Reviewed, UniProtKB/Swiss-Prot P02545 (LMNA_HUMAN)

Names and origin

Protein names

Recommended name:
    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) [Complete proteome]

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 not processed.
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.
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 and TMEM43 By similarity. Proteolytically processed isoform A interacts with NARF.
Subcellular location	Nucleus.
Post-translational modification	Increased phosphorylation of the lamins occurs before envelope disintegration and probably plays a role in regulating lamin associations. The C-terminal 18 residues are removed by proteolytic cleavage in isoform A. Proteolytic cleavage requires prior farnesylation and absence of farnesylation blocks cleavage By similarity.
Involvement in disease	Defects in LMNA are a cause of Emery-Dreifuss muscular dystrophy type 2 (EDMD2) [MIM:181350]. EDMD2 is an autosomal dominant disorder characterized by slowly progressive muscle wasting and weakness, early contractures of the elbows Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects. Ref.26 Ref.36 Ref.55 Ref.68 Defects in LMNA are a cause of Emery-Dreifuss muscular dystrophy type 3 (EDMD3) [MIM:604929]. EDMD3 is an autosomal recessive disorder characterized by early contractures, muscle wasting and weakness and cardiomyopathy. 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.55 Ref.27 Ref.37 Ref.38 Ref.40 Ref.45 Ref.50 Ref.54 Ref.59 Ref.60 Ref.69 Defects in LMNA are a cause of generalized lipoatrophy associated with diabetes, hepatic steatosis, hypertrophic cardiomyopathy and leukomelanodermic papules (LDHCP) [MIM:608056]. LDHCP is a disorder characterized by acquired generalized lipoatrophy with metabolic alterations, massive liver steatosis, distinctive cutaneous manifestations, and cardiac abnormalities involving both endocardium and myocardium. Ref.52 Defects in LMNA are a cause of familial partial lipodystrophy type 2 (FPLD2) [MIM:151660]; also known as familial partial lipodystrophy Dunnigan type. FPLD2 is an autosomal dominant disorder characterized by marked loss of subcutaneous adipose tissue from the extremities and trunk but by excess fat deposition in the head and neck. Frequently associated with profound insulin resistance, dyslipidemia, and diabetes. Ref.38 Ref.28 Ref.32 Ref.44 Ref.47 Ref.71 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.68 Ref.33 Ref.39 Ref.46 Ref.49 Ref.73 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.41 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. Ref.53 Ref.57 Ref.63 Ref.65 Defects in LMNA are a cause of Werner syndrome (WRN) [MIM:277700]. WRN is an autosomal, recessively inherited, segmental progeroid syndrome, in which multiple aspects (or segments) of aging phenotypes seem to be entailed. The features of Werner syndrome are scleroderma-like skin changes, especially in the extremities, cataract, subcutaneous calcification, premature arteriosclerosis, diabetes mellitus, and a wizened and prematurely aged facies. Ref.56 Defects in LMNA are the cause of mandibuloacral dysplasia with type A lipodystrophy (MADA) [MIM:248370]. Mandibuloacral dysplasia (MAD) is a rare autosomal recessive disorder characterized by mandibular and clavicular hypoplasia, acroosteolysis, delayed closure of the cranial suture, joint contractures, and types A or B patterns of lipodystrophy. Type A lipodystrophy observed in MADA, is characterized by fat loss restricted to the extremities. Ref.43 Ref.67 Defects in LMNA are a cause of lethal tight skin contracture syndrome [MIM:275210]; also called 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. Defects in LMNA are a cause of tendinous calcinosis arthropathy and progeroid features (TCAPF) [MIM:611618]. This disorder consists of an autosomal recessive arthropathy syndrome affecting predominantly the distal femora and proximal tibia in the knees with tendinous calcifications, associated with progeroide appearance, such as pinched nose and micrognathia, cataract, alopecia, generalized lipodystrophy and sclerodermatous skin. Ref.70 Defects in LMNA are the cause of heart-hand syndrome Slovenian type [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.
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 Disease mutation Limb-girdle muscular dystrophy Neuropathy
Domain	Coiled coil
PTM	Acetylation Lipoprotein Phosphoprotein Prenylation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from direct assay. Source: HPA intermediate filament Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from direct assay. Source: MGI plasma membrane Inferred from direct assay. Source: HPA
Molecular function	protein binding Ref.8 Inferred from physical interaction. Source: UniProtKB structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ALOX12	P18054	3	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 – 664

664

Lamin-A/C

PRO_0000063810

Regions

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

Amino acid modifications

Modified residue

1

1

Blocked amino end (Met)

Modified residue

10

1

Phosphothreonine Ref.12

Modified residue

12

1

Phosphoserine Ref.21

Modified residue

18

1

Phosphoserine Ref.21

Modified residue

19

1

Phosphothreonine Ref.12 Ref.21 Ref.14 Ref.16

Modified residue

22

1

Phosphoserine Ref.12 Ref.21 Ref.14 Ref.16 Ref.5 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20

Modified residue

277

1

Phosphoserine Ref.12

Modified residue

301

1

Phosphoserine Ref.21

Modified residue

390

1

Phosphoserine Ref.12 Ref.21 Ref.14 Ref.16 Ref.15 Ref.18 Ref.19 Ref.20 Ref.10 Ref.11

Modified residue

392

1

Phosphoserine Ref.12 Ref.21 Ref.14 Ref.16 Ref.15 Ref.18 Ref.19 Ref.20 Ref.10 Ref.11

Modified residue

394

1

Phosphothreonine Ref.21

Modified residue

395

1

Phosphoserine Ref.21 Ref.14 Ref.16 Ref.18

Modified residue

398

1

Phosphoserine Ref.21

Modified residue

403

1

Phosphoserine Ref.16

Modified residue

404

1

Phosphoserine Ref.16

Modified residue

406

1

Phosphoserine Ref.11

Modified residue

407

1

Phosphoserine Ref.11

Modified residue

409

1

Phosphothreonine Ref.11

Modified residue

414

1

Phosphoserine Ref.16

Modified residue

416

1

Phosphothreonine Ref.16

Modified residue

417

1

N6-acetyllysine Ref.13

Modified residue

423

1

Phosphoserine Ref.11

Modified residue

424

1

Phosphothreonine Ref.12

Modified residue

458

1

Phosphoserine Ref.21

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

628

1

Phosphoserine Ref.21 Ref.14 Ref.16 Ref.19

Modified residue

632

1

Phosphoserine Ref.21 Ref.14 Ref.16 Ref.20

Modified residue

636

1

Phosphoserine Ref.21 Ref.14

Modified residue

652

1

Phosphoserine Ref.21 Ref.20 Ref.10

Lipidation

661

1

S-farnesyl cysteine By similarity

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.36 Ref.62

VAR_039745

Natural variant

25

1

R → G in EDMD2. Ref.36 Ref.55

VAR_039746

Natural variant

25

1

R → P in EDMD2. Ref.36 Ref.55

VAR_039747

Natural variant

28

1

R → W in FPLD2. Ref.44

VAR_039748

Natural variant

32

1

Missing in EDMD2. Ref.55

VAR_039749

Natural variant

33

1

E → D in CMT2; autosomal dominant form. Ref.64

VAR_039750

Natural variant

33

1

E → G in EDMD. Ref.64

VAR_039751

Natural variant

35

1

L → V in EDMD2. Ref.55

VAR_039752

Natural variant

43

1

A → T in EDMD2. Ref.36

VAR_039753

Natural variant

45

1

Y → C in EDMD. Ref.31

VAR_009971

Natural variant

50

1

R → P in EDMD. Ref.36 Ref.31

VAR_009972

Natural variant

50

1

R → S in EDMD2. Ref.36

VAR_039754

Natural variant

57

1

A → P in WRN; atypical. dbSNP rs28928903. Ref.56

VAR_017656

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. dbSNP rs28928900.

VAR_034706

Natural variant

62

1

R → G in FPLD2. Ref.44

VAR_039755

Natural variant

63

1

I → N in EDMD. Ref.68 Ref.31 Ref.58

VAR_039756

Natural variant

63

1

I → S in EDMD. Ref.68 Ref.31 Ref.58

VAR_009974

Natural variant

65

1

E → G in EDMD; unclassified muscular dystrophy. Ref.55

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. dbSNP rs28933090. Ref.27 Ref.38

VAR_009975

Natural variant

89

1

R → L in CMD1A. Ref.50

VAR_039758

Natural variant

97

1

K → E in CMD1A. Ref.45

VAR_039759

Natural variant

112

1

Missing in EDMD. Ref.55 Ref.31

VAR_009976

Natural variant

133

1

R → L in LDHCP. Ref.52

VAR_016913

Natural variant

133

1

R → P in EDMD2. Ref.36

VAR_017657

Natural variant

140

1

L → P in EDMD. Ref.36 Ref.68 Ref.58

VAR_039760

Natural variant

140

1

L → R in WRN. Ref.56

VAR_017658

Natural variant

143

1

S → F in HGPS. Ref.65

VAR_034707

Natural variant

143

1

S → P in CMD1A. Ref.60

VAR_039761

Natural variant

145

1

E → K in HGPS; atypical. Ref.57

VAR_017659

Natural variant

150

1

T → P in EDMD; autosomal dominant form. Ref.36 Ref.35

VAR_039762

Natural variant

161

1

E → K in CMD1A. Ref.54

VAR_017660

Natural variant

190

1

R → Q in EDMD2. Ref.36 Ref.68

VAR_039763

Natural variant

190

1

R → W in CMD1A. Ref.45 Ref.59 Ref.69

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.69

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.27 Ref.38

VAR_009977

Natural variant

196 – 199

4

RLQT → S in EDMD2. Ref.36

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. dbSNP rs28933092. Ref.27 Ref.37 Ref.38

VAR_009978

Natural variant

203

1

E → K in CMD1A. Ref.27 Ref.37 Ref.38

VAR_039767

Natural variant

208

1

Missing in LGMD1B. Ref.33

VAR_034708

Natural variant

215

1

L → P in CMD1A. Ref.40

VAR_039768

Natural variant

222

1

H → P in EDMD. Ref.31 Ref.30

VAR_039769

Natural variant

222

1

H → Y in EDMD. dbSNP rs28928901. Ref.31 Ref.30

VAR_009979

Natural variant

230

1

D → N in FPLD2. Ref.71

VAR_039770

Natural variant

232

1

G → E in EDMD. Ref.31

VAR_039771

Natural variant

248

1

L → P in EDMD2. Ref.55

VAR_039772

Natural variant

249

1

R → Q in EDMD. Ref.36 Ref.55 Ref.68 Ref.31 Ref.58 Ref.30

VAR_009980

Natural variant

260

1

K → N in CMDA1. Ref.66

VAR_039773

Natural variant

261

1

Missing in EDMD. Ref.36 Ref.31 Ref.35

VAR_009981

Natural variant

267

1

Y → C in EDMD2. Ref.55

VAR_039774

Natural variant

294

1

Q → P in EDMD. Ref.31

VAR_009982

Natural variant

298

1

R → C in CMT2B1. Ref.41

VAR_017661

Natural variant

317

1

E → K in CMD1A. Ref.45

VAR_039775

Natural variant

336

1

R → Q in EDMD. Ref.30

VAR_009983

Natural variant

343

1

R → Q in EDMD.

VAR_009984

Natural variant

349

1

R → L in CMD1A. Ref.59

VAR_039776

Natural variant

358

1

E → K in EDMD; 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; einteracts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. Ref.36 Ref.38 Ref.31

VAR_009985

Natural variant

371

1

M → K in EDMD; 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.38 Ref.31

VAR_009986

Natural variant

377

1

R → H in LGMD1B. Ref.68 Ref.33 Ref.46 Ref.49 Ref.73

VAR_016205

Natural variant

377

1

R → L in EDMD and LGMD1B.

