LMNA
entrez
4000
canonical
uniprot
P02545
canonical
ensembl
ENSG00000160789
resolver
ensp
ENSP00000357280
resolver
ensp
ENSP00000357282
resolver
ensp
ENSP00000357283
resolver
ensp
ENSP00000357284
resolver
ensp
ENSP00000395597
resolver
ensp
ENSP00000421821
resolver
ensp
ENSP00000426535
resolver
ensp
ENSP00000503633
resolver
ensp
ENSP00000569612
resolver
ensp
ENSP00000598058
resolver
ensp
ENSP00000638843
resolver
ensp
ENSP00000727092
resolver
ensp
ENSP00000727093
resolver
ensp
ENSP00000791671
resolver
enst
ENST00000368297
resolver
enst
ENST00000504687
resolver
genesymbol
LMNA
resolver
genesymbol_syn
LMN1
resolver
hgnc
HGNC:6636
resolver
uniprot
A0A384MQX1
resolver
uniprot
B4DI32
resolver
uniprot
D3DVB0
resolver
uniprot
D6RAQ3
resolver
uniprot
E7EUI9
resolver
uniprot
H0YAB0
resolver
uniprot
P02546
resolver
uniprot
Q5I6Y4
resolver
uniprot
Q5I6Y6
resolver
uniprot
Q5TCI8
resolver
uniprot
Q5TCJ2
resolver
uniprot
Q5TCJ3
resolver
uniprot
Q6UYC3
resolver
uniprot
Q969I8
resolver
uniprot
Q96JA2
resolver
uniprot_entry
A0A384MQX1_HUMAN
resolver
uniprot_entry
H0YAB0_HUMAN
resolver
uniprot_entry
LMNA_HUMAN
resolver
uniprot_entry
Q5TCI8_HUMAN
resolver
uniprot_sec
B4DI32
resolver
uniprot_sec
D3DVB0
resolver
uniprot_sec
D6RAQ3
resolver
uniprot_sec
E7EUI9
resolver
uniprot_sec
P02546
resolver
uniprot_sec
Q5I6Y4
resolver
uniprot_sec
Q5I6Y6
resolver
uniprot_sec
Q5TCJ2
resolver
uniprot_sec
Q5TCJ3
resolver
uniprot_sec
Q6UYC3
resolver
uniprot_sec
Q969I8
resolver
uniprot_sec
Q96JA2
resolver
amino_acid_sequence
METPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRSRGRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEEGKFVRLRNKSNEDQSMGNWQIKRQNGDDPLLTYRFPPKFTLKAGQVVTIWAAGAGATHSPPTDLVWKAQNTWGCGNSLRTALINSTGEEVAMRKLVRSVTVVEDDEDEDGDDLLHHHHGSHCSSSGDPAEYNLRSRTVLCGTCGQPADKASASGSGAQVGGPISSGSSASSVTVTRSYRSVGGSGGGSFGDNLVTRSYLLGNSSPRTQSPQNCSIM
uniprot
proteins
disease_involvement
DISEASE: Emery-Dreifuss muscular dystrophy 2, autosomal dominant (EDMD2) [MIM:181350]: A form of Emery-Dreifuss muscular dystrophy, a degenerative myopathy characterized by weakness and atrophy of muscle without involvement of the nervous system, early contractures of the elbows, Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects. {ECO:0000269|PubMed:22431096, ECO:0000269|PubMed:27234031}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Emery-Dreifuss muscular dystrophy 3, autosomal recessive (EDMD3) [MIM:616516]: A form of Emery-Dreifuss muscular dystrophy, a degenerative myopathy characterized by weakness and atrophy of muscle without involvement of the nervous system, early contractures of the elbows, Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects. {ECO:0000269|PubMed:22431096, ECO:0000269|PubMed:27234031}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, dilated, 1A (CMD1A) [MIM:115200]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:10580070, ECO:0000269|PubMed:11561226, ECO:0000269|PubMed:11792809, ECO:0000269|PubMed:11897440, ECO:0000269|PubMed:12486434, ECO:0000269|PubMed:12628721, ECO:0000269|PubMed:12920062, ECO:0000269|PubMed:14675861, ECO:0000269|PubMed:14684700, ECO:0000269|PubMed:15140538, ECO:0000269|PubMed:15219508, ECO:0000269|PubMed:15372542, ECO:0000269|PubMed:16061563, ECO:0000269|PubMed:16156025, ECO:0000269|PubMed:18606848, ECO:0000269|PubMed:19167105, ECO:0000269|PubMed:20160190, ECO:0000269|PubMed:21846512}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Lipodystrophy, familial partial, 2 (FPLD2) [MIM:151660]: An autosomal dominant disorder characterized by the loss of subcutaneous adipose tissue in the lower parts of the body (limbs, buttocks, trunk). It is accompanied by an accumulation of adipose tissue in the face and neck causing a double chin, fat neck, or cushingoid appearance. Adipose tissue may also accumulate in the axillae, back, labia majora, and intraabdominal region. Affected patients are insulin-resistant and may develop glucose intolerance and diabetes mellitus after age 20 years, hypertriglyceridemia, and low levels of high density lipoprotein cholesterol. {ECO:0000269|PubMed:10587585, ECO:0000269|PubMed:10655060, ECO:0000269|PubMed:10739751, ECO:0000269|PubMed:11792809, ECO:0000269|PubMed:12015247, ECO:0000269|PubMed:12196663, ECO:0000269|PubMed:12629077, ECO:0000269|PubMed:15372542, ECO:0000269|PubMed:17250669, ECO:0000269|PubMed:19220582, ECO:0000269|PubMed:24485160}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Charcot-Marie-Tooth disease, axonal, type 2B1 (CMT2B1) [MIM:605588]: A recessive axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. {ECO:0000269|PubMed:11799477}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Hutchinson-Gilford progeria syndrome (HGPS) [MIM:176670]: Rare genetic disorder characterized by features reminiscent of marked premature aging. {ECO:0000269|PubMed:12714972, ECO:0000269|PubMed:12768443, ECO:0000269|PubMed:12927431, ECO:0000269|PubMed:15060110, ECO:0000269|PubMed:15286156, ECO:0000269|PubMed:15622532, ECO:0000269|PubMed:19933576, ECO:0000269|PubMed:21791255, ECO:0000269|PubMed:22355414, ECO:0000269|PubMed:23666920}. Note=The disease is caused by variants affecting the gene represented in this entry. HGPS is caused by the toxic accumulation of a truncated form of lamin-A/C. This mutant protein, called progerin (isoform 6), acts to deregulate mitosis and DNA damage signaling, leading to premature cell death and senescence. The mutant form is mainly generated by a silent or missense mutation at codon 608 of prelamin A that causes activation of a cryptic splice donor site, resulting in production of isoform 6 with a deletion of 50 amino acids near the C terminus. Progerin lacks the conserved ZMPSTE24/FACE1 cleavage site and therefore remains permanently farnesylated. Thus, although it can enter the nucleus and associate with the nuclear envelope, it cannot incorporate normally into the nuclear lamina (PubMed:12714972). {ECO:0000269|PubMed:12714972}.; DISEASE: Cardiomyopathy, dilated, with hypergonadotropic hypogonadism (CMDHH) [MIM:212112]: A disorder characterized by the association of genital anomalies, hypergonadotropic hypogonadism and dilated cardiomyopathy. Patients can present other variable clinical manifestations including intellectual disability, skeletal anomalies, scleroderma-like skin, graying and thinning of hair, osteoporosis. Dilated cardiomyopathy is characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. {ECO:0000269|PubMed:12927431, ECO:0000269|PubMed:17150192, ECO:0000269|PubMed:19283854}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Mandibuloacral dysplasia with type A lipodystrophy (MADA) [MIM:248370]: A form of mandibuloacral dysplasia, a rare progeroid disorder with clinical and genetic heterogeneity, characterized by growth retardation, craniofacial dysmorphic features due to distal bone resorption, musculoskeletal and skin abnormalities associated with lipodystrophy. MADA is an autosomal recessive disease characterized by mandibular and clavicular hypoplasia, acroosteolysis, delayed closure of the cranial suture, progeroid appearance, partial alopecia, soft tissue calcinosis, joint contractures, and partial lipodystrophy with loss of subcutaneous fat from the extremities. Adipose tissue in the face, neck and trunk is normal or increased. {ECO:0000269|PubMed:12075506, ECO:0000269|PubMed:15998779, ECO:0000269|PubMed:16278265}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Restrictive dermopathy 2 (RSDM2) [MIM:619793]: An autosomal dominant form of restrictive dermopathy, a genodermatosis mainly characterized by intrauterine growth retardation, tight and rigid skin with erosions, prominent superficial vasculature and epidermal hyperkeratosis, facial dysmorphism, 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. {ECO:0000269|PubMed:15317753}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Heart-hand syndrome Slovenian type (HHS-Slovenian) [MIM:610140]: Heart-hand syndrome (HHS) is a clinically and genetically heterogeneous disorder characterized by the co-occurrence of a congenital cardiac disease and limb malformations. {ECO:0000269|PubMed:18611980}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Muscular dystrophy congenital LMNA-related (MDCL) [MIM:613205]: A form of congenital muscular dystrophy. Patients present at birth, or within the first few months of life, with hypotonia, muscle weakness and often with joint contractures. {ECO:0000269|PubMed:18551513}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Note=Defects in LMNA may cause a late-onset cardiocutaneous progeria syndrome characterized by cutaneous manifestations of aging appearing in the third decade of life, cardiac valve calcification and dysfunction, prominent atherosclerosis, and cardiomyopathy, leading to death on average in the fourth decade. {ECO:0000269|PubMed:23666920}.
uniprot
proteins
function
FUNCTION: [Lamin-A/C]: Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:2188730, PubMed:22431096, PubMed:2344612, PubMed:23666920, PubMed:24741066, PubMed:31434876, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:24741066, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamin A and C also regulate matrix stiffness by conferring nuclear mechanical properties (PubMed:23990565, PubMed:25127216). 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 (PubMed:2188730, PubMed:2344612). Lamin A and C are present in equal amounts in the lamina of mammals (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:31548606). Also involved in DNA repair: recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends (PubMed:31548606). Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation (PubMed:10080180, PubMed:10814726, PubMed:11799477, PubMed:18551513, PubMed:22431096). Required for osteoblastogenesis and bone formation (PubMed:12075506, PubMed:15317753, PubMed:18611980). Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone (PubMed:10587585). Required for cardiac homeostasis (PubMed:10580070, PubMed:12927431, PubMed:18611980, PubMed:23666920). {ECO:0000269|PubMed:10080180, ECO:0000269|PubMed:10580070, ECO:0000269|PubMed:10587585, ECO:0000269|PubMed:10814726, ECO:0000269|PubMed:11799477, ECO:0000269|PubMed:12075506, ECO:0000269|PubMed:12927431, ECO:0000269|PubMed:15317753, ECO:0000269|PubMed:18551513, ECO:0000269|PubMed:18611980, ECO:0000269|PubMed:2188730, ECO:0000269|PubMed:22431096, ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:23666920, ECO:0000269|PubMed:23990565, ECO:0000269|PubMed:24741066, ECO:0000269|PubMed:25127216, ECO:0000269|PubMed:31434876, ECO:0000269|PubMed:31548606, ECO:0000269|PubMed:37788673, ECO:0000269|PubMed:37832547}.; FUNCTION: [Prelamin-A/C]: Prelamin-A/C can accelerate smooth muscle cell senescence (PubMed:20458013). It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence (PubMed:20458013). {ECO:0000269|PubMed:20458013}.
uniprot
proteins
mass_dalton
74139
uniprot
proteins
mutagenesis
MUTAGEN 20..23; /note="Missing: Mitotic arrest; when associated with Missing 391-P--P-393."; /evidence="ECO:0000269|PubMed:2344612"; MUTAGEN 22; /note="S->A: Impaired disassembly of the nuclear envelope during mitosis. Strongly decreased disassembly of the nuclear envelope during mitosis; when associated with A-392. Decreased accumulation to the double-strand break (DSB) sites."; /evidence="ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:24741066, ECO:0000269|PubMed:31548606"; MUTAGEN 22; /note="S->D: Mimics phosphorylation; increased localization to the nucleoplasm during interphase. Causes redistribution between the nucleus and the cytoplasm during interphase; when associated with D-392 and D-628. Decreased nuclear mechanical properties. Increased accumulation to the double-strand break (DSB) sites."; /evidence="ECO:0000269|PubMed:24741066, ECO:0000269|PubMed:25127216, ECO:0000269|PubMed:31548606"; MUTAGEN 28; /note="R->T: Impaired lamin assembly."; /evidence="ECO:0000269|PubMed:2344612"; MUTAGEN 32; /note="K->Q: Impaired lamin assembly."; /evidence="ECO:0000269|PubMed:2344612"; MUTAGEN 41; /note="R->H: Impaired lamin assembly."; /evidence="ECO:0000269|PubMed:2344612"; MUTAGEN 201; /note="K->L: Decreased sumoylation; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; associated with increased cell death."; /evidence="ECO:0000269|PubMed:18606848"; MUTAGEN 282; /note="S->A: Impaired phosphorylation by ATR in response to DNA damage, leading to decreased nuclear envelope rupture."; /evidence="ECO:0000269|PubMed:37832547"; MUTAGEN 373; /note="I->E: Impaired lamin assembly."; /evidence="ECO:0000269|PubMed:2344612"; MUTAGEN 375; /note="A->D: Impaired lamin assembly."; /evidence="ECO:0000269|PubMed:2344612"; MUTAGEN 377; /note="R->H,P: Impaired lamin assembly."; /evidence="ECO:0000269|PubMed:2344612"; MUTAGEN 381; /note="E->K: Impaired lamin assembly."; /evidence="ECO:0000269|PubMed:2344612"; MUTAGEN 384; /note="E->K: Impaired lamin assembly."; /evidence="ECO:0000269|PubMed:2344612"; MUTAGEN 386; /note="R->M: Loss of interaction with IFFO1."; /evidence="ECO:0000269|PubMed:31548606"; MUTAGEN 386; /note="R->V,L,P: Impaired lamin assembly."; /evidence="ECO:0000269|PubMed:2344612"; MUTAGEN 390; /note="S->A: Decreased localization to the nucleoplasm during interphase."; /evidence="ECO:0000269|PubMed:24741066"; MUTAGEN 391..393; /note="Missing: Mitotic arrest; when associated with Missing 20-P--P-23."; /evidence="ECO:0000269|PubMed:2344612"; MUTAGEN 392; /note="S->A: Impaired disassembly of the nuclear envelope during mitosis. Strongly decreased disassembly of the nuclear envelope during mitosis; when associated with A-22. Decreased localization to the nucleoplasm during interphase. Impaired disassembly of the micronuclear envelope in response to genome instability."; /evidence="ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:24741066, ECO:0000269|PubMed:37788673"; MUTAGEN 392; /note="S->D: Mimics phosphorylation; increased localization to the nucleoplasm during interphase. Causes redistribution between the nucleus and the cytoplasm during interphase; when associated with D-22 and D-628."; /evidence="ECO:0000269|PubMed:24741066"; MUTAGEN 395; /note="S->A: Impaired phosphorylation by ATR in response to genome instability leading ro decreased phosphorylation by CDK1."; /evidence="ECO:0000269|PubMed:37788673"; MUTAGEN 395; /note="S->D: Mimics phosphorylation; disassembly of the micronuclear envelope in response to genome instability."; /evidence="ECO:0000269|PubMed:37788673"; MUTAGEN 404..407; /note="SHSS->DHSD: Mimics phosphorylation; increased localization to the nucleoplasm during interphase."; /evidence="ECO:0000269|PubMed:24741066"; MUTAGEN 628; /note="S->D: Mimics phosphorylation; causes redistribution between the nucleus and the cytoplasm during interphase; when associated with D-22 and D-392."; MUTAGEN 644; /note="R->A: Does not affect tail cleavage."; /evidence="ECO:0000269|PubMed:22355414"; MUTAGEN 647; /note="L->R: Completely inhibits tail cleavage."; /evidence="ECO:0000269|PubMed:22355414"; MUTAGEN 648; /note="L->A: Completely inhibits tail cleavage."; /evidence="ECO:0000269|PubMed:22355414"; MUTAGEN 650; /note="N->A: Partially inhibits tail cleavage."; /evidence="ECO:0000269|PubMed:22355414"; MUTAGEN 661; /note="C->S: Loss of interaction with NARF. Abolishes farnesylation."; /evidence="ECO:0000269|PubMed:10514485, ECO:0000269|PubMed:22355414
uniprot
proteins
post_translational_modification
PTM: Proteolytic cleavage of the C-terminal of 18 residues of prelamin-A/C results in the production of lamin-A/C (PubMed:20458013, PubMed:8175923, PubMed:9030603). The prelamin-A/C maturation pathway includes farnesylation of CAAX motif by protein farnesyltransferase (FNTA and FNTB), removal of the last three amino acids (-AAX) by RCE1/FACE2 and/or ZMPSTE24, methylation of the C-terminal cysteine by ICMT and endoproteolytic removal of the last 15 C-terminal amino acids by ZMPSTE24 (PubMed:20458013, PubMed:8175923, PubMed:9030603). Proteolytic cleavage requires prior farnesylation and methylation, and absence of these blocks cleavage (PubMed:20458013, PubMed:8175923, PubMed:9030603). {ECO:0000269|PubMed:20458013, ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603}.; PTM: Farnesylation of prelamin-A/C facilitates nuclear envelope targeting. {ECO:0000269|PubMed:15317753, ECO:0000269|PubMed:22355414}.; PTM: Phosphorylation plays a key role in lamin organization, subcellular localization and nuclear envelope disintegration (PubMed:2188730, PubMed:2344612, PubMed:24741066, PubMed:37788673, PubMed:37832547). Phosphorylation by CDK1 at Ser-22 and Ser-392 at the onset of mitosis drives lamin disassembly and nuclear envelope breakdown (PubMed:2188730, PubMed:2344612). Phosphorylation at Ser-22 and Ser-392 during interphase promotes localization to the nucleoplasm and regulates lamina assembly (PubMed:24741066). Phosphorylation at Ser-22, Ser-392 and Ser-628 during interphase causes redistribution between the nucleus and the cytoplasm (PubMed:24741066). Phosphorylation at Ser-22 by CDK1 regulates matrix stiffness (PubMed:25127216). Phosphorylation status of Ser-22 determines its localization between double-strand break (DSB) sites and the nuclear matrix (PubMed:31548606). Phosphorylated by ATR at Ser-282 in response to DNA damage, leading to lamin disassembly and nuclear envelope rupture (PubMed:37832547). Phosphorylation also regulates stability in micronuclei arising from genome instability: phosphorylation at Ser-395 by ATR in response to genome instability and double-stranded DNA breaks primes LMNA for subsequent phosphorylation at Ser-392 by CDK1 and micronuclei envelope rupture (PubMed:37788673). The rupture of micronuclear envelope triggers the cGAS-STING pathway thereby activating the type I interferon response and innate immunity (PubMed:37788673). {ECO:0000269|PubMed:2188730, ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:24741066, ECO:0000269|PubMed:25127216, ECO:0000269|PubMed:31548606, ECO:0000269|PubMed:37788673, ECO:0000269|PubMed:37832547}.; PTM: Acetylation by KAT8 is required for nuclear architecture. {ECO:0000250|UniProtKB:P48678}.; PTM: Sumoylation is necessary for the localization to the nuclear envelope. {ECO:0000269|PubMed:18606848}.
uniprot
proteins
protein_family
Intermediate filament family
uniprot
proteins
pubmed
10080180
uniprot
proteins
pubmed
10508479
uniprot
proteins
pubmed
10514485
uniprot
proteins
pubmed
10580070
uniprot
proteins
pubmed
10587585
uniprot
proteins
pubmed
10655060
uniprot
proteins
pubmed
10739751
uniprot
proteins
pubmed
10739764
uniprot
proteins
pubmed
10814726
uniprot
proteins
pubmed
10908904
uniprot
proteins
pubmed
10939567
uniprot
proteins
pubmed
11503164
uniprot
proteins
pubmed
11525883
uniprot
proteins
pubmed
11561226
uniprot
proteins
pubmed
11792809
uniprot
proteins
pubmed
11799477
uniprot
proteins
pubmed
11897440
uniprot
proteins
pubmed
11901143
uniprot
proteins
pubmed
12015247
uniprot
proteins
pubmed
12032588
uniprot
proteins
pubmed
12057196
uniprot
proteins
pubmed
12075506
uniprot
proteins
pubmed
12196663
uniprot
proteins
pubmed
12467752
uniprot
proteins
pubmed
12475961
uniprot
proteins
pubmed
12486434
uniprot
proteins
pubmed
12628721
uniprot
proteins
pubmed
12629077
uniprot
proteins
pubmed
12649505
uniprot
proteins
pubmed
12673789
uniprot
proteins
pubmed
12714972
uniprot
proteins
pubmed
12768443
uniprot
proteins
pubmed
12920062
uniprot
proteins
pubmed
12927431
uniprot
proteins
pubmed
14675861
uniprot
proteins
pubmed
14684700
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14985400
uniprot
proteins
pubmed
15060110
uniprot
proteins
pubmed
15140538
uniprot
proteins
pubmed
15219508
uniprot
proteins
pubmed
15286156
uniprot
proteins
pubmed
15317753
uniprot
proteins
pubmed
15372542
uniprot
proteins
pubmed
15476822
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15622532
uniprot
proteins
pubmed
15744034
uniprot
proteins
pubmed
15998779
uniprot
proteins
pubmed
16061563
uniprot
proteins
pubmed
16156025
uniprot
proteins
pubmed
16278265
uniprot
proteins
pubmed
16339967
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17136397
uniprot
proteins
pubmed
17150192
uniprot
proteins
pubmed
17250669
uniprot
proteins
pubmed
17711925
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18551513
uniprot
proteins
pubmed
18606848
uniprot
proteins
pubmed
18611980
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19167105
uniprot
proteins
pubmed
19220582
uniprot
proteins
pubmed
19283854
uniprot
proteins
pubmed
19323649
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19427440
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19933576
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20079404
uniprot
proteins
pubmed
20160190
uniprot
proteins
pubmed
20458013
uniprot
proteins
pubmed
20848652
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21498514
uniprot
proteins
pubmed
21724554
uniprot
proteins
pubmed
21791255
uniprot
proteins
pubmed
21846512
uniprot
proteins
pubmed
2188730
uniprot
proteins
pubmed
21949239
uniprot
proteins
pubmed
22355414
uniprot
proteins
pubmed
22431096
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
2344612
uniprot
proteins
pubmed
23666920
uniprot
proteins
pubmed
23695662
uniprot
proteins
pubmed
23977161
uniprot
proteins
pubmed
23990565
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24485160
uniprot
proteins
pubmed
24741066
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25127216
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26237509
uniprot
proteins
pubmed
27234031
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
29599122
uniprot
proteins
pubmed
31434876
uniprot
proteins
pubmed
31548606
uniprot
proteins
pubmed
33706103
uniprot
proteins
pubmed
3453101
uniprot
proteins
pubmed
3462705
uniprot
proteins
pubmed
35311970
uniprot
proteins
pubmed
37788673
uniprot
proteins
pubmed
37832547
uniprot
proteins
pubmed
8175923
uniprot
proteins
pubmed
8621584
uniprot
proteins
pubmed
9030603
uniprot
proteins
sequence_length
664
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus lamina {ECO:0000269|PubMed:2188730, ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:24741066, ECO:0000269|PubMed:37788673, ECO:0000269|PubMed:37832547, ECO:0000305|PubMed:10080180}. Nucleus envelope {ECO:0000269|PubMed:29599122, ECO:0000269|PubMed:37788673, ECO:0000269|PubMed:37832547}. Nucleus, nucleoplasm {ECO:0000269|PubMed:15372542, ECO:0000269|PubMed:24741066, ECO:0000269|PubMed:31548606}. Nucleus matrix {ECO:0000269|PubMed:31548606}. Note=Farnesylation of prelamin-A/C facilitates nuclear envelope targeting and subsequent cleavage by ZMPSTE24/FACE1 to remove the farnesyl group produces mature lamin-A/C, which can then be inserted into the nuclear lamina (PubMed:15317753). EMD is required for proper localization of non-farnesylated prelamin-A/C (PubMed:19323649). Also localizes to the micronuclear envelope in response to response to genome instability (PubMed:37788673). {ECO:0000269|PubMed:15317753, ECO:0000269|PubMed:19323649, ECO:0000269|PubMed:37788673}.; SUBCELLULAR LOCATION: [Isoform C]: Nucleus speckle {ECO:0000269|PubMed:16061563}.
uniprot
proteins