Details for: LMNA

Gene ID: 4000

Symbol: LMNA

Ensembl ID: ENSG00000160789

Description: lamin A/C

Associated with

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

  • Cell Name: polychromatophilic erythroblast (CL0000550)
    Fold Change: 548.9079
    Cell Significance Index: -85.3800
  • Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
    Fold Change: 405.3329
    Cell Significance Index: -102.8100
  • Cell Name: embryonic stem cell (CL0002322)
    Fold Change: 273.5542
    Cell Significance Index: -112.6900
  • Cell Name: smooth muscle fiber of ileum (CL1000278)
    Fold Change: 226.0006
    Cell Significance Index: -106.7000
  • Cell Name: mucosal type mast cell (CL0000485)
    Fold Change: 224.5376
    Cell Significance Index: -91.2200
  • Cell Name: peripheral blood mononuclear cell (CL2000001)
    Fold Change: 198.2950
    Cell Significance Index: -102.0000
  • Cell Name: ileal goblet cell (CL1000326)
    Fold Change: 160.0841
    Cell Significance Index: -107.4200
  • Cell Name: ciliated cell of the bronchus (CL0002332)
    Fold Change: 96.1201
    Cell Significance Index: -91.7700
  • Cell Name: orthochromatic erythroblast (CL0000552)
    Fold Change: 82.5658
    Cell Significance Index: -101.8000
  • Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
    Fold Change: 39.3638
    Cell Significance Index: -105.4500
  • Cell Name: stromal cell of bone marrow (CL0010001)
    Fold Change: 26.3960
    Cell Significance Index: -104.1600
  • Cell Name: epidermal Langerhans cell (CL0002457)
    Fold Change: 24.2988
    Cell Significance Index: -53.1800
  • Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
    Fold Change: 20.8696
    Cell Significance Index: -64.1000
  • Cell Name: vascular lymphangioblast (CL0005022)
    Fold Change: 10.1679
    Cell Significance Index: 179.6800
  • Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
    Fold Change: 7.3519
    Cell Significance Index: 547.9300
  • Cell Name: luminal hormone-sensing cell of mammary gland (CL4033058)
    Fold Change: 6.8750
    Cell Significance Index: 42.3100
  • Cell Name: lactocyte (CL0002325)
    Fold Change: 6.5506
    Cell Significance Index: 846.2900
  • Cell Name: endothelial cell of venule (CL1000414)
    Fold Change: 6.2612
    Cell Significance Index: 71.1300
  • Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
    Fold Change: 5.6635
    Cell Significance Index: 266.1800
  • Cell Name: oral mucosa squamous cell (CL1001576)
    Fold Change: 5.0367
    Cell Significance Index: 43.2800
  • Cell Name: fibroblast of mammary gland (CL0002555)
    Fold Change: 3.7794
    Cell Significance Index: 108.3400
  • Cell Name: hair follicular keratinocyte (CL2000092)
    Fold Change: 3.7564
    Cell Significance Index: 1660.8000
  • Cell Name: basal cell of prostate epithelium (CL0002341)
    Fold Change: 3.4406
    Cell Significance Index: 93.6500
  • Cell Name: basal cell of urothelium (CL1000486)
    Fold Change: 3.4316
    Cell Significance Index: 421.9500
  • Cell Name: intermediate cell of urothelium (CL4030055)
    Fold Change: 3.1107
    Cell Significance Index: 560.7700
  • Cell Name: sebum secreting cell (CL0000317)
    Fold Change: 3.0478
    Cell Significance Index: 215.5500
  • Cell Name: stromal cell of ovary (CL0002132)
    Fold Change: 2.9749
    Cell Significance Index: 408.5400
  • Cell Name: odontoblast (CL0000060)
    Fold Change: 2.8752
    Cell Significance Index: 368.5800
  • Cell Name: bladder urothelial cell (CL1001428)
    Fold Change: 2.6169
    Cell Significance Index: 135.9400
  • Cell Name: enterocyte of epithelium of large intestine (CL0002071)
    Fold Change: 2.0112
    Cell Significance Index: 91.1600
  • Cell Name: placental villous trophoblast (CL2000060)
    Fold Change: 1.9503
    Cell Significance Index: 52.0800
  • Cell Name: cell in vitro (CL0001034)
    Fold Change: 1.9450
    Cell Significance Index: 1062.2300
  • Cell Name: acinar cell of salivary gland (CL0002623)
    Fold Change: 1.6824
    Cell Significance Index: 78.4400
  • Cell Name: colon goblet cell (CL0009039)
    Fold Change: 1.4009
    Cell Significance Index: 138.5800
  • Cell Name: enterocyte of epithelium of small intestine (CL1000334)
    Fold Change: 1.3552
    Cell Significance Index: 39.0500
  • Cell Name: umbrella cell of urothelium (CL4030056)
    Fold Change: 1.2830
    Cell Significance Index: 11.8200
  • Cell Name: neoplastic cell (CL0001063)
    Fold Change: 1.0706
    Cell Significance Index: 212.4600
  • Cell Name: peg cell (CL4033014)
    Fold Change: 0.9981
    Cell Significance Index: 23.0600
  • Cell Name: epithelial cell of small intestine (CL0002254)
    Fold Change: 0.9781
    Cell Significance Index: 159.0700
  • Cell Name: lung endothelial cell (CL1001567)
    Fold Change: 0.9154
    Cell Significance Index: 47.6800
  • Cell Name: gut absorptive cell (CL0000677)
    Fold Change: 0.7874
    Cell Significance Index: 47.2700
  • Cell Name: paneth cell of epithelium of small intestine (CL1000343)
    Fold Change: 0.7713
    Cell Significance Index: 16.7100
  • Cell Name: tuft cell of colon (CL0009041)
    Fold Change: 0.4946
    Cell Significance Index: 446.5500
  • Cell Name: small intestine goblet cell (CL1000495)
    Fold Change: 0.4219
    Cell Significance Index: 14.8300
  • Cell Name: cardiac muscle myoblast (CL0000513)
    Fold Change: 0.3540
    Cell Significance Index: 27.1700
  • Cell Name: intestinal crypt stem cell of colon (CL0009043)
    Fold Change: 0.3324
    Cell Significance Index: 36.1600
  • Cell Name: enteroendocrine cell of colon (CL0009042)
    Fold Change: 0.3098
    Cell Significance Index: 58.9600
  • Cell Name: fibroblast of dermis (CL0002551)
    Fold Change: 0.2862
    Cell Significance Index: 5.9900
  • Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
    Fold Change: 0.2324
    Cell Significance Index: 83.3500
  • Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
    Fold Change: 0.1214
    Cell Significance Index: 24.3600
  • Cell Name: pancreatic acinar cell (CL0002064)
    Fold Change: 0.1168
    Cell Significance Index: 19.9400
  • Cell Name: pigmented epithelial cell (CL0000529)
    Fold Change: 0.1040
    Cell Significance Index: 195.9000
  • Cell Name: anterior lens cell (CL0002223)
    Fold Change: 0.0829
    Cell Significance Index: 152.9700
  • Cell Name: pulmonary alveolar epithelial cell (CL0000322)
    Fold Change: 0.0604
    Cell Significance Index: 45.7000
  • Cell Name: lens epithelial cell (CL0002224)
    Fold Change: 0.0540
    Cell Significance Index: 83.1900
  • Cell Name: preadipocyte (CL0002334)
    Fold Change: 0.0502
    Cell Significance Index: 0.9800
  • Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
    Fold Change: 0.0410
    Cell Significance Index: 26.0200
  • Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
    Fold Change: -0.0153
    Cell Significance Index: -11.2400
  • Cell Name: secondary lens fiber (CL0002225)
    Fold Change: -0.0307
    Cell Significance Index: -41.7700
  • Cell Name: ciliary muscle cell (CL1000443)
    Fold Change: -0.0454
    Cell Significance Index: -20.5900
  • Cell Name: GABAergic interneuron (CL0011005)
    Fold Change: -0.0482
    Cell Significance Index: -33.3100
  • Cell Name: pancreatic A cell (CL0000171)
    Fold Change: -0.0503
    Cell Significance Index: -37.2900
  • Cell Name: abnormal cell (CL0001061)
    Fold Change: -0.0584
    Cell Significance Index: -5.9700
  • Cell Name: mesenchymal cell (CL0008019)
    Fold Change: -0.0723
    Cell Significance Index: -1.2100
  • Cell Name: pancreatic PP cell (CL0002275)
    Fold Change: -0.0759
    Cell Significance Index: -47.4100
  • Cell Name: prostate gland microvascular endothelial cell (CL2000059)
    Fold Change: -0.0822
    Cell Significance Index: -0.5900
  • Cell Name: type B pancreatic cell (CL0000169)
    Fold Change: -0.1219
    Cell Significance Index: -68.7200
  • Cell Name: transit amplifying cell of colon (CL0009011)
    Fold Change: -0.1652
    Cell Significance Index: -5.2900
  • Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
    Fold Change: -0.2226
    Cell Significance Index: -6.2200
  • Cell Name: dopaminergic neuron (CL0000700)
    Fold Change: -0.3171
    Cell Significance Index: -91.2500
  • Cell Name: pigmented ciliary epithelial cell (CL0002303)
    Fold Change: -0.3321
    Cell Significance Index: -48.2800
  • Cell Name: pancreatic D cell (CL0000173)
    Fold Change: -0.3458
    Cell Significance Index: -72.8300
  • Cell Name: conjunctival epithelial cell (CL1000432)
    Fold Change: -0.4771
    Cell Significance Index: -6.5100
  • Cell Name: forebrain neuroblast (CL1000042)
    Fold Change: -0.5035
    Cell Significance Index: -30.9500
  • Cell Name: pancreatic ductal cell (CL0002079)
    Fold Change: -0.5688
    Cell Significance Index: -65.1600
  • Cell Name: enteroendocrine cell of small intestine (CL0009006)
    Fold Change: -0.5901
    Cell Significance Index: -14.7500
  • Cell Name: early pro-B cell (CL0002046)
    Fold Change: -0.6336
    Cell Significance Index: -40.8800
  • Cell Name: retinal progenitor cell (CL0002672)
    Fold Change: -0.6366
    Cell Significance Index: -35.7200
  • Cell Name: epithelial cell of stomach (CL0002178)
    Fold Change: -0.6376
    Cell Significance Index: -74.3000
  • Cell Name: pancreatic endocrine cell (CL0008024)
    Fold Change: -0.7503
    Cell Significance Index: -85.6500
  • Cell Name: endothelial cell of placenta (CL0009092)
    Fold Change: -0.8044
    Cell Significance Index: -4.8600
  • Cell Name: microcirculation associated smooth muscle cell (CL0008035)
    Fold Change: -0.8131
    Cell Significance Index: -6.8300
  • Cell Name: paneth cell of colon (CL0009009)
    Fold Change: -0.8562
    Cell Significance Index: -12.8300
  • Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
    Fold Change: -0.8639
    Cell Significance Index: -89.9500
  • Cell Name: tonsil germinal center B cell (CL2000006)
    Fold Change: -0.8764
    Cell Significance Index: -103.3500
  • Cell Name: fibro/adipogenic progenitor cell (CL0009099)
    Fold Change: -0.9060
    Cell Significance Index: -45.7900
  • Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
    Fold Change: -1.0251
    Cell Significance Index: -81.1900
  • Cell Name: skeletal muscle fiber (CL0008002)
    Fold Change: -1.1017
    Cell Significance Index: -28.3200
  • Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
    Fold Change: -1.1432
    Cell Significance Index: -39.7300
  • Cell Name: granulosa cell (CL0000501)
    Fold Change: -1.1708
    Cell Significance Index: -30.7900
  • Cell Name: glycinergic neuron (CL1001509)
    Fold Change: -1.4115
    Cell Significance Index: -74.1100
  • Cell Name: intestinal tuft cell (CL0019032)
    Fold Change: -1.4310
    Cell Significance Index: -87.7400
  • Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
    Fold Change: -1.4703
    Cell Significance Index: -43.1800
  • Cell Name: hippocampal granule cell (CL0001033)
    Fold Change: -1.4824
    Cell Significance Index: -99.6800
  • Cell Name: eye photoreceptor cell (CL0000287)
    Fold Change: -1.4894
    Cell Significance Index: -93.8700
  • Cell Name: theca cell (CL0000503)
    Fold Change: -1.7872
    Cell Significance Index: -10.5000
  • Cell Name: type I muscle cell (CL0002211)
    Fold Change: -1.9869
    Cell Significance Index: -48.4800
  • Cell Name: epithelial cell of urethra (CL1000296)
    Fold Change: -1.9955
    Cell Significance Index: -12.3500
  • Cell Name: indirect pathway medium spiny neuron (CL4023029)
    Fold Change: -2.0012
    Cell Significance Index: -88.5200
  • Cell Name: kidney epithelial cell (CL0002518)
    Fold Change: -2.0825
    Cell Significance Index: -61.3400

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Other Information

**Key Characteristics** The LMNA gene is a long (3.5 kb) gene that encodes for the protein lamin A/C, which is a type of intermediate filament protein. Lamin A/C is composed of three domains: the head domain, the rod domain, and the tail domain. The head domain is responsible for protein-protein interactions, while the rod domain provides structural support to the protein. The tail domain is involved in the regulation of protein localization and stability. Mutations in the LMNA gene can result in the production of aberrant lamin A/C proteins, which can disrupt normal nuclear architecture and function. **Pathways and Functions** Lamin A/C plays a critical role in regulating various cellular processes, including: 1. **Apoptosis**: Lamin A/C regulates the apoptotic pathway by interacting with pro-apoptotic proteins, such as BAX and BAK. 2. **Cell Cycle**: Lamin A/C regulates cell cycle progression by interacting with cyclin-dependent kinases (CDKs) and other cell cycle regulators. 3. **Protein Localization**: Lamin A/C regulates the localization of proteins to the nucleus by interacting with nuclear localization signals (NLSs) and nuclear export signals (NESs). 4. **Stress Response**: Lamin A/C regulates the unfolded protein response (UPR) by interacting with chaperones and other stress response proteins. 5. **Mitosis**: Lamin A/C regulates mitotic progression by interacting with mitotic kinases and other mitotic regulators. **Clinical Significance** Mutations in the LMNA gene have been associated with a wide range of disorders, including: 1. **Laminopathies**: A group of genetic diseases characterized by the disruption of nuclear architecture and function. 2. **Huntington's Disease**: A neurodegenerative disorder characterized by the expansion of CAG repeats in the huntingtin gene. 3. **Frontotemporal Dementia**: A group of neurodegenerative disorders characterized by the degeneration of the frontal and temporal lobes. 4. **Cardiac Disease**: Mutations in the LMNA gene have been associated with cardiac disease, including cardiomyopathy and cardiac arrhythmias. 5. **Prostate Cancer**: Mutations in the LMNA gene have been associated with an increased risk of prostate cancer. In conclusion, the LMNA gene plays a critical role in regulating various cellular processes, including apoptosis, cell cycle progression, and protein localization. Mutations in the LMNA gene have been associated with a wide range of disorders, highlighting the importance of this gene in maintaining normal cellular function and preventing disease.

Genular Protein ID: 3457081316

Symbol: LMNA_HUMAN

Name: Prelamin-A/C

UniProtKB Accession Codes:

P02545 B4DI32 D3DVB0 D6RAQ3 E7EUI9 P02546 Q5I6Y4 Q5I6Y6 Q5TCJ2 Q5TCJ3 Q6UYC3 Q969I8 Q96JA2

Database IDs:

AGR 1 AlphaFoldDB 1 Antibodypedia 1 BMRB 1 Bgee 1 BioGRID 1 BioGRID-ORCS 1 BioMuta 1 CCDS 4 CORUM 1 CPTAC 4 CTD 1 ChEMBL 1 ChiTaRS 1 DIP 2 DMDM 1 DNASU 1 DisGeNET 1 DisProt 1 EMBL 17 Ensembl 11 EvolutionaryTrace 1 ExpressionAtlas 1 GO 40 Gene3D 4 GeneCards 1 GeneReviews 1 GeneTree 1 GeneWiki 1 GenomeRNAi 1 GlyConnect 1 GlyCosmos 1 GlyGen 1 HGNC 1 HOGENOM 1 HPA 1 InParanoid 1 IntAct 1 InterPro 4 KEGG 1 MANE-Select 1 MIM 23 MINT 1 MalaCards 1 MassIVE 1 MetOSite 1 NCBI Taxonomy 1 OMA 1 OpenTargets 1 Orphanet 20 OrthoDB 1 PANTHER 2 PDB 22 PDBsum 22 PIR 2 PRIDE 1 PRO 1 PROSITE 3 PathwayCommons 1 PaxDb 1 PeptideAtlas 1 Pfam 2 PharmGKB 1 Pharos 1 PhosphoSitePlus 1 PhylomeDB 1 Proteomes 1 ProteomicsDB 6 Pumba 1 REPRODUCTION-2DPAGE 3 RNAct 1 Reactome 8 RefSeq 7 SABIO-RK 1 SIGNOR 1 SMART 1 SMR 1 STRING 1 SUPFAM 3 SignaLink 1 SwissPalm 1 TopDownProteomics 3 TreeFam 1 UCSC 1 UniProtKB 1 VEuPathDB 1 eggNOG 1 iPTMnet 1 jPOST 1 neXtProt 1

Citations:

PubMed ID: 3453101

Title: Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins.

PubMed ID: 3453101

DOI: 10.1038/319463a0

PubMed ID: 3462705

Title: cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins.

PubMed ID: 3462705

DOI: 10.1073/pnas.83.17.6450

PubMed ID: 16061563

Title: In vivo and in vitro examination of the functional significances of novel lamin gene mutations in heart failure patients.

PubMed ID: 16061563

DOI: 10.1136/jmg.2004.023283

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 16710414

Title: The DNA sequence and biological annotation of human chromosome 1.

PubMed ID: 16710414

DOI: 10.1038/nature04727

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 8621584

Title: An alternative splicing product of the lamin A/C gene lacks exon 10.

PubMed ID: 8621584

DOI: 10.1074/jbc.271.16.9249

PubMed ID: 2344612

Title: Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis.

PubMed ID: 2344612

DOI: 10.1016/0092-8674(90)90470-y

PubMed ID: 2188730

Title: Identification of cell cycle-regulated phosphorylation sites on nuclear lamin C.

PubMed ID: 2188730

DOI: 10.1016/0092-8674(90)90469-u

PubMed ID: 8175923

Title: The processing pathway of prelamin A.

PubMed ID: 8175923

DOI: 10.1242/jcs.107.1.61

PubMed ID: 9030603

Title: In vitro assay and characterization of the farnesylation-dependent prelamin A endoprotease.

PubMed ID: 9030603

DOI: 10.1074/jbc.272.8.5298

PubMed ID: 10508479

Title: Antigens recognized by autologous antibody in patients with renal-cell carcinoma.

PubMed ID: 10508479

DOI: 10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5

PubMed ID: 10514485

Title: Prenylated prelamin A interacts with Narf, a novel nuclear protein.

PubMed ID: 10514485

DOI: 10.1074/jbc.274.42.30008

PubMed ID: 12475961

Title: Lamin A/C binding protein LAP2alpha is required for nuclear anchorage of retinoblastoma protein.

PubMed ID: 12475961

DOI: 10.1091/mbc.e02-07-0450

PubMed ID: 12714972

Title: Recurrent de novo point mutations in lamin A cause Hutchinson-Gilford progeria syndrome.

PubMed ID: 12714972

DOI: 10.1038/nature01629

PubMed ID: 16339967

Title: LEM2 is a novel MAN1-related inner nuclear membrane protein associated with A-type lamins.

PubMed ID: 16339967

DOI: 10.1242/jcs.02701

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 17924679

Title: 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.

PubMed ID: 17924679

DOI: 10.1021/pr070152u

PubMed ID: 18606848

Title: Sumoylation regulates lamin A function and is lost in lamin A mutants associated with familial cardiomyopathies.

PubMed ID: 18606848

DOI: 10.1083/jcb.200712124

PubMed ID: 18220336

Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

PubMed ID: 18220336

DOI: 10.1021/pr0705441

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19323649

Title: Emerin-prelamin A interplay in human fibroblasts.

PubMed ID: 19323649

DOI: 10.1042/bc20080175

PubMed ID: 19220582

Title: The R439C mutation in LMNA causes lamin oligomerization and susceptibility to oxidative stress.

PubMed ID: 19220582

DOI: 10.1111/j.1582-4934.2009.00690.x

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20079404

Title: Increased plasticity of the nuclear envelope and hypermobility of telomeres due to the loss of A-type lamins.

PubMed ID: 20079404

DOI: 10.1016/j.bbagen.2010.01.002

PubMed ID: 20160190

Title: Morphological analysis of 13 LMNA variants identified in a cohort of 324 unrelated patients with idiopathic or familial dilated cardiomyopathy.

PubMed ID: 20160190

DOI: 10.1161/circgenetics.109.905422

PubMed ID: 20458013

Title: Prelamin A acts to accelerate smooth muscle cell senescence and is a novel biomarker of human vascular aging.

PubMed ID: 20458013

DOI: 10.1161/circulationaha.109.902056

PubMed ID: 19933576

Title: Mammalian SUN protein interaction networks at the inner nuclear membrane and their role in laminopathy disease processes.

PubMed ID: 19933576

DOI: 10.1074/jbc.m109.071910

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21498514

Title: Identification of a novel muscle enriched A-type Lamin interacting protein (MLIP).

PubMed ID: 21498514

DOI: 10.1074/jbc.m110.165548

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22355414

Title: Requirements for efficient proteolytic cleavage of prelamin A by ZMPSTE24.

PubMed ID: 22355414

DOI: 10.1371/journal.pone.0032120

PubMed ID: 23666920

Title: LMNA-associated cardiocutaneous progeria: An inherited autosomal dominant premature aging syndrome with late onset.

PubMed ID: 23666920

DOI: 10.1002/ajmg.a.35971

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 23695662

Title: Depleting the methyltransferase Suv39h1 improves DNA repair and extends lifespan in a progeria mouse model.

PubMed ID: 23695662

DOI: 10.1038/ncomms2885

PubMed ID: 21949239

Title: Myotonic dystrophy protein kinase is critical for nuclear envelope integrity.

PubMed ID: 21949239

DOI: 10.1074/jbc.m111.241455

PubMed ID: 23990565

Title: Nuclear lamin-A scales with tissue stiffness and enhances matrix-directed differentiation.

PubMed ID: 23990565

DOI: 10.1126/science.1240104

PubMed ID: 25127216

Title: Matrix elasticity regulates lamin-A,C phosphorylation and turnover with feedback to actomyosin.

PubMed ID: 25127216

DOI: 10.1016/j.cub.2014.07.001

PubMed ID: 24741066

Title: Interphase phosphorylation of lamin A.

PubMed ID: 24741066

DOI: 10.1242/jcs.141820

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

DOI: 10.1038/nsmb.2890

PubMed ID: 25114211

Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.

PubMed ID: 25114211

DOI: 10.1073/pnas.1413825111

PubMed ID: 25772364

Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.

PubMed ID: 25772364

DOI: 10.1016/j.celrep.2015.02.033

PubMed ID: 25755297

Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.

PubMed ID: 25755297

DOI: 10.1074/mcp.o114.044792

PubMed ID: 26237509

Title: The active site of O-GlcNAc transferase imposes constraints on substrate sequence.

PubMed ID: 26237509

DOI: 10.1038/nsmb.3063

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 29599122

Title: Intersectin goes nuclear: secret life of an endocytic protein.

PubMed ID: 29599122

DOI: 10.1042/bcj20170897

PubMed ID: 37788673

Title: ATR promotes clearance of damaged DNA and damaged cells by rupturing micronuclei.

PubMed ID: 37788673

DOI: 10.1016/j.molcel.2023.09.003

PubMed ID: 37832547

Title: DNA damage induces nuclear envelope rupture through ATR-mediated phosphorylation of lamin A/C.

PubMed ID: 37832547

DOI: 10.1016/j.molcel.2023.09.023

PubMed ID: 11901143

Title: Structure of the globular tail of nuclear lamin.

PubMed ID: 11901143

DOI: 10.1074/jbc.c200038200

PubMed ID: 12057196

Title: The Ig-like structure of the C-terminal domain of lamin A/C, mutated in muscular dystrophies, cardiomyopathy, and partial lipodystrophy.

PubMed ID: 12057196

DOI: 10.1016/s0969-2126(02)00777-3

PubMed ID: 15476822

Title: Crystal structure of the human lamin A coil 2B dimer: implications for the head-to-tail association of nuclear lamins.

PubMed ID: 15476822

DOI: 10.1016/j.jmb.2004.08.093

PubMed ID: 31434876

Title: Structural basis for lamin assembly at the molecular level.

PubMed ID: 31434876

DOI: 10.1038/s41467-019-11684-x

PubMed ID: 33706103

Title: Beta-strand-mediated dimeric formation of the Ig-like domains of human lamin A/C and B1.

PubMed ID: 33706103

DOI: 10.1016/j.bbrc.2021.02.102

PubMed ID: 10080180

Title: Mutations in the gene encoding lamin A/C cause autosomal dominant Emery-Dreifuss muscular dystrophy.

PubMed ID: 10080180

DOI: 10.1038/6799

PubMed ID: 10580070

Title: Missense mutations in the rod domain of the lamin A/C gene as causes of dilated cardiomyopathy and conduction-system disease.

PubMed ID: 10580070

DOI: 10.1056/nejm199912023412302

PubMed ID: 10739751

Title: 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.

PubMed ID: 10739751

DOI: 10.1086/302836

PubMed ID: 10739764

Title: Different mutations in the LMNA gene cause autosomal dominant and autosomal recessive Emery-Dreifuss muscular dystrophy.

PubMed ID: 10739764

DOI: 10.1086/302869

PubMed ID: 10939567

Title: Clinical and molecular genetic spectrum of autosomal dominant Emery-Dreifuss muscular dystrophy due to mutations of the lamin A/C gene.

PubMed ID: 10939567

DOI: 10.1002/1531-8249(200008)48:2<170::aid-ana6>3.3.co;2-a

PubMed ID: 10587585

Title: Nuclear lamin A/C R482Q mutation in Canadian kindreds with Dunnigan-type familial partial lipodystrophy.

PubMed ID: 10587585

DOI: 10.1093/hmg/9.1.109

PubMed ID: 10814726

Title: Identification of mutations in the gene encoding lamins A/C in autosomal dominant limb girdle muscular dystrophy with atrioventricular conduction disturbances (LGMD1B).

PubMed ID: 10814726

DOI: 10.1093/hmg/9.9.1453

PubMed ID: 10655060

Title: LMNA, encoding lamin A/C, is mutated in partial lipodystrophy.

PubMed ID: 10655060

DOI: 10.1038/72807

PubMed ID: 10908904

Title: Autosomal dominant Emery-Dreifuss dystrophy due to mutations in rod domain of the lamin A/C gene.

PubMed ID: 10908904

DOI: 10.1212/wnl.55.2.275

PubMed ID: 11503164

Title: Novel and recurrent mutations in lamin A/C in patients with Emery-Dreifuss muscular dystrophy.

PubMed ID: 11503164

DOI: 10.1002/ajmg.1463

PubMed ID: 11561226

Title: Novel lamin A/C mutations in two families with dilated cardiomyopathy and conduction system disease.

PubMed ID: 11561226

DOI: 10.1054/jcaf.2001.26339

PubMed ID: 11792809

Title: Properties of lamin A mutants found in Emery-Dreifuss muscular dystrophy, cardiomyopathy and Dunnigan-type partial lipodystrophy.

PubMed ID: 11792809

DOI: 10.1242/jcs.114.24.4435

PubMed ID: 11525883

Title: 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.

PubMed ID: 11525883

DOI: 10.1016/s0960-8966(01)00207-3

PubMed ID: 12486434

Title: A novel lamin A/C mutation in a family with dilated cardiomyopathy, prominent conduction system disease, and need for permanent pacemaker implantation.

PubMed ID: 12486434

DOI: 10.1067/mhj.2002.126737

PubMed ID: 11799477

Title: 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.

PubMed ID: 11799477

DOI: 10.1086/339274

PubMed ID: 12075506

Title: Mandibuloacral dysplasia is caused by a mutation in LMNA-encoding lamin A/C.

PubMed ID: 12075506

DOI: 10.1086/341908

PubMed ID: 12015247

Title: Multisystem dystrophy syndrome due to novel missense mutations in the amino-terminal head and alpha-helical rod domains of the lamin A/C gene.

PubMed ID: 12015247

DOI: 10.1016/s0002-9343(02)01070-7

PubMed ID: 11897440

Title: Autosomal dominant dilated cardiomyopathy with atrioventricular block: a lamin A/C defect-related disease.

PubMed ID: 11897440

DOI: 10.1016/s0735-1097(02)01724-2

PubMed ID: 12032588

Title: Identification of lamin A/C (LMNA) gene mutations in Korean patients with autosomal dominant Emery-Dreifuss muscular dystrophy and limb-girdle muscular dystrophy 1B.

PubMed ID: 12032588

DOI: 10.1007/s100380200029

PubMed ID: 12196663

Title: Lamin A/C mutations with lipodystrophy, cardiac abnormalities, and muscular dystrophy.

PubMed ID: 12196663

DOI: 10.1212/wnl.59.4.620

PubMed ID: 12467752

Title: Frequent low penetrance mutations in the Lamin A/C gene, causing Emery Dreifuss muscular dystrophy.

PubMed ID: 12467752

DOI: 10.1016/s0960-8966(02)00178-5

PubMed ID: 14675861

Title: Apical left ventricular aneurysm without atrio-ventricular block due to a lamin A/C gene mutation.

PubMed ID: 14675861

DOI: 10.1016/s1388-9842(03)00149-1

PubMed ID: 12673789

Title: Functional consequences of an LMNA mutation associated with a new cardiac and non-cardiac phenotype.

PubMed ID: 12673789

DOI: 10.1002/humu.10170

PubMed ID: 12628721

Title: Natural history of dilated cardiomyopathy due to lamin A/C gene mutations.

PubMed ID: 12628721

DOI: 10.1016/s0735-1097(02)02954-6

PubMed ID: 12629077

Title: 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.

PubMed ID: 12629077

DOI: 10.1210/jc.2002-021506

PubMed ID: 12768443

Title: LMNA is mutated in Hutchinson-Gilford progeria (MIM 176670) but not in Wiedemann-Rautenstrauch progeroid syndrome (MIM 264090).

PubMed ID: 12768443

DOI: 10.1007/s10038-003-0025-3

PubMed ID: 12920062

Title: Expanding the phenotype of LMNA mutations in dilated cardiomyopathy and functional consequences of these mutations.

PubMed ID: 12920062

DOI: 10.1136/jmg.40.8.560

PubMed ID: 14684700

Title: Mutation analysis of the lamin A/C gene (LMNA) among patients with different cardiomuscular phenotypes.

PubMed ID: 14684700

DOI: 10.1136/jmg.40.12.e132

PubMed ID: 12927431

Title: LMNA mutations in atypical Werner's syndrome.

PubMed ID: 12927431

DOI: 10.1016/s0140-6736(03)14069-x

PubMed ID: 12649505

Title: Clinical relevance of atrial fibrillation/flutter, stroke, pacemaker implant, and heart failure in Emery-Dreifuss muscular dystrophy: a long-term longitudinal study.

PubMed ID: 12649505

DOI: 10.1161/01.str.0000064322.47667.49

PubMed ID: 15219508

Title: Familial dilated cardiomyopathy and isolated left ventricular noncompaction associated with lamin A/C gene mutations.

PubMed ID: 15219508

DOI: 10.1016/j.amjcard.2004.03.029

PubMed ID: 15140538

Title: A novel mutation, Ser143Pro, in the lamin A/C gene is common in Finnish patients with familial dilated cardiomyopathy.

PubMed ID: 15140538

DOI: 10.1016/j.ehj.2004.01.020

PubMed ID: 15317753

Title: Lamin A and ZMPSTE24 (FACE-1) defects cause nuclear disorganization and identify restrictive dermopathy as a lethal neonatal laminopathy.

PubMed ID: 15317753

DOI: 10.1093/hmg/ddh265

PubMed ID: 15060110

Title: Novel lamin A/C gene (LMNA) mutations in atypical progeroid syndromes.

PubMed ID: 15060110

DOI: 10.1136/jmg.2003.015651

PubMed ID: 15286156

Title: Homozygous missense mutation in the lamin A/C gene causes autosomal recessive Hutchinson-Gilford progeria syndrome.

PubMed ID: 15286156

DOI: 10.1136/jmg.2004.019661

PubMed ID: 14985400

Title: A new mutation of the lamin A/C gene leading to autosomal dominant axonal neuropathy, muscular dystrophy, cardiac disease, and leuconychia.

PubMed ID: 14985400

DOI: 10.1136/jmg.2003.013383

PubMed ID: 15372542

Title: Nuclear envelope alterations in fibroblasts from patients with muscular dystrophy, cardiomyopathy, and partial lipodystrophy carrying lamin A/C gene mutations.

PubMed ID: 15372542

DOI: 10.1002/mus.20122

PubMed ID: 15622532

Title: p.S143F mutation in lamin A/C: a new phenotype combining myopathy and progeria.

PubMed ID: 15622532

DOI: 10.1002/ana.20359

PubMed ID: 16156025

Title: Gene symbol: LMNA. Disease: cardiomyopathy, dilated, with conduction defect 1.

PubMed ID: 16156025

PubMed ID: 15998779

Title: A novel homozygous Ala529Val LMNA mutation in Turkish patients with mandibuloacral dysplasia.

PubMed ID: 15998779

DOI: 10.1210/jc.2004-2560

PubMed ID: 15744034

Title: Lamin A N-terminal phosphorylation is associated with myoblast activation: impairment in Emery-Dreifuss muscular dystrophy.

PubMed ID: 15744034

DOI: 10.1136/jmg.2004.026112

Sequence Information:

  • Length: 664
  • Mass: 74139
  • Checksum: E0855F7699F0318B
  • Sequence:
    • METPSQRRAT RSGAQASSTP LSPTRITRLQ EKEDLQELND RLAVYIDRVR SLETENAGLR 
LRITESEEVV SREVSGIKAA YEAELGDARK TLDSVAKERA RLQLELSKVR EEFKELKARN 
TKKEGDLIAA QARLKDLEAL LNSKEAALST ALSEKRTLEG ELHDLRGQVA KLEAALGEAK 
KQLQDEMLRR VDAENRLQTM KEELDFQKNI YSEELRETKR RHETRLVEID NGKQREFESR 
LADALQELRA QHEDQVEQYK KELEKTYSAK LDNARQSAER NSNLVGAAHE ELQQSRIRID 
SLSAQLSQLQ KQLAAKEAKL RDLEDSLARE RDTSRRLLAE KEREMAEMRA RMQQQLDEYQ 
ELLDIKLALD MEIHAYRKLL EGEEERLRLS PSPTSQRSRG RASSHSSQTQ GGGSVTKKRK 
LESTESRSSF SQHARTSGRV AVEEVDEEGK FVRLRNKSNE DQSMGNWQIK RQNGDDPLLT 
YRFPPKFTLK AGQVVTIWAA GAGATHSPPT DLVWKAQNTW GCGNSLRTAL INSTGEEVAM 
RKLVRSVTVV EDDEDEDGDD LLHHHHGSHC SSSGDPAEYN LRSRTVLCGT CGQPADKASA 
SGSGAQVGGP ISSGSSASSV TVTRSYRSVG GSGGGSFGDN LVTRSYLLGN SSPRTQSPQN 
CSIM

Genular Protein ID: 666326040

Symbol: Q5TCI8_HUMAN

Name: N/A

UniProtKB Accession Codes:

Q5TCI8

Database IDs:

ARBA 8 AlphaFoldDB 1 Antibodypedia 1 Bgee 1 BioGRID-ORCS 1 CTD 1 ChiTaRS 1 DNASU 1 DisGeNET 1 EMBL 3 Ensembl 2 ExpressionAtlas 1 GO 6 Gene3D 4 GeneTree 1 HGNC 1 HOGENOM 1 InterPro 4 MassIVE 1 NCBI Taxonomy 1 OrthoDB 1 PANTHER 2 PRIDE 1 PROSITE 5 PeptideAtlas 2 Pfam 2 Proteomes 2 ProteomicsDB 2 RefSeq 1 RuleBase 1 SAM 2 SMART 1 SMR 1 SUPFAM 2 SwissPalm 1 UCSC 1 VEuPathDB 1

Citations:

PubMed ID: 11237011

Title: Initial sequencing and analysis of the human genome.

PubMed ID: 11237011

DOI: 10.1038/35057062

PubMed ID: 15496913

Title: Finishing the euchromatic sequence of the human genome.

PubMed ID: 15496913

DOI: 10.1038/nature03001

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 16710414

Title: The DNA sequence and biological annotation of human chromosome 1.

PubMed ID: 16710414

DOI: 10.1038/nature04727

PubMed ID: 17924679

Title: 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.

PubMed ID: 17924679

DOI: 10.1021/pr070152u

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

PubMed ID: 25114211

Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.

PubMed ID: 25114211

PubMed ID: 25772364

Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.

PubMed ID: 25772364

DOI: 10.1016/j.celrep.2015.02.033

PubMed ID: 25755297

Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.

PubMed ID: 25755297

DOI: 10.1074/mcp.O114.044792

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

Sequence Information:

  • Length: 491
  • Mass: 55762
  • Checksum: 620B6533D9D65D70
  • Sequence:
    • MQPLLCLGNL EDARERTGTL LAQHPAWGRT RAKPGSPLNT KKEGDLIAAQ ARLKDLEALL 
NSKEAALSTA LSEKRTLEGE LHDLRGQVAK LEAALGEAKK QLQDEMLRRV DAENRLQTMK 
EELDFQKNIY SEELRETKRR HETRLVEIDN GKQREFESRL ADALQELRAQ HEDQVEQYKK 
ELEKTYSAKL DNARQSAERN SNLVGAAHEE LQQSRIRIDS LSAQLSQLQK QLAAKEAKLR 
DLEDSLARER DTSRRLLAEK EREMAEMRAR MQQQLDEYQE LLDIKLALDM EIHAYRKLLE 
GEEERLRLSP SPTSQRSRGR ASSHSSQTQG GGSVTKKRKL ESTESRSSFS QHARTSGRVA 
VEEVDEEGKF VRLRNKSNED QSMGNWQIKR QNGDDPLLTY RFPPKFTLKA GQVVTIWAAG 
AGATHSPPTD LVWKAQNTWG CGNSLRTALI NSTGEEVAMR KLVRSVTVVE DDEDEDGDDL 
LHHHHVSGSR R

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.