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Reviewed, UniProtKB/Swiss-Prot P02545 (LMNA_HUMAN)

Last modified July 7, 2009. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

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

Protein attributes

Sequence length664 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. Lamin A and C are present in equal amounts in the lamina of mammals.

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ALOX12P180543EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 664664Lamin-A/C
PRO_0000063810

Regions

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

Sites

Site2661Heptad change of phase
Site3251Stutter By similarity
Site3301Heptad change of phase

Amino acid modifications

Modified residue11Blocked amino end (Met)
Modified residue101Phosphothreonine Ref.12
Modified residue121Phosphoserine Ref.21
Modified residue181Phosphoserine Ref.21
Modified residue191Phosphothreonine Ref.12 Ref.21 Ref.14 Ref.16
Modified residue221Phosphoserine Ref.12 Ref.21 Ref.14 Ref.16 Ref.5 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20
Modified residue2771Phosphoserine Ref.12
Modified residue3011Phosphoserine Ref.21
Modified residue3901Phosphoserine Ref.12 Ref.21 Ref.14 Ref.16 Ref.15 Ref.18 Ref.19 Ref.20 Ref.10 Ref.11
Modified residue3921Phosphoserine Ref.12 Ref.21 Ref.14 Ref.16 Ref.15 Ref.18 Ref.19 Ref.20 Ref.10 Ref.11
Modified residue3941Phosphothreonine Ref.21
Modified residue3951Phosphoserine Ref.21 Ref.14 Ref.16 Ref.18
Modified residue3981Phosphoserine Ref.21
Modified residue4031Phosphoserine Ref.16
Modified residue4041Phosphoserine Ref.16
Modified residue4061Phosphoserine Ref.11
Modified residue4071Phosphoserine Ref.11
Modified residue4091Phosphothreonine Ref.11
Modified residue4141Phosphoserine Ref.16
Modified residue4161Phosphothreonine Ref.16
Modified residue4171N6-acetyllysine Ref.13
Modified residue4231Phosphoserine Ref.11
Modified residue4241Phosphothreonine Ref.12
Modified residue4581Phosphoserine Ref.21
Modified residue4961Phosphothreonine By similarity
Modified residue5051Phosphothreonine By similarity
Modified residue5071Phosphoserine By similarity
Modified residue5101Phosphothreonine By similarity
Modified residue6281Phosphoserine Ref.21 Ref.14 Ref.16 Ref.19
Modified residue6321Phosphoserine Ref.21 Ref.14 Ref.16 Ref.20
Modified residue6361Phosphoserine Ref.21 Ref.14
Modified residue6521Phosphoserine Ref.21 Ref.20 Ref.10
Lipidation6611S-farnesyl cysteine By similarity

Natural variations

Alternative sequence537 – 56630Missing in isoform ADelta10.
VSP_002468
Alternative sequence567 – 5726GSHCSS → VSGSRR in isoform C.
VSP_002469
Alternative sequence573 – 66492Missing in isoform C.
VSP_002470
Natural variant101T → I in an atypical progeroid patient; diagnosed as Seip syndrome. Ref.36 Ref.62
VAR_039745
Natural variant251R → G in EDMD2. Ref.36 Ref.55
VAR_039746
Natural variant251R → P in EDMD2. Ref.36 Ref.55
VAR_039747
Natural variant281R → W in FPLD2. Ref.44
VAR_039748
Natural variant321Missing in EDMD2. Ref.55
VAR_039749
Natural variant331E → D in CMT2; autosomal dominant form. Ref.64
VAR_039750
Natural variant331E → G in EDMD. Ref.64
VAR_039751
Natural variant351L → V in EDMD2. Ref.55
VAR_039752
Natural variant431A → T in EDMD2. Ref.36
VAR_039753
Natural variant451Y → C in EDMD. Ref.31
VAR_009971
Natural variant501R → P in EDMD. Ref.36 Ref.31
VAR_009972
Natural variant501R → S in EDMD2. Ref.36
VAR_039754
Natural variant571A → P in WRN; atypical. dbSNP rs28928903. Ref.56
VAR_017656
Natural variant601R → G in CMD1A and FPLD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. dbSNP rs28928900.
VAR_034706
Natural variant621R → G in FPLD2. Ref.44
VAR_039755
Natural variant631I → N in EDMD. Ref.68 Ref.31 Ref.58
VAR_039756
Natural variant631I → S in EDMD. Ref.68 Ref.31 Ref.58
VAR_009974
Natural variant651E → G in EDMD; unclassified muscular dystrophy. Ref.55
VAR_039757
Natural variant851L → R in CMD1A; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. dbSNP rs28933090. Ref.27 Ref.38
VAR_009975
Natural variant891R → L in CMD1A. Ref.50
VAR_039758
Natural variant971K → E in CMD1A. Ref.45
VAR_039759
Natural variant1121Missing in EDMD. Ref.55 Ref.31
VAR_009976
Natural variant1331R → L in LDHCP. Ref.52
VAR_016913
Natural variant1331R → P in EDMD2. Ref.36
VAR_017657
Natural variant1401L → P in EDMD. Ref.36 Ref.68 Ref.58
VAR_039760
Natural variant1401L → R in WRN. Ref.56
VAR_017658
Natural variant1431S → F in HGPS. Ref.65
VAR_034707
Natural variant1431S → P in CMD1A. Ref.60
VAR_039761
Natural variant1451E → K in HGPS; atypical. Ref.57
VAR_017659
Natural variant1501T → P in EDMD; autosomal dominant form. Ref.36 Ref.35
VAR_039762
Natural variant1611E → K in CMD1A. Ref.54
VAR_017660
Natural variant1901R → Q in EDMD2. Ref.36 Ref.68
VAR_039763
Natural variant1901R → W in CMD1A. Ref.45 Ref.59 Ref.69
VAR_039764
Natural variant1921D → 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 variant1951N → 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 variant196 – 1994RLQT → S in EDMD2. Ref.36
VAR_039766
Natural variant2031E → G in CMD1A; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. dbSNP rs28933092. Ref.27 Ref.37 Ref.38
VAR_009978
Natural variant2031E → K in CMD1A. Ref.27 Ref.37 Ref.38
VAR_039767
Natural variant2081Missing in LGMD1B. Ref.33
VAR_034708
Natural variant2151L → P in CMD1A. Ref.40
VAR_039768
Natural variant2221H → P in EDMD. Ref.31 Ref.30
VAR_039769
Natural variant2221H → Y in EDMD. dbSNP rs28928901. Ref.31 Ref.30
VAR_009979
Natural variant2301D → N in FPLD2. Ref.71
VAR_039770
Natural variant2321G → E in EDMD. Ref.31
VAR_039771
Natural variant2481L → P in EDMD2. Ref.55
VAR_039772
Natural variant2491R → Q in EDMD. Ref.36 Ref.55 Ref.68 Ref.31 Ref.58 Ref.30
VAR_009980
Natural variant2601K → N in CMDA1. Ref.66
VAR_039773
Natural variant2611Missing in EDMD. Ref.36 Ref.31 Ref.35
VAR_009981
Natural variant2671Y → C in EDMD2. Ref.55
VAR_039774
Natural variant2941Q → P in EDMD. Ref.31
VAR_009982
Natural variant2981R → C in CMT2B1. Ref.41
VAR_017661
Natural variant3171E → K in CMD1A. Ref.45
VAR_039775
Natural variant3361R → Q in EDMD. Ref.30
VAR_009983
Natural variant3431R → Q in EDMD.
VAR_009984
Natural variant3491R → L in CMD1A. Ref.59
VAR_039776
Natural variant3581E → 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 variant3711M → 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 variant3771R → H in LGMD1B. Ref.68 Ref.33 Ref.46 Ref.49 Ref.73
VAR_016205
Natural variant3771R → L in EDMD and LGMD1B.
VAR_039777
Natural variant3861R → 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 variant3991R → C in FPLD2. Ref.71
VAR_039778
Natural variant4351R → C in CMD1A. Ref.55
VAR_039779
Natural variant4461D → V in EDMD2. Ref.55
VAR_039780
Natural variant4531R → W in EDMD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. Ref.26 Ref.36 Ref.55
VAR_009988
Natural variant4561N → I in EDMD2. Ref.36
VAR_039781
Natural variant4561N → K in EDMD. Ref.36 Ref.31
VAR_039782
Natural variant4651G → D in FPLD2. Ref.28
VAR_009989
Natural variant4691I → T in EDMD. Ref.30
VAR_009990
Natural variant4711R → C in HGPS. dbSNP rs28928902. Ref.53
VAR_017662
Natural variant4811Y → H in LGMD1B. Ref.39
VAR_039783
Natural variant4821R → L in FPLD2. Ref.38 Ref.28 Ref.32
VAR_009991
Natural variant4821R → Q in FPLD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. dbSNP rs11575937. Ref.38 Ref.28 Ref.32
VAR_009992
Natural variant4821R → W in FPLD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. Ref.38 Ref.28 Ref.32
VAR_009993
Natural variant4861K → N in FPLD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type. Ref.38
VAR_009994
Natural variant5201W → 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 variant5271R → C in HGPS. Ref.53
VAR_017663
Natural variant5271R → H in MADA. Ref.43
VAR_018727
Natural variant5271R → 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 variant5281T → 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 variant5281T → R in EDMD2. Ref.55
VAR_039785
Natural variant5291A → V in MADA. Ref.67
VAR_034709
Natural variant5301L → 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 variant5411R → C in apical left ventricular aneurysm. Ref.55 Ref.69 Ref.48
VAR_039786
Natural variant5411R → H in EDMD2. Ref.55
VAR_039787
Natural variant5411R → 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 variant5421K → N in HGPS. Ref.63
VAR_034710
Natural variant5731S → L in CMD1A, FPLD2 and tendinous calcinosis arthropathy and progeroid features.
VAR_039789
Natural variant5781E → V in an atypical progeroid patient; diagnosed as Werner syndrome. Ref.62
VAR_039790
Natural variant5821R → H in FPLD2. Ref.28
VAR_009998
Natural variant6081G → S in HGPS. Ref.53 Ref.57
VAR_017664
Natural variant6241R → H in EDMD2. Ref.36
VAR_039791
Natural variant6441R → C in an atypical progeroid patient; diagnosed as Hutchinson-Gilford progeria syndrome. Ref.62
VAR_039792

Experimental info

Mutagenesis6611C → S: Loss of interaction with NARF. Ref.8

Secondary structure

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

Details...

Sequences

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

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

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

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

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

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

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

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

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

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

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

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

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


CSIM 

« Hide

Isoform C (Lamin C).

Checksum: CFF0FE0F230FCDE2
Show »

FASTA57265,135
Isoform ADelta10 (Lamin ADelta10).

Checksum: 4ED0A48922D0A9F7
Show »

FASTA63470,661

References

« Hide 'large scale' references
[1]"Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins."
McKeon F.D., Kirschner M.W., Caput D.
Nature 319:463-468(1986) [PubMed: 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. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed: 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. expand/collapse author list , Lacombe D., Bushby K., Pollitt C., Toniolo D., Fardeau M., Schwartz K., Muntoni F.
Ann. Neurol. 48:170-180(2000) [PubMed: 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.

Cross-references

Sequence databases

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.
IPIIPI00021405.
IPI00216952.
IPI00216953.
PIRVEHULA. A02961.
VEHULC. A02962.
RefSeqNP_005563.1.
NP_733821.1.
NP_733822.1.
UniGeneHs.594444

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1IFRX-ray1.40A435-552[»]
1IVTNMR-A428-549[»]
1X8YX-ray2.20A305-387[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP02545. 11 interactions.

PTM databases

PhosphoSiteP02545.

2-D gel databases

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

Proteomic databases

PeptideAtlasP02545.
PRIDEP02545.

Genome annotation databases

EnsemblENSG00000160789. Homo sapiens. [Contig view]
GeneID4000.
KEGGhsa:4000.
UCSCuc001fnh.2. human.
uc001fni.2. human.

Organism-specific databases

GeneCardsGC01P154318.
H-InvDBHIX0001147.
HGNCHGNC:6636. LMNA.
HPACAB004022.
HPA006660.
MIM115200. 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.
Orphanet64746. 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.
PharmGKBPA231.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP02545.
HOVERGENP02545.
OMAP02545. HCSGSGD.

Enzyme and pathway databases

Pathway_Interaction_DBcaspase_pathway. Caspase cascade in apoptosis.
faspathway. FAS signaling pathway (CD95).
ReactomeREACT_578. Apoptosis.

Gene expression databases

ArrayExpressP02545.
BgeeP02545.
CleanExHS_LMNA.
GermOnlineENSG00000160789. Homo sapiens.

Family and domain databases

InterProIPR016044. F.
IPR001664. IF.
IPR001322. IF_tail_C.
IPR018039. Intermediate_filament_CS.
[Graphical view]
PANTHERPTHR23239. IF. 1 hit.
PfamPF00038. Filament. 1 hit.
PF00932. IF_tail. 1 hit.
[Graphical view]
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio15692.
PMAP-CutDBP02545.
SOURCESearch...

Entry information

Entry nameLMNA_HUMAN
AccessionPrimary (citable) accession number: P02545
Secondary accession number(s): P02546 expand/collapse secondary AC list , 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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 1

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents