P02545 (LMNA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	664 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Play an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics. Ref.30 Ref.31 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.30 Ref.31
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. Ref.11 Ref.12 Ref.28 Ref.32 Ref.34 Ref.35
Subcellular location	Nucleus. Nucleus envelope. 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.23 Ref.28
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.31
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. Farnesylation of prelamin-A/C facilitates nuclear envelope targeting.
Involvement in disease	Defects in LMNA are the cause of Emery-Dreifuss muscular dystrophy type 2 (EDMD2) [MIM:181350]. 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. Ref.32 Ref.39 Ref.43 Ref.44 Ref.48 Ref.49 Ref.51 Ref.59 Ref.68 Ref.71 Ref.77 Ref.81 Ref.90 Defects in LMNA are the cause of cardiomyopathy dilated type 1A (CMD1A) [MIM:115200]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. Ref.23 Ref.40 Ref.50 Ref.51 Ref.53 Ref.58 Ref.63 Ref.67 Ref.68 Ref.72 Ref.73 Ref.82 Defects in LMNA are the cause of familial partial lipodystrophy type 2 (FPLD2) [MIM:151660]; also known as familial partial lipodystrophy Dunnigan type. 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. Ref.41 Ref.45 Ref.47 Ref.51 Ref.57 Ref.60 Ref.65 Ref.85 Defects in LMNA are the cause of limb-girdle muscular dystrophy type 1B (LGMD1B) [MIM:159001]. LGMD1B is an autosomal dominant degenerative myopathy with age-related atrioventricular cardiac conduction disturbances, dilated cardiomyopathy, and the absence of early contractures. LGMD1B is characterized by slowly progressive skeletal muscle weakness of the hip and shoulder girdles. Muscle biopsy shows mild dystrophic changes. Ref.46 Ref.52 Ref.59 Ref.62 Ref.81 Ref.87 Defects in LMNA are the cause of Charcot-Marie-Tooth disease type 2B1 (CMT2B1) [MIM:605588]. CMT2B1 is a form of Charcot-Marie-Tooth disease, the most common inherited disorder of the peripheral nervous system. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathy or CMT1, and primary peripheral axonal neuropathy or CMT2. Neuropathies of the CMT2 group are characterized by signs of axonal regeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. CMT2B1 inheritance is autosomal recessive. Ref.54 Defects in LMNA are the cause of Hutchinson-Gilford progeria syndrome (HGPS) [MIM:176670]. HGPS is a rare genetic disorder characterized by features reminiscent of marked premature aging. Note=HGPS is caused by the toxic accumulation of a mutant form of lamin-A/C. This mutant protein, called progerin, acts to deregulate mitosis and DNA damage signaling, leading to premature cell death and senescence. 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.32 Ref.66 Ref.69 Ref.70 Ref.76 Ref.78 Defects in LMNA are the cause of 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. Defects in LMNA are the cause of mandibuloacral dysplasia with type A lipodystrophy (MADA) [MIM:248370]. A disorder characterized by mandibular and clavicular hypoplasia, acroosteolysis, delayed closure of the cranial suture, progeroide 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. Ref.56 Ref.80 Ref.83 Defects in LMNA are a cause of lethal tight skin contracture syndrome (LTSCS) [MIM:275210]; also known as restrictive dermopathy (RD). Lethal tight skin contracture syndrome is a 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. Ref.74 Defects in LMNA are the cause of 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. Defects in LMNA are the cause of muscular dystrophy congenital LMNA-related (MDCL) [MIM:613205]. It is 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. Ref.88
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 component	Intermediate filament Nucleus
Coding sequence diversity	Alternative splicing
Disease	Cardiomyopathy Charcot-Marie-Tooth disease Congenital muscular dystrophy Disease mutation Emery-Dreifuss muscular dystrophy Limb-girdle muscular dystrophy Neuropathy
Domain	Coiled coil
PTM	Acetylation Isopeptide bond Lipoprotein Methylation Phosphoprotein Prenylation Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cellular component disassembly involved in apoptosis Traceable author statement. Source: Reactome cellular response to hypoxia Inferred from expression pattern. Source: UniProtKB establishment or maintenance of microtubule cytoskeleton polarity Inferred from sequence or structural similarity. Source: BHF-UCL muscle organ development Inferred from mutant phenotype Ref.39. Source: UniProtKB positive regulation of cell aging Inferred from direct assay Ref.31. Source: UniProtKB regulation of apoptotic process Inferred from sequence or structural similarity. Source: BHF-UCL regulation of cell migration Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular component	cytoplasm Inferred from direct assay. Source: HPA lamin filament Traceable author statement Ref.39. Source: UniProtKB nuclear envelope Inferred from direct assay Ref.23. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome perinuclear region of cytoplasm Inferred from direct assay Ref.39. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction Ref.28Ref.32Ref.35. Source: UniProtKB structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ALOX12	P18054	4	EBI-351935,EBI-1633210

Alternative products

This entry describes 3 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 661

661

Prelamin-A/C

PRO_0000398835

Chain

1 – 646

646

Lamin-A/C

PRO_0000063810

Propeptide

647 – 661

15

Removed in Lamin-A/C form

PRO_0000398836

Propeptide

662 – 664

3

Removed in Prelamin-A/C form and in Lamin-A/C form

PRO_0000403442

Regions

Region

1 – 130

130

Interaction with MLIP

Region

1 – 33

33

Head

Region

34 – 383

350

Rod

Region

34 – 70

37

Coil 1A

Region

71 – 80

10

Linker 1

Region

81 – 218

138

Coil 1B

Region

219 – 242

24

Linker 2

Region

243 – 383

141

Coil 2

Region

384 – 664

281

Tail

Motif

417 – 422

6

Nuclear localization signal Potential

Sites

Site

266

1

Heptad change of phase

Site

325

1

Stutter By similarity

Site

330

1

Heptad change of phase

Site

646 – 647

2

Cleavage; by endoprotease

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.27

Modified residue

10

1

Phosphothreonine Ref.15

Modified residue

12

1

Phosphoserine Ref.26

Modified residue

18

1

Phosphoserine Ref.26

Modified residue

19

1

Phosphothreonine Ref.15 Ref.17 Ref.19 Ref.26 Ref.27

Modified residue

22

1

Phosphoserine Ref.6 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.24 Ref.25 Ref.26 Ref.27

Modified residue

24

1

Phosphothreonine Ref.27

Modified residue

97

1

N6-acetyllysine Ref.29

Modified residue

108

1

N6-acetyllysine Ref.29

Modified residue

114

1

N6-acetyllysine Ref.29

Modified residue

270

1

N6-acetyllysine Ref.29

Modified residue

277

1

Phosphoserine Ref.15

Modified residue

301

1

Phosphoserine Ref.26

Modified residue

311

1

N6-acetyllysine Ref.29

Modified residue

390

1

Phosphoserine Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.24 Ref.25 Ref.26

Modified residue

392

1

Phosphoserine Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.24 Ref.25 Ref.26

Modified residue

394

1

Phosphothreonine Ref.26

Modified residue

395

1

Phosphoserine Ref.17 Ref.19 Ref.21 Ref.22 Ref.26

Modified residue

398

1

Phosphoserine Ref.26

Modified residue

403

1

Phosphoserine Ref.19

Modified residue

404

1

Phosphoserine Ref.19 Ref.27

Modified residue

406

1

Phosphoserine Ref.14 Ref.27

Modified residue

407

1

Phosphoserine Ref.14

Modified residue

409

1

Phosphothreonine Ref.14

Modified residue

414

1

Phosphoserine Ref.19

Modified residue

416

1

Phosphothreonine Ref.19

Modified residue

417

1

N6-acetyllysine Ref.16

Modified residue

423

1

Phosphoserine Ref.14

Modified residue

424

1

Phosphothreonine Ref.15

Modified residue

450

1

N6-acetyllysine Ref.29

Modified residue

458

1

Phosphoserine Ref.26

Modified residue

496

1

Phosphothreonine By similarity

Modified residue

505

1

Phosphothreonine By similarity

Modified residue

507

1

Phosphoserine By similarity

Modified residue

510

1

Phosphothreonine By similarity

Modified residue

571

1

Phosphoserine By similarity

Modified residue

573

1

Phosphoserine By similarity

Modified residue

628

1

Phosphoserine Ref.17 Ref.19 Ref.24 Ref.26

Modified residue

632

1

Phosphoserine Ref.17 Ref.19 Ref.25 Ref.26

Modified residue

636

1

Phosphoserine Ref.17 Ref.26

Modified residue

652

1

Phosphoserine Ref.13 Ref.25 Ref.26

Modified residue

661

1

Cysteine methyl ester Ref.8 Ref.9

Lipidation

661

1

S-farnesyl cysteine Ref.8 Ref.9

Cross-link

201

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.23

Natural variations

Alternative sequence

537 – 566

30

Missing in isoform ADelta10.

VSP_002468

Alternative sequence

567 – 572

6

GSHCSS → VSGSRR in isoform C.

VSP_002469

Alternative sequence

573 – 664

92

Missing in isoform C.

VSP_002470

Natural variant

10

1

T → I in an atypical progeroid patient; diagnosed as Seip syndrome. Ref.75
Corresponds to variant rs57077886 [ dbSNP | Ensembl ].

VAR_039745

Natural variant

25

1

R → G in EDMD2. Ref.68
Corresponds to variant rs58327533 [ dbSNP | Ensembl ].

VAR_039746

Natural variant

25

1

R → P in EDMD2; mis-localized in the nucleus; causes nuclear deformations and LMNB1 redistribution. Ref.49 Ref.90
Corresponds to variant rs61578124 [ dbSNP | Ensembl ].

VAR_039747

Natural variant

28

1

R → W in FPLD2. Ref.57
Corresponds to variant rs59914820 [ dbSNP | Ensembl ].

VAR_039748

Natural variant

32

1

Missing in EDMD2.

VAR_039749

Natural variant

33

1

E → D in CMT2; autosomal dominant form. Ref.77
Corresponds to variant rs57966821 [ dbSNP | Ensembl ].

VAR_039750

Natural variant

33

1

E → G in EDMD2. Ref.77

VAR_039751

Natural variant

35

1

L → V in EDMD2. Ref.68
Corresponds to variant rs56694480 [ dbSNP | Ensembl ].

VAR_039752

Natural variant

39

1

N → S in MDCL and EDMD2. Ref.88 Ref.90

VAR_063588

Natural variant

43

1

A → T in EDMD2. Ref.49
Corresponds to variant rs60446065 [ dbSNP | Ensembl ].

VAR_039753

Natural variant

45

1

Y → C in EDMD2. Ref.44 Ref.90
Corresponds to variant rs58436778 [ dbSNP | Ensembl ].

VAR_009971

Natural variant

50

1

R → P in EDMD2 and MDCL. Ref.44 Ref.88
Corresponds to variant rs60695352 [ dbSNP | Ensembl ].

VAR_009972

Natural variant

50

1

R → S in EDMD2. Ref.49
Corresponds to variant rs59931416 [ dbSNP | Ensembl ].

VAR_039754

Natural variant

57

1

A → P in CMDHH; phenotype originally designated as atypical Werner syndrome. Ref.69
Corresponds to variant rs28928903 [ dbSNP | Ensembl ].

VAR_017656

Natural variant

59

1

L → R in CMDHH. Ref.84 Ref.89

VAR_064055

Natural variant

60

1

R → 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.40 Ref.51 Ref.60
Corresponds to variant rs28928900 [ dbSNP | Ensembl ].

VAR_034706

Natural variant

62

1

R → G in FPLD2. Ref.57
Corresponds to variant rs56793579 [ dbSNP | Ensembl ].

VAR_039755

Natural variant

63

1

I → N in EDMD2. Ref.71 Ref.81

VAR_039756

Natural variant

63

1

I → S in EDMD2. Ref.44
Corresponds to variant rs57793737 [ dbSNP | Ensembl ].

VAR_009974

Natural variant

65

1

E → G in EDMD2. Ref.68

VAR_039757

Natural variant

85

1

L → R in CMD1A; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. Ref.40 Ref.51
Corresponds to variant rs28933090 [ dbSNP | Ensembl ].

VAR_009975

Natural variant

89

1

R → L in CMD1A. Ref.63
Corresponds to variant rs59040894 [ dbSNP | Ensembl ].

VAR_039758

Natural variant

97

1

K → E in CMD1A. Ref.58
Corresponds to variant rs59065411 [ dbSNP | Ensembl ].

VAR_039759

Natural variant

112

1

Missing in EDMD2.

VAR_009976

Natural variant

133

1

R → L in FPLD2. Ref.65

VAR_016913

Natural variant

133

1

R → P in EDMD2. Ref.49
Corresponds to variant rs60864230 [ dbSNP | Ensembl ].

VAR_017657

Natural variant

140

1

L → P in EDMD2. Ref.71 Ref.81

VAR_039760

Natural variant

140

1

L → R in HGPS; phenotype originally designated as atypical Werner syndrome. Ref.69
Corresponds to variant rs60652225 [ dbSNP | Ensembl ].

VAR_017658

Natural variant

143

1

S → F in HGPS. Ref.78
Corresponds to variant rs58912633 [ dbSNP | Ensembl ].

VAR_034707

Natural variant

143

1

S → P in CMD1A. Ref.73
Corresponds to variant rs61661343 [ dbSNP | Ensembl ].

VAR_039761

Natural variant

145

1

E → K in HGPS; atypical. Ref.70
Corresponds to variant rs60310264 [ dbSNP | Ensembl ].

VAR_017659

Natural variant

150

1

T → P in EDMD2. Ref.48 Ref.90
Corresponds to variant rs58917027 [ dbSNP | Ensembl ].

VAR_039762

Natural variant

161

1

E → K in CMD1A. Ref.67
Corresponds to variant rs28933093 [ dbSNP | Ensembl ].

VAR_017660

Natural variant

189

1

R → P in EDMD2; found also in a patient with limb-girdle muscular dystrophy; sporadic. Ref.90

VAR_064962

Natural variant

190

1

R → Q in EDMD2. Ref.81

VAR_039763

Natural variant

190

1

R → RR in EDMD2. Ref.90

VAR_064963

Natural variant

190

1

R → W in CMD1A. Ref.58 Ref.72 Ref.82
Corresponds to variant rs59026483 [ dbSNP | Ensembl ].

VAR_039764

Natural variant

192

1

D → G in CMD1A; dramatically increases the size of intranuclear speckles and reduced 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.82
Corresponds to variant rs57045855 [ dbSNP | Ensembl ].

VAR_039765

Natural variant

195

1

N → K in CMD1A; has a 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.40 Ref.51
Corresponds to variant rs28933091 [ dbSNP | Ensembl ].

VAR_009977

Natural variant

196 – 199

4

RLQT → S in EDMD2.

VAR_039766

Natural variant

203

1

E → 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.23 Ref.40 Ref.51
Corresponds to variant rs28933092 [ dbSNP | Ensembl ].

VAR_009978

Natural variant

203

1

E → K in CMD1A; Decreased sumoylation; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; associated with increased cell death. Ref.23 Ref.50
Corresponds to variant rs61195471 [ dbSNP | Ensembl ].

VAR_039767

Natural variant

206

1

F → L in EDMD2. Ref.90

VAR_064964

Natural variant

208

1

Missing in LGMD1B.

VAR_034708

Natural variant

215

1

L → P in CMD1A. Ref.53

VAR_039768

Natural variant

222

1

H → P in EDMD2. Ref.44

VAR_039769

Natural variant

222

1

H → Y in EDMD2. Ref.43
Corresponds to variant rs28928901 [ dbSNP | Ensembl ].

VAR_009979

Natural variant

230

1

D → N in FPLD2. Ref.85

VAR_039770

Natural variant

232

1

G → E in EDMD2. Ref.44

VAR_039771

Natural variant

248

1

L → P in EDMD2. Ref.68

VAR_039772

Natural variant

249

1

R → Q in EDMD2. Ref.43 Ref.44 Ref.49 Ref.59 Ref.68 Ref.71 Ref.81 Ref.90

VAR_009980

Natural variant

249

1

R → W in MDCL and EDMD2; mis-localized in the nucleus; causes nuclear deformations and LMNB1 redistribution. Ref.88 Ref.90

VAR_063589

Natural variant

260

1

K → N in CMDA1. Ref.79

VAR_039773

Natural variant

261

1

Missing in EDMD2.

VAR_009981

Natural variant

267

1

Y → C in EDMD2. Ref.68

VAR_039774

Natural variant

268

1

S → P in EDMD2. Ref.90

VAR_064965

Natural variant

271

1

L → P in EDMD2. Ref.90

VAR_064966

Natural variant

294

1

Q → P in EDMD2. Ref.44 Ref.90

VAR_009982

Natural variant

295

1

S → P in EDMD2. Ref.90

VAR_064967

Natural variant

298

1

R → C in CMT2B1. Ref.54

VAR_017661

Natural variant

302

1

L → P in MDCL. Ref.88

VAR_063590

Natural variant

303

1

S → P in EDMD2. Ref.90

VAR_064968

Natural variant

317

1

E → K in CMD1A. Ref.58

VAR_039775

Natural variant

336

1

R → Q in EDMD2. Ref.43

VAR_009983

Natural variant

343

1

R → Q in EDMD2.

VAR_009984

Natural variant

349

1

R → L in CMD1A. Ref.72

VAR_039776

Natural variant

355

1

Missing in EDMD2.

VAR_064969

Natural variant

358

1

E → 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.44 Ref.49 Ref.51 Ref.88 Ref.90

VAR_009985

Natural variant

361

1

E → K in EDMD2. Ref.90

VAR_064970

Natural variant

371

1

M → K in EDMD2; has a 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.51

VAR_009986

Natural variant

377

1

R → H in LGMD1B. Ref.46 Ref.62 Ref.63 Ref.81 Ref.87

VAR_016205

Natural variant

377

1

R → L in EDMD2 and LGMD1B. Ref.59 Ref.71

VAR_039777

Natural variant

380

1

L → S in MDCL. Ref.88

VAR_063591

Natural variant

386

1

R → K in EDMD2; has a 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.51 Ref.71 Ref.90

VAR_009987

Natural variant

399

1

R → C in FPLD2. Ref.85

VAR_039778

Natural variant

435

1

R → C in CMD1A. Ref.68

VAR_039779

Natural variant

446

1

D → V in EDMD2. Ref.68

VAR_039780

Natural variant

449

1

G → D in EDMD2. Ref.90

VAR_064971

Natural variant

453

1

R → P in MDCL. Ref.88

VAR_063592

Natural variant

453

1

R → W in EDMD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. Ref.39 Ref.43 Ref.44 Ref.49 Ref.51 Ref.68 Ref.90

VAR_009988

Natural variant

454

1

L → P in EDMD2. Ref.90

VAR_064972

Natural variant

455

1

R → P in MDCL. Ref.88

VAR_063593

Natural variant

456

1

N → D in MDCL. Ref.88

VAR_063594

Natural variant

456

1

N → I in EDMD2; mis-localized in the nucleus; does not alter nuclear size or shape. Ref.49 Ref.90

VAR_039781

Natural variant

456

1

N → K in EDMD2. Ref.44

VAR_039782

Natural variant

461

1

D → Y in EDMD2. Ref.90

VAR_064973

Natural variant

465

1

G → D in FPLD2. Ref.41

VAR_009989

Natural variant

467

1

W → R in EDMD2. Ref.90

VAR_064974

Natural variant

469

1

I → T in EDMD2. Ref.43

VAR_009990

Natural variant

471

1

R → C in HGPS. Ref.66
Corresponds to variant rs28928902 [ dbSNP | Ensembl ].

VAR_017662

Natural variant

481

1

Y → H in LGMD1B. Ref.52

VAR_039783

Natural variant

482

1

R → L in FPLD2. Ref.47

VAR_009991

Natural variant

482

1

R → Q in FPLD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. Ref.41 Ref.45 Ref.51
Corresponds to variant rs11575937 [ dbSNP | Ensembl ].

VAR_009992

Natural variant

482

1

R → W in FPLD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. Ref.41 Ref.47 Ref.51

VAR_009993

Natural variant

486

1

K → N in FPLD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. Ref.51

VAR_009994

Natural variant

520

1

W → S in EDMD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. Ref.44 Ref.51

VAR_039784

Natural variant

527

1

R → C in HGPS. Ref.66

VAR_017663

Natural variant

527

1

R → H in MADA. Ref.56

VAR_018727

Natural variant

527

1

R → 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.32 Ref.39 Ref.43 Ref.44 Ref.49 Ref.51 Ref.60 Ref.71 Ref.81 Ref.90

VAR_009995

Natural variant

528

1

T → K in EDMD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. Ref.43 Ref.44 Ref.51 Ref.90

VAR_009996

Natural variant

528

1

T → R in EDMD2. Ref.68 Ref.90

VAR_039785

Natural variant

529

1

A → V in MADA. Ref.80

VAR_034709

Natural variant

530

1

L → 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.32 Ref.39 Ref.51

VAR_009997

Natural variant

541

1

R → C in apical left ventricular aneurysm. Ref.61

VAR_039786

Natural variant

541

1

R → H in EDMD2. Ref.68

VAR_039787

Natural variant

541

1

R → P in EDMD2; mis-localized in the nucleus; does not alter nuclear size or shape. Ref.90

VAR_064975

Natural variant

541

1

R → S in EDMD2 and CMD1A; the phenotype is entirely reversed by coexpression of the S-541 mutation and wild-type lamin-C. Ref.82 Ref.90

VAR_039788

Natural variant

542

1

K → N in HGPS. Ref.76

VAR_034710

Natural variant

573

1

S → L in CMD1A, FPLD2 and MADA. Ref.63 Ref.83 Ref.85

VAR_039789

Natural variant

578

1

E → V in an atypical progeroid patient; diagnosed as Werner syndrome. Ref.75

VAR_039790

Natural variant

582

1

R → H in FPLD2. Ref.41

VAR_009998

Natural variant

602

1

G → S in EDMD2. Ref.90

VAR_064976

Natural variant

608

1

G → S in HGPS; reduced binding to SUN1. Ref.32 Ref.66 Ref.70

VAR_017664

Natural variant

624

1

R → H in EDMD2. Ref.49

VAR_039791

Natural variant

644

1

R → C in an atypical progeroid patient; diagnosed as Hutchinson-Gilford progeria syndrome. Ref.75 Ref.90

VAR_039792

Experimental info

Mutagenesis

201

1

K → L: Decreased sumoylation; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; associated with increased cell death. Ref.23

Mutagenesis

661

1

C → S: Loss of interaction with NARF. Ref.11

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

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.

.

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664

Helix Strand Turn

Details...

Helix

316 – 384

69

Beta strand

430 – 434

5

Beta strand

438 – 445

8

Beta strand

449 – 456

8

Beta strand

458 – 460

3

Beta strand

468 – 473

6

Beta strand

479 – 482

4

Beta strand

494 – 499

6

Turn

508 – 510

3

Beta strand

511 – 514

4

Beta strand

526 – 531

6

Beta strand

537 – 543

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform A (Lamin A) [UniParc]. Last modified March 20, 1987. Version 1. Checksum: E0855F7699F0318B	FASTA	664	74,139
	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
	Isoform C (Lamin C) [UniParc]. Checksum: CFF0FE0F230FCDE2	FASTA	572	65,135
	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 RKLVRSVTVV EDDEDEDGDD LLHHHHVSGS RR
	Isoform ADelta10 (Lamin ADelta10) [UniParc]. Checksum: 4ED0A48922D0A9F7	FASTA	634	70,661
	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 INSTGEGSHC 550 560 570 580 590 600 SSSGDPAEYN LRSRTVLCGT CGQPADKASA SGSGAQVGGP ISSGSSASSV TVTRSYRSVG 610 620 630 GSGGGSFGDN LVTRSYLLGN SSPRTQSPQN CSIM

References

	« Hide 'large scale' referencesShow '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: 3453101] [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: 3462705] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND C), PROTEIN SEQUENCE OF 583-644.
[3]	"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. , 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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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. , 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].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND C). Tissue: Kidney, Lung and Skin.
[6]	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, MASS SPECTROMETRY. Tissue: Ovarian carcinoma.
[7]	"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: 8621584] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 375-664 (ISOFORM ADELTA10). Tissue: Colon.
[8]	"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: 8175923] [Abstract] Cited for: PROTEOLYTIC CLEAVAGE, ISOPRENYLATION AT CYS-661, METHYLATION AT CYS-661.
[9]	"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: 9030603] [Abstract] Cited for: PROTEOLYTIC CLEAVAGE, ISOPRENYLATION AT CYS-661, METHYLATION AT CYS-661.
[10]	"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: 10508479] [Abstract] Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN. Tissue: Renal cell carcinoma.
[11]	"Prenylated prelamin A interacts with Narf, a novel nuclear protein." Barton R.M., Worman H.J. J. Biol. Chem. 274:30008-30018(1999) [PubMed: 10514485] [Abstract] Cited for: INTERACTION WITH NARF, MUTAGENESIS OF CYS-661.
[12]	"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: 12475961] [Abstract] Cited for: INTERACTION WITH TMPO-ALPHA AND RB1.
[13]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390; SER-392 AND SER-652, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390; SER-392; SER-406; SER-407; THR-409 AND SER-423, MASS SPECTROMETRY. Tissue: Colon adenocarcinoma.
[15]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-10; THR-19; SER-22; SER-277; SER-390; SER-392 AND THR-424, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-417, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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: 16964243] [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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-390 AND SER-392, MASS SPECTROMETRY. Tissue: Cervix adenocarcinoma.
[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: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-22; SER-390; SER-392; SER-395; SER-403; SER-404; SER-414; THR-416; SER-628 AND SER-632, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[21]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-390; SER-392 AND SER-395, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-390; SER-392 AND SER-395, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"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: 18606848] [Abstract] Cited for: SUBCELLULAR LOCATION, SUMOYLATION AT LYS-201, MUTAGENESIS OF LYS-201, CHARACTERIZATION OF VARIANTS CMD1A GLY-203 AND LYS-203.
[24]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-390; SER-392 AND SER-628, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[25]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-390; SER-392; SER-632 AND SER-652, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[26]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-18; THR-19; SER-22; SER-301; SER-390; SER-392; THR-394; SER-395; SER-398; SER-458; SER-628; SER-632; SER-636 AND SER-652, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[27]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-22; THR-24; SER-404 AND SER-406, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[28]	"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: 19323649] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH EMD.
[29]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-97; LYS-108; LYS-114; LYS-270; LYS-311 AND LYS-450, MASS SPECTROMETRY.
[30]	"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: 20079404] [Abstract] Cited for: FUNCTION.
[31]	"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: 20458013] [Abstract] Cited for: FUNCTION, PROTEOLYTIC PROCESSING, TISSUE SPECIFICITY.
[32]	"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: 19933576] [Abstract] Cited for: INTERACTION WITH SUN1, CHARACTERIZATION OF VARIANTS EDMD2 PRO-527 AND PRO-530, CHARACTERIZATION OF VARIANT HGPS SER-608.
[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: 21269460] [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: 21498514] [Abstract] Cited for: INTERACTION WITH MLIP.
[35]	"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: 21949239] [Abstract] Cited for: INTERACTION WITH DMPK.
[36]	"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: 11901143] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 435-552.
[37]	"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: 12057196] [Abstract] Cited for: STRUCTURE BY NMR OF 428-549.
[38]	"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: 15476822] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 305-387.
[39]	"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: 10080180] [Abstract] Cited for: VARIANTS EDMD2 TRP-453; PRO-527 AND PRO-530.
[40]	"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: 10580070] [Abstract] Cited for: VARIANTS CMD1A GLY-60; ARG-85; LYS-195 AND GLY-203.
[41]	"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: 10739751] [Abstract] Cited for: VARIANTS FPLD2 ASP-465; GLN-482; TRP-482 AND HIS-582.
[42]	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)
[43]	"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: 10739764] [Abstract] Cited for: VARIANTS EDMD2 TYR-222; GLN-249; GLN-336; TRP-453; THR-469; PRO-527 AND LYS-528.
[44]	"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. , Lacombe D., Bushby K., Pollitt C., Toniolo D., Fardeau M., Schwartz K., Muntoni F. Ann. Neurol. 48:170-180(2000) [PubMed: 10939567] [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.
[45]	"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: 10587585] [Abstract] Cited for: VARIANT FPLD2 GLN-482.
[46]	"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: 10814726] [Abstract] Cited for: VARIANTS LGMD1B LYS-208 DEL AND HIS-377.
[47]	"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: 10655060] [Abstract] Cited for: VARIANTS FPLD2 LEU-482 AND TRP-482.
[48]	"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: 10908904] [Abstract] Cited for: VARIANTS EDMD2 PRO-150 AND LYS-261 DEL.
[49]	"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: 11503164] [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.
[50]	"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: 11561226] [Abstract] Cited for: VARIANT CMD1A LYS-203.
[51]	"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: 11792809] [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.
[52]	"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: 11525883] [Abstract] Cited for: VARIANT LGMD1B HIS-481.
[53]	"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: 12486434] [Abstract] Cited for: VARIANT CMD1A PRO-215.
[54]	"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: 11799477] [Abstract] Cited for: VARIANT CMT2B1 CYS-298.
[55]	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)
[56]	"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: 12075506] [Abstract] Cited for: VARIANT MADA HIS-527.
[57]	"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: 12015247] [Abstract] Cited for: VARIANTS FPLD2 TRP-28 AND GLY-62.
[58]	"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: 11897440] [Abstract] Cited for: VARIANTS CMD1A GLU-97; TRP-190 AND LYS-317.
[59]	"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: 12032588] [Abstract] Cited for: VARIANT EDMD2 GLN-249, VARIANT LGMD1B LEU-377.
[60]	"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: 12196663] [Abstract] Cited for: VARIANTS FPLD2 GLY-60 AND PRO-527.
[61]	"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: 14675861] [Abstract] Cited for: VARIANT APICAL LEFT VENTRICULAR ANEURYSM CYS-541.
[62]	"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: 12673789] [Abstract] Cited for: VARIANT LGMD1B HIS-377.
[63]	"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: 12628721] [Abstract] Cited for: VARIANTS CMD1A LEU-89; HIS-377 AND LEU-573.
[64]	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)
[65]	"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: 12629077] [Abstract] Cited for: VARIANT FPLD2 LEU-133.
[66]	"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: 12768443] [Abstract] Cited for: VARIANTS HGPS CYS-471; CYS-527 AND SER-608.
[67]	"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: 12920062] [Abstract] Cited for: VARIANT CMD1A LYS-161.
[68]	"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: 14684700] [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.
[69]	"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: 12927431] [Abstract] Cited for: VARIANT CMDHH PRO-57, VARIANT HGPS ARG-140.
[70]	"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: 12714972] [Abstract] Cited for: VARIANTS HGPS LYS-145 AND SER-608.
[71]	"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: 12649505] [Abstract] Cited for: VARIANTS EDMD2 ASN-63; PRO-140; GLN-249; LEU-377; LYS-386 AND PRO-527.
[72]	"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: 15219508] [Abstract] Cited for: VARIANTS CMD1A TRP-190 AND LEU-349.
[73]	"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: 15140538] [Abstract] Cited for: VARIANT CMD1A PRO-143.
[74]	"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: 15317753] [Abstract] Cited for: INVOLVEMENT IN LTSCS.
[75]	"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: 15060110] [Abstract] Cited for: VARIANTS ILE-10; VAL-578 AND CYS-644.
[76]	"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: 15286156] [Abstract] Cited for: VARIANT HGPS ASN-542.
[77]	"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: 14985400] [Abstract] Cited for: VARIANT CMT2 ASP-33, VARIANT EDMD2 GLY-33.
[78]	"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: 15622532] [Abstract] Cited for: VARIANT HGPS PHE-143.
[79]	"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: 16156025] [Abstract] Cited for: VARIANT CMDA1 ASN-260.
[80]	"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: 15998779] [Abstract] Cited for: VARIANT MADA VAL-529.
[81]	"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: 15744034] [Abstract] Cited for: VARIANT LGMD1B HIS-377, VARIANTS EDMD2 ASN-63; PRO-140; GLN-190; GLN-249 AND PRO-527.
[82]	"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: 16061563] [Abstract] Cited for: VARIANTS CMD1A TRP-190; GLY-192 AND SER-541, CHARACTERIZATION OF VARIANTS CMD1A GLY-192 AND SER-541.
[83]	"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: 16278265] [Abstract] Cited for: VARIANT MADA LEU-573.
[84]	"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: 17150192] [Abstract] Cited for: VARIANT CMDHH ARG-59.
[85]	"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: 17250669] [Abstract] Cited for: VARIANTS FPLD2 ASN-230; CYS-399 AND LEU-573.
[86]	"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: 18611980] [Abstract] Cited for: INVOLVEMENT IN HHS-SLOVENIAN.
[87]	"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: 17136397] [Abstract] Cited for: VARIANT LGMD1B HIS-377.
[88]	"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. , Ryan M., Muntoni F., Guicheney P., Richard P., Bonne G., Estournet B. Ann. Neurol. 64:177-186(2008) [PubMed: 18551513] [Abstract] Cited for: VARIANTS MDCL SER-39; PRO-50; TRP-249; PRO-302; LYS-358; SER-380; PRO-453; PRO-455 AND ASP-456.
[89]	"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: 19283854] [Abstract] Cited for: VARIANT CMDHH ARG-59.
[90]	"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: 20848652] [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.
+	Additional computationally mapped references.

Web resources

Human Intermediate Filament Mutation Database

GeneReviews

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.
AL135927 Genomic DNA. Translation: CAI15521.1.
AL135927 Genomic DNA. Translation: CAI15522.1.
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.

IPI

IPI00021405.
IPI00216952.
IPI00216953.

PIR

VEHULA. A02961.
VEHULC. A02962.

RefSeq

NP_005563.1. NM_005572.3.
NP_733821.1. NM_170707.2.
NP_733822.1. NM_170708.2.

UniGene

Hs.594444.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IFR	X-ray	1.40	A	435-552	[»]
1IVT	NMR	-	A	428-549	[»]
1X8Y	X-ray	2.20	A	305-387	[»]
2XV5	X-ray	2.40	A/B	328-398	[»]
3GEF	X-ray	1.50	A/B/C/D	436-552	[»]

ProteinModelPortal

P02545.

SMR

P02545. Positions 313-386, 428-549.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-32948N.

IntAct

P02545. 24 interactions.

MINT

MINT-5003995.

STRING

P02545.

PTM databases

PhosphoSite

P02545.

Polymorphism databases

DMDM

125962.

2D gel databases

SWISS-2DPAGE

P02545.

REPRODUCTION-2DPAGE

IPI00021405.
IPI00216952.
P02545.

Proteomic databases

PeptideAtlas

P02545.

PRIDE

P02545.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000368300; ENSP00000357283; ENSG00000160789.

GeneID

4000.

KEGG

hsa:4000.

UCSC

uc001fnh.2. human.
uc001fni.2. human.

Organism-specific databases

CTD

4000.

GeneCards

GC01P156053.

HGNC

HGNC:6636. LMNA.

HPA

CAB004022.
HPA006660.

MIM

115200. phenotype.
150330. gene.
151660. phenotype.
159001. phenotype.
176670. phenotype.
181350. phenotype.
212112. phenotype.
248370. phenotype.
275210. phenotype.
605588. phenotype.
610140. phenotype.
613205. phenotype.

neXtProt

NX_P02545.

Orphanet

98853. Autosomal dominant Emery-Dreifuss muscular dystrophy.
264. Autosomal dominant limb-girdle muscular dystrophy type 1B.
98855. Autosomal recessive Emery-dreifuss muscular dystrophy.
157973. Congenital muscular dystrophy due to lamine A/C deficiency.
2229. Dilated cardiomyopathy - hypergonadotropic hypogonadism.
154. Familial isolated dilated cardiomyopathy.
2348. Familial partial lipodystrophy, Dunnigan 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.
90153. Mandibuloacral dysplasia with type A lipodystrophy.
83618. Severe dilated cardiomyopathy due to lamin A/C mutation.
902. Werner syndrome.

PharmGKB

PA231.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG13164.

HOGENOM

HBG716303.

HOVERGEN

HBG013015.

InParanoid

P02545.

OMA

HCSGSGD.

OrthoDB

EOG4S4PG2.

PhylomeDB

P02545.

Enzyme and pathway databases

Pathway_Interaction_DB

caspase_pathway. Caspase cascade in apoptosis.
faspathway. FAS signaling pathway (CD95).

Reactome

REACT_111183. Meiosis.
REACT_15380. Diabetes pathways.
REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

P02545.

Bgee

P02545.

CleanEx

HS_LMNA.

Genevestigator

P02545.

GermOnline

ENSG00000160789. Homo sapiens.

Family and domain databases

InterPro

IPR016044. F.
IPR001664. IF.
IPR001322. IF_tail_C.
IPR018039. Intermediate_filament_CS.
[Graphical view]

KO

K12641.

PANTHER

PTHR23239. IF. 1 hit.

Pfam

PF00038. Filament. 1 hit.
PF00932. IF_tail. 1 hit.
[Graphical view]

PROSITE

PS00226. IF. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

15692.

PMAP-CutDB

P02545.

SOURCE

Search...

Entry information

Entry name

LMNA_HUMAN

Accession

Primary (citable) accession number: P02545
Secondary accession number(s): D3DVB0 , P02546, Q5TCJ2, Q5TCJ3, Q969I8, Q96JA2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	March 20, 1987
Last modified:	January 25, 2012
This is version 168 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.