaction.
1662. Lethal restrictive dermopathy.
363618. LMNA-related cardiocutaneous progeria syndrome.
90153. Mandibuloacral dysplasia with type A lipodystrophy.
99706. Progeria-associated arthropathy.
PharmGKBPA231.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG325506.
HOVERGENHBG013015.
InParanoidP02545.
KOK12641.
OMAHCSGSGD.
OrthoDBEOG7MD4PW.
PhylomeDBP02545.
TreeFamTF101181.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_17015. Metabolism of proteins.
REACT_21300. Mitotic M-M/G1 phases.
REACT_578. Apoptosis.

Gene expression databases

ArrayExpressP02545.
BgeeP02545.
CleanExHS_LMNA.
GenevestigatorP02545.

Family and domain databases

Gene3D2.60.40.1260. 1 hit.
InterProIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR001322. Lamin_tail_dom.
[Graphical view]
PANTHERPTHR23239. PTHR23239. 1 hit.
PfamPF00038. Filament. 1 hit.
PF00932. LTD. 1 hit.
[Graphical view]
SUPFAMSSF74853. SSF74853. 1 hit.
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLMNA. human.
EvolutionaryTraceP02545.
GeneWikiLMNA.
GenomeRNAi4000.
NextBio15692.
PMAP-CutDBP02545.
PROP02545.
SOURCESearch...

Entry information

Entry nameLMNA_HUMAN
AccessionPrimary (citable) accession number: P02545
Secondary accession number(s): B4DI32 expand/collapse secondary AC list , D3DVB0, D6RAQ3, E7EUI9, P02546, Q5I6Y4, Q5I6Y6, Q5TCJ2, Q5TCJ3, Q6UYC3, Q969I8, Q96JA2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 20, 1987
Last modified: July 9, 2014
This is version 197 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM