LMNA lamin A/C [Homo sapiens] - Gene

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Summary

Official Symbol: LMNAprovided by HGNC
Official Full Name: lamin A/Cprovided by HGNC
Primary source: HGNC:6636
Locus tag: RP11-54H19.1
See related: Ensembl:ENSG00000160789; HPRD:01035; MIM:150330; Vega:OTTHUMG00000013961
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: FPL; IDC; LFP; CDDC; EMD2; FPLD; HGPS; LDP1; LMN1; LMNC; PRO1; CDCD1; CMD1A; FPLD2; LMNL1; CMT2B1; LGMD1B
Summary: The nuclear lamina consists of a two-dimensional matrix of proteins located next to the inner nuclear membrane. The lamin family of proteins make up the matrix and are highly conserved in evolution. During mitosis, the lamina matrix is reversibly disassembled as the lamin proteins are phosphorylated. Lamin proteins are thought to be involved in nuclear stability, chromatin structure and gene expression. Vertebrate lamins consist of two types, A and B. Through alternate splicing, this gene encodes three type A lamin isoforms. Mutations in this gene lead to several diseases: Emery-Dreifuss muscular dystrophy, familial partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease, and Hutchinson-Gilford progeria syndrome. [provided by RefSeq, Jul 2008]

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Genomic context

Location :: 1q22

Sequence :: Chromosome: 1; NC_000001.10 (156084461..156109878)

See LMNA in Epigenomics, MapViewer

Chromosome 1 - NC_000001.10 Genomic Context describing neighboring genes

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Genomic regions, transcripts, and products

Genomic Sequence

Go to nucleotideGraphics FASTA GenBank

Go to reference sequence details

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Bibliography

GeneRIFs: Gene References Into Functions What's a GeneRIF?

low and high expressing alleles of the LMNA gene
Title: Low and high expressing alleles of the LMNA gene: implications for laminopathy disease development.
Three of 87 patients with metabolic syndrome carry a heterozygous mutation in LMNA or in ZMPSTE24.
Title: High prevalence of laminopathies among patients with metabolic syndrome.
LMNA mutation should be considered in myopathy patients with inflammatory changes during infancy
Title: Inflammatory changes in infantile-onset LMNA-associated myopathy.
LMNA mutations represent the most prevalent genetic cause for dilated cardiomyopathy.
Title: Clinical and mutational spectrum in a cohort of 105 unrelated patients with dilated cardiomyopathy.
Depletion of lamin A in primary cells does not increase cell proliferation but triggers a senescent cell cycle arrest.
Title: Retinoblastoma-independent regulation of cell proliferation and senescence by the p53-p21 axis in lamin A /C-depleted cells.
Mutations in LMNA cause more than 10 different disorders, called "laminopathies." These diseases affect tissues in a specific (striated muscle, adipose tissue, peripheral nerve) or in a systemic manner (premature ageing syndromes). Review.
Title: [Laminopathies: one gene, several diseases].
recombinant C-terminal tail domain of human A- and B-type lamins binds directly to purified actin
Title: Direct actin binding to A- and B-type lamin tails and actin filament bundling by the lamin A tail.
Data suggest that a pool of Nup88 on the nuclear side of the nuclear pore complex provides a novel, unexpected binding site for nuclear lamin A.
Title: The nucleoporin Nup88 is interacting with nuclear lamin A.
These results demonstrate that the interplay between SUN1 and farnesylated prelamin A contributes to nuclear positioning in human myofibers and may be implicated in pathogenetic mechanisms.
Title: Prelamin A-mediated recruitment of SUN1 to the nuclear envelope directs nuclear positioning in human muscle.
the cellular effects of progerin expression in Hutchinson-Gilford progeria syndrome are transduced, at least in part, through reduced function of the Ran GTPase and E2 SUMOylation pathways
Title: The defective nuclear lamina in Hutchinson-gilford progeria syndrome disrupts the nucleocytoplasmic Ran gradient and inhibits nuclear localization of Ubc9.