VAR_039777

Natural variant

386

1

R → K in EDMD; 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.38 Ref.31 Ref.58

VAR_009987

Natural variant

399

1

R → C in FPLD2. Ref.71

VAR_039778

Natural variant

435

1

R → C in CMD1A. Ref.55

VAR_039779

Natural variant

446

1

D → V in EDMD2. Ref.55

VAR_039780

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.26 Ref.36 Ref.55

VAR_009988

Natural variant

456

1

N → I in EDMD2. Ref.36

VAR_039781

Natural variant

456

1

N → K in EDMD. Ref.36 Ref.31

VAR_039782

Natural variant

465

1

G → D in FPLD2. Ref.28

VAR_009989

Natural variant

469

1

I → T in EDMD. Ref.30

VAR_009990

Natural variant

471

1

R → C in HGPS. dbSNP rs28928902. Ref.53

VAR_017662

Natural variant

481

1

Y → H in LGMD1B. Ref.39

VAR_039783

Natural variant

482

1

R → L in FPLD2. Ref.38 Ref.28 Ref.32

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. dbSNP rs11575937. Ref.38 Ref.28 Ref.32

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.38 Ref.28 Ref.32

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.38

VAR_009994

Natural variant

520

1

W → S in EDMD; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. Ref.36 Ref.38 Ref.31

VAR_039784

Natural variant

527

1

R → C in HGPS. Ref.53

VAR_017663

Natural variant

527

1

R → H in MADA. Ref.43

VAR_018727

Natural variant

527

1

R → P in EDMD2 and FPLD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type.

VAR_009995

Natural variant

528

1

T → K in EDMD; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. Ref.55 Ref.38 Ref.31 Ref.30

VAR_009996

Natural variant

528

1

T → R in EDMD2. Ref.55

VAR_039785

Natural variant

529

1

A → V in MADA. Ref.67

VAR_034709

Natural variant

530

1

L → P in EDMD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. Ref.26 Ref.36

VAR_009997

Natural variant

541

1

R → C in apical left ventricular aneurysm. Ref.55 Ref.69 Ref.48

VAR_039786

Natural variant

541

1

R → H in EDMD2. Ref.55

VAR_039787

Natural variant

541

1

R → S in CMD1A; the phenotype is entirely reversed by coexpression of the S-541 mutation and wild-type lamin-C. Ref.69

VAR_039788

Natural variant

542

1

K → N in HGPS. Ref.63

VAR_034710

Natural variant

573

1

S → L in CMD1A, FPLD2 and tendinous calcinosis arthropathy and progeroid features.

VAR_039789

Natural variant

578

1

E → V in an atypical progeroid patient; diagnosed as Werner syndrome. Ref.62

VAR_039790

Natural variant

582

1

R → H in FPLD2. Ref.28

VAR_009998

Natural variant

608

1

G → S in HGPS. Ref.53 Ref.57

VAR_017664

Natural variant

624

1

R → H in EDMD2. Ref.36

VAR_039791

Natural variant

644

1

R → C in an atypical progeroid patient; diagnosed as Hutchinson-Gilford progeria syndrome. Ref.62

VAR_039792

Experimental info

Mutagenesis

661

1

C → S: Loss of interaction with NARF. Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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). 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). 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

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[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]	"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.
[5]	Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 12-25; 29-48; 51-60; 63-72; 79-90; 102-108; 123-166; 172-189; 197-216; 226-233; 241-260; 281-311; 320-329; 352-386; 440-453; 458-470; 472-482; 516-542; 585-624 AND 628-644, PHOSPHORYLATION AT SER-22, MASS SPECTROMETRY. Tissue: Ovarian carcinoma.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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: Epithelium.
[11]	"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.
[12]	"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: Epithelium.
[13]	"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: Epithelium.
[14]	"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: Epithelium.
[15]	"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: Epithelium.
[16]	"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: Epithelium.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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.
[27]	"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.
[28]	"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.
[29]	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)
[30]	"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 EDMD TYR-222; GLN-249; GLN-336; TRP-453; THR-469; PRO-527 AND LYS-528.
[31]	"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 EDMD 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.
[32]	"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.
[33]	"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.
[34]	"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 FPLD LEU-482 AND TRP-482.
[35]	"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 EDMD PRO-150 AND LYS-261 DEL.
[36]	"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.
[37]	"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.
[38]	"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 EDMD 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.
[39]	"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.
[40]	"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.
[41]	"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.
[42]	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)
[43]	"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.
[44]	"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.
[45]	"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.
[46]	"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 EDND2 GLN-249, VARIANT LGMD1B LEU-377.
[47]	"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.
[48]	"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.
[49]	"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.
[50]	"Natural history of dilated cardiomyopathy due to lamin A/C gene mutations." Familial dilatd 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.
[51]	Erratum Familial dilatd 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)
[52]	"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 LDHCP LEU-133.
[53]	"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.
[54]	"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.
[55]	"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; GLU-112 DEL; PRO-248; GLN-249; CYS-267; VAL-446; TRP-453; ARG-528 AND HIS-541, VARIANT EDMD GLY-65, VARIANT CMD1A CYS-435.
[56]	"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: VARIANTS WRN PRO-57 AND ARG-140.
[57]	"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.
[58]	"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 EDMD ASN-63; PRO-140; GLN-249; LEU-377; LYS-386 AND PRO-527.
[59]	"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.
[60]	"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.
[61]	"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 LETHAL TIGHT SKIN CONTRACTURE SYNDROME.
[62]	"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 ATYPICAL PROGEROID PATIENTS ILE-10; VAL-578 AND CYS-644.
[63]	"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.
[64]	"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 EDMD GLY-33.
[65]	"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.
[66]	"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.
[67]	"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.
[68]	"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.
[69]	"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.
[70]	"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 TCAPF LEU-573.
[71]	"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.
[72]	"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 HEART-HAND SYNDROME SLOVENIAN TYPE.
[73]	"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.
+	Additional computationally mapped references.

Web resources

Human Intermediate Filament Mutation Database

GeneReviews

Cross-references

Sequence databases

EMBLGenBankDDBJ

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: CAI15522.1.
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.
NP_733821.1.
NP_733822.1.

UniGene

Hs.594444

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P02545. 11 interactions.

PTM databases

PhosphoSite

P02545.

2-D gel databases

SWISS-2DPAGE

P02545.

REPRODUCTION-2DPAGE

IPI00021405.
IPI00216952.
P02545.

Proteomic databases

PeptideAtlas

P02545.

PRIDE

P02545.

Genome annotation databases

Ensembl

ENSG00000160789. Homo sapiens. [Contig view]

GeneID

4000.

KEGG

hsa:4000.

UCSC

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

Organism-specific databases

GeneCards

GC01P154318.

H-InvDB

HIX0001147.

HGNC

HGNC:6636. LMNA.

HPA

CAB004022.
HPA006660.

MIM

115200. phenotype.
150330. gene.
151660. phenotype.
159001. phenotype.
176670. phenotype.
181350. phenotype.
248370. phenotype.
275210. phenotype.
277700. phenotype.
604929. phenotype.
605588. phenotype.
608056. phenotype.
610140. phenotype.
611618. phenotype.

Orphanet

64746. Autosomal dominant Charcot-Marie-Tooth disease, type 2.
264. Autosomal dominant limb-girdle muscular dystrophy, type 1B.
91024. Autosomal recessive Charcot-Marie-Tooth disease, type 2.
153. Cardiomyopathy, dilated, with conduction defect.
154. Cardiomyopathy, familial dilated.
98856. Charcot-Marie-Tooth disease, type 2B1.
1662. Dermopathy restrictive, lethal.
2457. Dysplasia, mandibuloacral.
90153. Dysplasia, mandibuloacral with type A lipodystrophia.
261. Emery-Dreifuss muscular dystrophy.
168796. Heart-hand syndrome, Slovenian type.
98301. Laminopathy.
137871. Laminopathy, type Decaudain-Vigouroux.
2348. Lipodystrophy, familial partial, Dunnigan type.
740. Progeria.
83618. Severe dilated cardiomyopathy due to lamin A/C mutation.
902. Werner syndrome.

PharmGKB

PA231.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P02545.

HOVERGEN

P02545.

OMA

P02545. HCSGSGD.

Enzyme and pathway databases

Pathway_Interaction_DB

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

Reactome

REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

P02545.

Bgee

P02545.

CleanEx

HS_LMNA.

GermOnline

ENSG00000160789. Homo sapiens.

Family and domain databases

InterPro

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

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 Resources

NextBio

15692.

PMAP-CutDB

P02545.

SOURCE

Search...

Entry information

Entry name

LMNA_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	March 20, 1987
Last modified:	July 7, 2009
This is version 137 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)