Submit: New GeneRIF Correction See all (254)

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Phenotypes

Review eQTL and phenotype association data in this region using PheGenI

Hutchinson-Gilford progeria syndrome (HGPS, progeria) is characterized by clinical features that develop in childhood and resemble some features of accelerated aging. Although signs and symptoms vary in age of onset and severity, they are remarkably consistent overall. Children with HGPS usually appear normal at birth. Profound failure to thrive occurs during the first year. Characteristic facies, with receding mandible, narrow nasal bridge and pointed nasal tip develop. During the first to third year the following usually become apparent: partial alopecia progressing to total alopecia, loss of subcutaneous fat, progressive joint contractures, bone changes, nail dystrophy, and abnormal tightness and/or small soft outpouchings of the skin over the abdomen and upper thighs, and delayed primary tooth eruption. Later findings include low-frequency conductive hearing loss, dental crowding, and partial lack of secondary tooth eruption. Additional findings present in some but not all affected individuals include photophobia, excessive ocular tearing, exposure keratitis, and Raynaud phenomenon. Motor and mental development is normal. Death occurs as a result of complications of severe atherosclerosis, either cardiac disease (myocardial infarction) or cerebrovascular disease (stroke), generally between ages six and 20 years. Average life span is approximately 13 years.

Diagnosis Testing

The diagnosis is based on recognition of common clinical features and detection of either the c.1824C>T (p.Gly608Gly) heterozygous LMNA mutation in the classic form of HGPS or one of three of the heterozygous LMNA mutations c.1822 G>A (p.Gly608Ser), c.1821 G>A (p.Val607Val), or c.1968+1G>A in atypical HGPS. Molecular genetic testing of LMNA, the only gene known to be associated with HGPS, is available on a clinical basis.

Genetic Counseling

Almost all individuals with HGPS have the disorder as the result of a de novo autosomal dominant mutation. Because HGPS is typically caused by a de novo mutation, the risk to the sibs of a proband is small. However, because one instance of apparent somatic and germline mosaicism has been reported, the recurrence risk for parents of a child with HGPS may be on the order of one in 500. Because of the (unlikely) possibility of recurrence as a result of germline mosaicism in one of the parents, prenatal testing is available.

References

PMID: 20301300

Restrictive dermopathy, lethal

MIM: 275210

Werner syndrome, atypical

MIM: 277700

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HIV-1 protein interactions

Protein	Gene	Interaction	Pubs
Rev	rev	putative interaction based on report of Rev binding to nuclear scaffold and lamin C from mouse cells	PubMed
Tat	tat	Purified HIV-1 Tat has been shown to bind with high affinity to the nuclear matrix from H9 cells and to link viral RNAs to the nuclear matrix	PubMed
Vpr	vpr	HIV-1 Vpr co-localizes with lamin A/C and induces localized disruptions in the normal nuclear lamin architecture, contributing to the formation of nuclear envelope herniations	PubMed

Go to the HIV-1, Human Protein Interaction Database

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Interactions

Products	Interactant	Other Gene	Source	Pubs	Description
NP_005563.1	NP_005563.1	LMNA	BIND	PubMed	Lamin C interacts with Lamin C.
NP_005563.1	NP_733822.1	LMNA	BIND	PubMed	Lamin C interacts with Lamin A.
NP_005563.1	NP_005564.1	LMNB1	BIND	PubMed	Lamin C interacts with Lamin B1.
NP_005563.1	NP_000312.1	RB1	BIND	PubMed	Rb interacts with lamin C
NP_005563.1	BAA09482.2	URB2	BIND	PubMed	Lamin C interacts with Lco1.
NP_733821.1	NP_005563.1	LMNA	BIND	PubMed	Prelamin A interacts with Lamin C.
NP_733821.1	NP_733821.1	LMNA	BIND	PubMed	Prelamin A interacts with itself to form a homodimer.
NP_733821.1	NP_733822.1	LMNA	BIND	PubMed	Prelamin A interacts with Lamin A.
NP_733821.1	NP_005564.1	LMNB1	BIND	PubMed	Prelamin A interacts with Lamin B1.
NP_733821.1	BAA09482.2	URB2	BIND	PubMed	Lamin A interacts with Lco1.
NP_733822.1	NP_733822.1	LMNA	BIND	PubMed	Lamin A interacts with itself to form a homodimer.
NP_733822.1	NP_005564.1	LMNB1	BIND	PubMed	Lamin A interacts with Lamin B1.
P02545	P60709	ACTB	HPRD	PubMed
P02545	P18054	ALOX12	HPRD	PubMed
P02545	O75342	ALOX12B	HPRD	PubMed
P02545	P29466	CASP1	HPRD	PubMed
P02545	P55212	CASP6	HPRD	PubMed
P02545	P06493	CDK1	HPRD	PubMed
P02545	P01133	EGF	HPRD	PubMed
P02545	P50402	EMD	HPRD	PubMed
P02545	P21333	FLNA	HPRD	PubMed
P02545	P01100	FOS	HPRD	PubMed
P02545	Q92993	KAT5	HPRD	PubMed
P02545	P02545	LMNA	HPRD	PubMed
P02545	P20700	LMNB1	HPRD	PubMed
P02545	Q9BYN8	MRPS26	HPRD	PubMed
P02545	NARF	NARF	HPRD	PubMed
P02545	Q15365	PCBP1	HPRD	PubMed
P02545	P35227	PCGF2	HPRD	PubMed
P02545	P17252	PRKCA	HPRD	PubMed
P02545	P06400	RB1	HPRD	PubMed
P02545	P84022	SMAD3	HPRD	PubMed
P02545	P36956	SREBF1	HPRD	PubMed
P02545	Q6EEV6	SUMO4	HPRD	PubMed
P02545	Q8NF91	SYNE1	HPRD	PubMed
P02545	P42166	TMPO	HPRD	PubMed
P02545	Q5JTV8	TOR1AIP1	HPRD	PubMed
P02545	P63279	UBE2I	HPRD	PubMed
P02545	Q70J99	UNC13D	HPRD	PubMed
P02545	Q14146	URB2	HPRD	PubMed
P02545	Q16600	ZNF239	HPRD	PubMed
	NP_000688.1	ALOX12	BIND	PubMed	12-LOX interacts with Lamin A.
BioGRID:110186	BioGRID:106740	ALOX12	BioGRID	PubMed	Affinity Capture-Western; Two-hybrid
BioGRID:110186	BioGRID:114342	BANF1	BioGRID	PubMed	Affinity Capture-MS
BioGRID:110186	BioGRID:120548	C20orf20	BioGRID	PubMed	Affinity Capture-MS
BioGRID:110186	BioGRID:115906	CTCF	BioGRID	PubMed	Affinity Capture-MS
BioGRID:110186	BioGRID:107880	CTNNB1	BioGRID	PubMed	Affinity Capture-Western
BioGRID:110186	BioGRID:108325	EMD	BioGRID	PubMed	Affinity Capture-MS; Affinity Capture-Western; Reconstituted Complex; Two-hybrid
BioGRID:110186	BioGRID:122669	FYCO1	BioGRID	PubMed	Affinity Capture-MS
BioGRID:110186	BioGRID:109268	H2AFX	BioGRID	PubMed	Affinity Capture-MS
BioGRID:110186	BioGRID:109833	ING1	BioGRID	PubMed	Affinity Capture-Western
BioGRID:110186	BioGRID:115779	KAT5	BioGRID	PubMed	Two-hybrid
BioGRID:110186	BioGRID:110187	LMNB1	BioGRID	PubMed	Two-hybrid
BioGRID:110186	BioGRID:110455	MME	BioGRID	PubMed	Affinity Capture-MS
BioGRID:110186	BioGRID:116134	MORF4L1	BioGRID	PubMed	Affinity Capture-MS
BioGRID:110186	BioGRID:115001	MORF4L2	BioGRID	PubMed	Affinity Capture-MS
BioGRID:110186	BioGRID:110694	MYC	BioGRID	PubMed	Affinity Capture-MS
BioGRID:110186	BioGRID:117709	NARF	BioGRID	PubMed	Reconstituted Complex; Two-hybrid
BioGRID:110186	BioGRID:111564	PRKCA	BioGRID	PubMed	Protein-peptide
BioGRID:110186	BioGRID:111860	RB1	BioGRID	PubMed	Reconstituted Complex
BioGRID:110186	BioGRID:111863	RBBP4	BioGRID	PubMed	Reconstituted Complex; Two-hybrid
BioGRID:110186	BioGRID:112598	SREBF1	BioGRID	PubMed	Affinity Capture-Western; Reconstituted Complex; Two-hybrid
BioGRID:110186	BioGRID:115544	SRRM1	BioGRID	PubMed	Affinity Capture-MS
BioGRID:110186	BioGRID:117071	SRRM2	BioGRID	PubMed	Affinity Capture-MS
BioGRID:110186	BioGRID:113188	SUMO1	BioGRID	PubMed	Affinity Capture-MS; Reconstituted Complex
BioGRID:110186	BioGRID:116928	SYNE1	BioGRID	PubMed	Affinity Capture-Western; Reconstituted Complex
BioGRID:110186	BioGRID:112967	TMPO	BioGRID	PubMed	Affinity Capture-Western; Co-localization; Far Western
BioGRID:110186	BioGRID:108193	TOR1A	BioGRID	PubMed	Reconstituted Complex
BioGRID:110186	BioGRID:117543	TOR1AIP1	BioGRID	PubMed	Reconstituted Complex
BioGRID:110186	BioGRID:113164	UBC	BioGRID	PubMed	Reconstituted Complex
BioGRID:110186	BioGRID:119509	UCHL5	BioGRID	PubMed	Reconstituted Complex
BioGRID:110186	BioGRID:116168	YWHAQ	BioGRID	PubMed	Affinity Capture-MS
BioGRID:110186	BioGRID:113831	ZNF239	BioGRID	PubMed	Reconstituted Complex; Two-hybrid

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General gene information

Markers

D20S1027 (e-PCR)
- UniSTS:55344

MARC_3281-3282:991936958:1 (e-PCR)
- UniSTS:231005

G15913 (e-PCR)
- UniSTS:8612

LMNA_902 (e-PCR)
- UniSTS:277454

PMC169171P1 (e-PCR)
- UniSTS:271604

PMC169171P2 (e-PCR)
- UniSTS:271605

PMC169171P3 (e-PCR)
- UniSTS:271606

PMC169171P4 (e-PCR)
- UniSTS:271607

PMC169171P5 (e-PCR)
- UniSTS:271608

PMC169171P6 (e-PCR)
- UniSTS:271609

RH69068 (e-PCR)
- UniSTS:50685

Genotypes

See LMNA SNP Geneview Report
See LMNA SNP Genotype Report
See LMNA SNP Variation Viewer Report

Homology

Homologs of the LMNA gene: The LMNA gene is conserved in chimpanzee, dog, cow, mouse, rat, zebrafish, and mosquito.
Map Viewer (Mouse, Rat)

Pathways from BioSystems

Activation of Chaperone Genes by XBP1(S), organism-specific biosystem (from REACTOME)
Activation of Chaperone Genes by XBP1(S), organism-specific biosystemXbp-1 (S) binds the sequence CCACG in ER Stress Responsive Elements (ERSE, consensus sequence CCAAT (N)9 CCACG) located upstream from many genes. The ubiquitous transcription factor NF-Y, a heterotri...
Activation of Chaperones by IRE1alpha, organism-specific biosystem (from REACTOME)
Activation of Chaperones by IRE1alpha, organism-specific biosystemIRE1-alpha is a single-pass transmembrane protein that resides in the endoplasmic reticulum (ER) membrane. The C-terminus of IRE1-alpha is located in the cytosol; the N-terminus is located in the ER ...
Adipogenesis, organism-specific biosystem (from WikiPathways)
Adipogenesis, organism-specific biosystemThe different classess of factors involved in adipogenesis are shown. Adipogenesis is the process by which fat cells differentiate from predadipocytes to adipocytes (fat cells). Adipose tissue, compo...
Apoptosis, organism-specific biosystem (from REACTOME)
Apoptosis, organism-specific biosystemApoptosis is a distinct form of cell death that is functionally and morphologically different from necrosis. Nuclear chromatin condensation, cytoplasmic shrinking, dilated endoplasmic reticulum, and ...
Apoptotic cleavage of cellular proteins, organism-specific biosystem (from REACTOME)
Apoptotic cleavage of cellular proteins, organism-specific biosystemApoptotic cell death is achieved by the caspase-mediatedcleavage of various vital proteins. Among caspase targets are proteins such as E-cadherin, Beta-catenin, alpha fodrin, GAS2, FADK, alpha adduc...
Apoptotic execution phase, organism-specific biosystem (from REACTOME)
Apoptotic execution phase, organism-specific biosystemIn the execution phase of apoptosis, effector caspases cleave vital cellular proteins leading to the morphological changes that characterize apoptosis. These changes include destruction of the nucle...
Arrhythmogenic right ventricular cardiomyopathy (ARVC), organism-specific biosystem (from KEGG)
Arrhythmogenic right ventricular cardiomyopathy (ARVC), organism-specific biosystemArrhythmogenic right ventricular cardiomyopathy (ARVC) is an inherited heart muscle disease that may result in arrhythmia, heart failure, and sudden death. The hallmark pathological findings are prog...
Arrhythmogenic right ventricular cardiomyopathy (ARVC), conserved biosystem (from KEGG)
Arrhythmogenic right ventricular cardiomyopathy (ARVC), conserved biosystemArrhythmogenic right ventricular cardiomyopathy (ARVC) is an inherited heart muscle disease that may result in arrhythmia, heart failure, and sudden death. The hallmark pathological findings are prog...
Breakdown of the nuclear lamina, organism-specific biosystem (from REACTOME)
Breakdown of the nuclear lamina, organism-specific biosystemActivated caspases cleave nuclear lamins causing the irreversible breakdown of the nuclear lamina.
Caspase cascade in apoptosis, organism-specific biosystem (from Pathway Interaction Database)
Caspase cascade in apoptosis, organism-specific biosystem
Caspase cascade in apoptosis
Cell Cycle, organism-specific biosystem (from REACTOME)
Cell Cycle, organism-specific biosystem
Cell Cycle
Chromosome Maintenance, organism-specific biosystem (from REACTOME)
Chromosome Maintenance, organism-specific biosystemChromosome maintenance is critical for stable chromosome function in mammalian and other eukaryotic cells. Aspects of telomere maintenance and nucleosome assembly are covered here.
Diabetes pathways, organism-specific biosystem (from REACTOME)
Diabetes pathways, organism-specific biosystemThis module groups several normal processes that have key roles in the synthesis and function of insulin, insulin-like growth factors and ghrelin, and whose derangement is thus central to the pathoge...
Dilated cardiomyopathy, organism-specific biosystem (from KEGG)
Dilated cardiomyopathy, organism-specific biosystemDilated cardiomyopathy (DCM) is a heart muscle disease characterised by dilation and impaired contraction of the left or both ventricles that results in progressive heart failure and sudden cardiac d...
Dilated cardiomyopathy, conserved biosystem (from KEGG)
Dilated cardiomyopathy, conserved biosystemDilated cardiomyopathy (DCM) is a heart muscle disease characterised by dilation and impaired contraction of the left or both ventricles that results in progressive heart failure and sudden cardiac d...
Disease, organism-specific biosystem (from REACTOME)
Disease, organism-specific biosystemBiological processes are captured in Reactome by identifying the molecules (DNA, RNA, protein, small molecules) involved in them and describing the details of their interactions. From this molecular ...
FAS pathway and Stress induction of HSP regulation, organism-specific biosystem (from WikiPathways)
FAS pathway and Stress induction of HSP regulation, organism-specific biosystemThis pathway describes the Fas induced apoptosis and interplay with Hsp27 in response to stress. More info: [http://www.biocarta.com/pathfiles/h_hsp27Pathway.asp BioCarta].
Hypertrophic cardiomyopathy (HCM), organism-specific biosystem (from KEGG)
Hypertrophic cardiomyopathy (HCM), organism-specific biosystemHypertrophic cardiomyopathy (HCM) is a primary myocardial disorder with an autosomal dominant pattern of inheritance that is characterized by hypertrophy of the left ventricles with histological feat...
Hypertrophic cardiomyopathy (HCM), conserved biosystem (from KEGG)
Hypertrophic cardiomyopathy (HCM), conserved biosystemHypertrophic cardiomyopathy (HCM) is a primary myocardial disorder with an autosomal dominant pattern of inheritance that is characterized by hypertrophy of the left ventricles with histological feat...
Meiosis, organism-specific biosystem (from REACTOME)
Meiosis, organism-specific biosystemDuring meiosis the replicated chromosomes of a single diploid cell are segregated into 4 haploid daughter cells by two successive divisions, meiosis I and meiosis II. In meiosis I, the distinguishing...
Meiotic Synapsis, organism-specific biosystem (from REACTOME)
Meiotic Synapsis, organism-specific biosystemMeiotic synapsis is the stable physical pairing of homologous chromosomes that begins in leptonema of prophase I and lasts until anaphase of prophase I. First, short segments of axial elements form a...
Unfolded Protein Response, organism-specific biosystem (from REACTOME)
Unfolded Protein Response, organism-specific biosystemThe Unfolded Protein Response (UPR) is a regulatory system that protects the Endoplasmic Reticulum (ER) from overload. The UPR is provoked by the accumulation of improperly folded protein in the ER d...

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
protein binding	IPI Inferred from Physical Interaction more info	PubMed
structural molecule activity	IEA Inferred from Electronic Annotation more info
structural molecule activity	TAS Traceable Author Statement more info	PubMed

Process	Evidence Code	Pubs
activation of signaling protein activity involved in unfolded protein response	TAS Traceable Author Statement more info
apoptotic process	TAS Traceable Author Statement more info
cellular component disassembly involved in apoptosis	TAS Traceable Author Statement more info
cellular response to hypoxia	IEP Inferred from Expression Pattern more info
endoplasmic reticulum unfolded protein response	TAS Traceable Author Statement more info
establishment or maintenance of microtubule cytoskeleton polarity	ISS Inferred from Sequence or Structural Similarity more info
muscle organ development	IMP Inferred from Mutant Phenotype more info	PubMed
nuclear envelope organization	IEA Inferred from Electronic Annotation more info
positive regulation of cell aging	IDA Inferred from Direct Assay more info
protein localization to nucleus	ISS Inferred from Sequence or Structural Similarity more info
regulation of apoptotic process	ISS Inferred from Sequence or Structural Similarity more info
regulation of cell migration	ISS Inferred from Sequence or Structural Similarity more info
spermatogenesis	IEA Inferred from Electronic Annotation more info
sterol regulatory element binding protein import into nucleus	IEA Inferred from Electronic Annotation more info
ventricular cardiac muscle cell development	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
cytoplasm	IDA Inferred from Direct Assay more info	PubMed
insoluble fraction	IEA Inferred from Electronic Annotation more info
intermediate filament	IEA Inferred from Electronic Annotation more info
intermediate filament	TAS Traceable Author Statement more info	PubMed
lamin filament	IEA Inferred from Electronic Annotation more info
lamin filament	TAS Traceable Author Statement more info	PubMed
nuclear envelope	IDA Inferred from Direct Assay more info	PubMed
nuclear envelope	TAS Traceable Author Statement more info
nuclear lamina	TAS Traceable Author Statement more info	PubMed
nuclear matrix	IEA Inferred from Electronic Annotation more info
nucleoplasm	TAS Traceable Author Statement more info
nucleus	IDA Inferred from Direct Assay more info	PubMed
perinuclear region of cytoplasm	IDA Inferred from Direct Assay more info	PubMed

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General protein information

Preferred Names: prelamin-A/C

Names: prelamin-A/C; 70 kDa lamin; lamin A/C-like 1; renal carcinoma antigen NY-REN-32

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NCBI Reference Sequences (RefSeq)

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

Genomic

NG_008692.2 RefSeqGene

Range

37098..62515

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_005572.3 → NP_005563.1 prelamin-A/C isoform 2

Status: REVIEWED

Description

Transcript Variant: This variant (2) uses an alternate splice site in the 3' coding region, compared to variant 1, resulting in a shorter isoform (2, also known as lamin C) with a distinct C-terminus when compared to isoform 1.

Source sequence(s)

AA558657, DA421696, X03445

Consensus CDS

CCDS1131.1

UniProtKB/Swiss-Prot

P02545

Related

ENSP00000355292, ENST00000361308

Conserved Domains (2) summary

pfam00038
Location:30 – 378
Blast Score: 496

Filament; Intermediate filament protein

pfam00932
Location:432 – 541
Blast Score: 209

LTD; Lamin Tail Domain
NM_170707.2 → NP_733821.1 prelamin-A/C isoform 1 precursor

Status: REVIEWED

Description

Transcript Variant: This variant (1) encodes isoform 1, also known as lamin A.

Source sequence(s)

BC014507, BU732343, CB854404, DA421696, X03444

Consensus CDS

CCDS1129.1

UniProtKB/Swiss-Prot

P02545

Related

ENSP00000357283, OTTHUMP00000015848, ENST00000368300, OTTHUMT00000039200

Conserved Domains (2) summary

pfam00038
Location:30 – 378
Blast Score: 517

Filament; Intermediate filament protein

pfam00932
Location:432 – 541
Blast Score: 208

LTD; Lamin Tail Domain
NM_170708.2 → NP_733822.1 prelamin-A/C isoform 3

Status: REVIEWED

Description

Transcript Variant: This variant (3) lacks an internal segment of sequence compared to variant 1. The encoded isoform (3), also known as the lamin Adelta10 isoform, is shorter but has the same C-terminus when compared to isoform 1 (lamin A).

Source sequence(s)

AF381029, BC014507, BU732343, CB854404, DA421696

UniProtKB/Swiss-Prot

P02545

Related

ENSP00000292304, ENST00000347559

Conserved Domains (2) summary

pfam00038
Location:30 – 378
Blast Score: 521

Filament; Intermediate filament protein

pfam00932
Location:432 – 536
Blast Score: 195

LTD; Lamin Tail Domain

RefSeqs of Annotated Genomes: Build 37.3

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh37.p5 Primary Assembly

Genomic

NC_000001.10 Reference GRCh37.p5 Primary Assembly

Range

156084461..156109878

Download

GenBank, FASTA, Sequence Viewer (Graphics)

Alternate HuRef

Genomic

AC_000133.1 Alternate HuRef

Range

127446672..127472060

Download

GenBank, FASTA, Sequence Viewer (Graphics)

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Related Sequences

Nucleotide		Protein
Heading	Accession and Version	Protein
genomic	AL135927.14	CAI15520.1
		CAI15521.1
		CAI15522.1
		CAI15523.1
		CAI15526.1
		CAI15527.1
genomic	AL356734.32	None
genomic	CH471121.2	EAW52996.1
		EAW52997.1
		EAW52998.1
		EAW52999.1
		EAW53000.1
genomic	L12399.3	None
mRNA	AA558657.1	None
mRNA	AF381029.1	AAK59326.1
mRNA	AK026584.1	None
mRNA	AK056143.1	None
mRNA	AK056191.1	None
mRNA	AK057997.1	None
mRNA	AK097801.1	None
mRNA	AK098128.1	None
mRNA	AK122732.1	None
mRNA	AK130179.1	None
mRNA	AK294217.1	BAG57524.1
mRNA	AK295390.1	BAG58344.1
mRNA	AK309539.1	None
mRNA	AY357727.1	AAR29466.1
mRNA	AY528714.1	ABB04050.1
mRNA	AY847595.1	AAW32538.1
mRNA	AY847596.1	AAW32539.1
mRNA	AY847597.1	AAW32540.1
mRNA	BC000511.2	AAH00511.1
mRNA	BC003162.1	AAH03162.1
mRNA	BC014507.1	AAH14507.1
mRNA	BC018863.2	None
mRNA	BC033088.1	AAH33088.1
mRNA	BU732343.1	None
mRNA	CB854404.1	None
mRNA	DA421696.1	None
mRNA	M13451.1	AAA36164.1
mRNA	M13452.1	AAA36160.1
mRNA	X03444.1	CAA27173.1
mRNA	X03445.1	CAA27174.1
other-genetic	EU831758.1	ACE87276.1
other-genetic	EU831836.1	ACE86595.1
other-genetic	EU832167.1	ACE87517.1
other-genetic	EU832261.1	ACE86831.1

Protein Accession	Links
Protein Accession	GenePept Link	UniProtKB Link
P02545.1	GenPept	UniProtKB/Swiss-Prot:P02545
Q3BDU5	GenPept	UniProtKB/TrEMBL:Q3BDU5
Q5I6Y4	GenPept	UniProtKB/TrEMBL:Q5I6Y4
Q5I6Y5	GenPept	UniProtKB/TrEMBL:Q5I6Y5
Q5I6Y6	GenPept	UniProtKB/TrEMBL:Q5I6Y6
Q5TCI9	GenPept	UniProtKB/TrEMBL:Q5TCI9
Q5TCJ4	GenPept	UniProtKB/TrEMBL:Q5TCJ4
Q6UYC3	GenPept	UniProtKB/TrEMBL:Q6UYC3
Q8N519	GenPept	UniProtKB/TrEMBL:Q8N519