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Prelamin-A/C [Cleaved into: Lamin-A/C (70 kDa lamin) (Renal carcinoma antigen NY-REN-32)]

 LMNA_HUMAN              Reviewed;         664 AA.
P02545; B4DI32; D3DVB0; D6RAQ3; E7EUI9; P02546; Q5I6Y4; Q5I6Y6; Q5TCJ2;
Q5TCJ3; Q6UYC3; Q969I8; Q96JA2;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
20-MAR-1987, sequence version 1.
02-JUN-2021, entry version 263.
RecName: Full=Prelamin-A/C;
Contains:
RecName: Full=Lamin-A/C;
AltName: Full=70 kDa lamin;
AltName: Full=Renal carcinoma antigen NY-REN-32;
Flags: Precursor;
Name=LMNA; Synonyms=LMN1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND C).
PubMed=3453101; DOI=10.1038/319463a0;
McKeon F.D., Kirschner M.W., Caput D.;
"Homologies in both primary and secondary structure between nuclear
envelope and intermediate filament proteins.";
Nature 319:463-468(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND C), AND PROTEIN SEQUENCE OF
583-644.
PubMed=3462705; DOI=10.1073/pnas.83.17.6450;
Fisher D.Z., Chaudhary N., Blobel G.;
"cDNA sequencing of nuclear lamins A and C reveals primary and secondary
structural homology to intermediate filament proteins.";
Proc. Natl. Acad. Sci. U.S.A. 83:6450-6454(1986).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), SUBCELLULAR LOCATION (ISOFORM C),
VARIANTS CMD1A TRP-190; GLY-192 AND SER-541, AND CHARACTERIZATION OF
VARIANTS CMD1A GLY-192 AND SER-541.
PubMed=16061563; DOI=10.1136/jmg.2004.023283;
Sylvius N., Bilinska Z.T., Veinot J.P., Fidzianska A., Bolongo P.M.,
Poon S., McKeown P., Davies R.A., Chan K.-L., Tang A.S.L., Dyack S.,
Grzybowski J., Ruzyllo W., McBride H., Tesson F.;
"In vivo and in vitro examination of the functional significances of novel
lamin gene mutations in heart failure patients.";
J. Med. Genet. 42:639-647(2005).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
Csoka A.B.;
"The progerin allele of lamin A disrupts chromatin organization.";
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Corpus callosum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND C).
TISSUE=Kidney, Lung, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 12-25; 29-90; 102-117; 120-166; 172-189; 197-216;
226-233; 241-260; 281-316; 320-329; 352-386; 440-453; 456-482; 472-482;
516-542; 585-624 AND 628-644, PHOSPHORYLATION AT SER-22, AND IDENTIFICATION
BY MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.,
Norman J.C.;
Submitted (OCT-2009) to UniProtKB.
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 375-664 (ISOFORM ADELTA10).
TISSUE=Colon;
PubMed=8621584; DOI=10.1074/jbc.271.16.9249;
Machiels B.M., Zorenc A.H., Endert J.M., Kuijpers H.J., van Eys G.J.,
Ramaekers F.C., Broers J.L.;
"An alternative splicing product of the lamin A/C gene lacks exon 10.";
J. Biol. Chem. 271:9249-9253(1996).
[11]
PROTEOLYTIC CLEAVAGE, ISOPRENYLATION AT CYS-661, AND METHYLATION AT
CYS-661.
PubMed=8175923;
Sinensky M., Fantle K., Trujillo M., McLain T., Kupfer A., Dalton M.;
"The processing pathway of prelamin A.";
J. Cell Sci. 107:61-67(1994).
[12]
PROTEOLYTIC CLEAVAGE, ISOPRENYLATION AT CYS-661, AND METHYLATION AT
CYS-661.
PubMed=9030603; DOI=10.1074/jbc.272.8.5298;
Kilic F., Dalton M.B., Burrell S.K., Mayer J.P., Patterson S.D.,
Sinensky M.;
"In vitro assay and characterization of the farnesylation-dependent
prelamin A endoprotease.";
J. Biol. Chem. 272:5298-5304(1997).
[13]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
PubMed=10508479;
DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
Old L.J.;
"Antigens recognized by autologous antibody in patients with renal-cell
carcinoma.";
Int. J. Cancer 83:456-464(1999).
[14]
INTERACTION WITH NARF, AND MUTAGENESIS OF CYS-661.
PubMed=10514485; DOI=10.1074/jbc.274.42.30008;
Barton R.M., Worman H.J.;
"Prenylated prelamin A interacts with Narf, a novel nuclear protein.";
J. Biol. Chem. 274:30008-30018(1999).
[15]
INTERACTION WITH TMPO-ALPHA AND RB1.
PubMed=12475961; DOI=10.1091/mbc.e02-07-0450;
Markiewicz E., Dechat T., Foisner R., Quinlan R.A., Hutchison C.J.;
"Lamin A/C binding protein LAP2alpha is required for nuclear anchorage of
retinoblastoma protein.";
Mol. Biol. Cell 13:4401-4413(2002).
[16]
ALTERNATIVE SPLICING, INVOLVEMENT IN HGPS (ISOFORM 6), AND VARIANTS HGPS
LYS-145 AND SER-608.
PubMed=12714972; DOI=10.1038/nature01629;
Eriksson M., Brown W.T., Gordon L.B., Glynn M.W., Singer J., Scott L.,
Erdos M.R., Robbins C.M., Moses T.Y., Berglund P., Dutra A., Pak E.,
Durkin S., Csoka A.B., Boehnke M., Glover T.W., Collins F.S.;
"Recurrent de novo point mutations in lamin A cause Hutchinson-Gilford
progeria syndrome.";
Nature 423:293-298(2003).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling
networks.";
Cell 127:635-648(2006).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-22; SER-390; SER-392;
SER-395; SER-628; SER-632 AND SER-636, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation
analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-628, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"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.";
J. Proteome Res. 6:4150-4162(2007).
[20]
SUBCELLULAR LOCATION, SUMOYLATION AT LYS-201, MUTAGENESIS OF LYS-201, AND
CHARACTERIZATION OF VARIANTS CMD1A GLY-203 AND LYS-203.
PubMed=18606848; DOI=10.1083/jcb.200712124;
Zhang Y.Q., Sarge K.D.;
"Sumoylation regulates lamin A function and is lost in lamin A mutants
associated with familial cardiomyopathies.";
J. Cell Biol. 182:35-39(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-628, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the
kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-18; THR-19; SER-22;
SER-301; SER-390; SER-392; SER-395; SER-458; SER-628; SER-632; SER-636 AND
SER-652, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in a
refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[25]
SUBCELLULAR LOCATION, AND INTERACTION WITH EMD.
PubMed=19323649; DOI=10.1042/bc20080175;
Capanni C., Del Coco R., Mattioli E., Camozzi D., Columbaro M., Schena E.,
Merlini L., Squarzoni S., Maraldi N.M., Lattanzi G.;
"Emerin-prelamin A interplay in human fibroblasts.";
Biol. Cell 101:541-554(2009).
[26]
SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANTS FPLD2 CYS-439 AND
TRP-482.
PubMed=19220582; DOI=10.1111/j.1582-4934.2009.00690.x;
Verstraeten V.L., Caputo S., van Steensel M.A., Duband-Goulet I.,
Zinn-Justin S., Kamps M., Kuijpers H.J., Ostlund C., Worman H.J.,
Briede J.J., Le Dour C., Marcelis C.L., van Geel M., Steijlen P.M.,
van den Wijngaard A., Ramaekers F.C., Broers J.L.;
"The R439C mutation in LMNA causes lamin oligomerization and susceptibility
to oxidative stress.";
J. Cell. Mol. Med. 13:959-971(2009).
[27]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-108; LYS-270; LYS-311 AND
LYS-450, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[28]
FUNCTION.
PubMed=20079404; DOI=10.1016/j.bbagen.2010.01.002;
De Vos W.H., Houben F., Hoebe R.A., Hennekam R., van Engelen B.,
Manders E.M., Ramaekers F.C., Broers J.L., Van Oostveldt P.;
"Increased plasticity of the nuclear envelope and hypermobility of
telomeres due to the loss of A-type lamins.";
Biochim. Biophys. Acta 1800:448-458(2010).
[29]
SUBCELLULAR LOCATION, AND VARIANTS CMD1A LEU-89; PRO-101; PRO-166; GLN-190;
LYS-203; SER-210; PRO-215; THR-318; HIS-388; CYS-399 AND HIS-471.
PubMed=20160190; DOI=10.1161/circgenetics.109.905422;
Cowan J., Li D., Gonzalez-Quintana J., Morales A., Hershberger R.E.;
"Morphological analysis of 13 LMNA variants identified in a cohort of 324
unrelated patients with idiopathic or familial dilated cardiomyopathy.";
Circ. Cardiovasc. Genet. 3:6-14(2010).
[30]
FUNCTION, PROTEOLYTIC PROCESSING, AND TISSUE SPECIFICITY.
PubMed=20458013; DOI=10.1161/circulationaha.109.902056;
Ragnauth C.D., Warren D.T., Liu Y., McNair R., Tajsic T., Figg N.,
Shroff R., Skepper J., Shanahan C.M.;
"Prelamin A acts to accelerate smooth muscle cell senescence and is a novel
biomarker of human vascular aging.";
Circulation 121:2200-2210(2010).
[31]
INTERACTION WITH SUN1, CHARACTERIZATION OF VARIANTS EDMD2 PRO-527 AND
PRO-530, AND CHARACTERIZATION OF VARIANT HGPS SER-608.
PubMed=19933576; DOI=10.1074/jbc.m109.071910;
Haque F., Mazzeo D., Patel J.T., Smallwood D.T., Ellis J.A., Shanahan C.M.,
Shackleton S.;
"Mammalian SUN protein interaction networks at the inner nuclear membrane
and their role in laminopathy disease processes.";
J. Biol. Chem. 285:3487-3498(2010).
[32]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
ANALYSIS] AT THR-3; SER-12; THR-19; SER-22; SER-212; SER-277; SER-301;
SER-390; SER-392; SER-395; SER-404; SER-414; SER-431; SER-458; SER-463;
THR-505; SER-628; SER-632; SER-636 AND SER-652, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[33]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[34]
INTERACTION WITH MLIP.
PubMed=21498514; DOI=10.1074/jbc.m110.165548;
Ahmady E., Deeke S.A., Rabaa S., Kouri L., Kenney L., Stewart A.F.,
Burgon P.G.;
"Identification of a novel muscle enriched A-type Lamin interacting protein
(MLIP).";
J. Biol. Chem. 286:19702-19713(2011).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390; SER-392; SER-404;
SER-414; SER-458 AND SER-636, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
"System-wide temporal characterization of the proteome and phosphoproteome
of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[36]
MUTAGENESIS OF ARG-644; LEU-647; LEU-648; ASN-650 AND CYS-661, AND
CHARACTERIZATION OF VARIANT HGPS CYS-644.
PubMed=22355414; DOI=10.1371/journal.pone.0032120;
Barrowman J., Hamblet C., Kane M.S., Michaelis S.;
"Requirements for efficient proteolytic cleavage of prelamin A by
ZMPSTE24.";
PLoS ONE 7:E32120-E32120(2012).
[37]
FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN HGPS, VARIANT HGPS GLY-300,
AND CHARACTERIZATION OF VARIANT HGPS GLY-300.
PubMed=23666920; DOI=10.1002/ajmg.a.35971;
Kane M.S., Lindsay M.E., Judge D.P., Barrowman J., Ap Rhys C., Simonson L.,
Dietz H.C., Michaelis S.;
"LMNA-associated cardiocutaneous progeria: An inherited autosomal dominant
premature aging syndrome with late onset.";
Am. J. Med. Genet. A 161:1599-1611(2013).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; THR-19; SER-22; SER-51;
SER-66; SER-71; SER-107; SER-212; SER-301; SER-390; SER-392; SER-398;
SER-429; SER-458; SER-463; SER-533; SER-613; SER-619; SER-628; SER-632 AND
SER-636, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[39]
SUBCELLULAR LOCATION, AND INTERACTION WITH SUV39H1.
PubMed=23695662; DOI=10.1038/ncomms2885;
Liu B., Wang Z., Zhang L., Ghosh S., Zheng H., Zhou Z.;
"Depleting the methyltransferase Suv39h1 improves DNA repair and extends
lifespan in a progeria mouse model.";
Nat. Commun. 4:1868-1868(2013).
[40]
INTERACTION WITH DMPK.
PubMed=21949239; DOI=10.1074/jbc.m111.241455;
Harmon E.B., Harmon M.L., Larsen T.D., Yang J., Glasford J.W.,
Perryman M.B.;
"Myotonic dystrophy protein kinase is critical for nuclear envelope
integrity.";
J. Biol. Chem. 286:40296-40306(2011).
[41]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; THR-19; SER-22; SER-212;
SER-301; SER-307; SER-390; SER-395; SER-403; SER-404; SER-414; SER-458;
SER-463; SER-612 AND SER-636, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[42]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-97; LYS-208; LYS-233; LYS-311;
LYS-378; LYS-417 AND LYS-420, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[43]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-233 AND LYS-597, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[44]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-97; LYS-311; LYS-378 AND LYS-420,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[45]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-233; LYS-260; LYS-270; LYS-378;
LYS-417 AND LYS-420, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.o114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"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.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[46]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[47]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-32; LYS-97; LYS-171; LYS-201;
LYS-208; LYS-219; LYS-233; LYS-260; LYS-270; LYS-311; LYS-366; LYS-378;
LYS-417; LYS-420; LYS-450; LYS-470; LYS-486 AND LYS-597, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-modification
with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[48]
INTERACTION WITH ITSN1 ISOFORM 2, AND SUBCELLULAR LOCATION.
PubMed=29599122; DOI=10.1042/bcj20170897;
Alvisi G., Paolini L., Contarini A., Zambarda C., Di Antonio V.,
Colosini A., Mercandelli N., Timmoneri M., Palu G., Caimi L., Ricotta D.,
Radeghieri A.;
"Intersectin goes nuclear: secret life of an endocytic protein.";
Biochem. J. 475:1455-1472(2018).
[49]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 435-552.
PubMed=11901143; DOI=10.1074/jbc.c200038200;
Dhe-Paganon S., Werner E.D., Chi Y.I., Shoelson S.E.;
"Structure of the globular tail of nuclear lamin.";
J. Biol. Chem. 277:17381-17384(2002).
[50]
STRUCTURE BY NMR OF 428-549.
PubMed=12057196; DOI=10.1016/s0969-2126(02)00777-3;
Krimm I., Ostlund C., Gilquin B., Couprie J., Hossenlopp P., Mornon J.-P.,
Bonne G., Courvalin J.-C., Worman H.J., Zinn-Justin S.;
"The Ig-like structure of the C-terminal domain of lamin A/C, mutated in
muscular dystrophies, cardiomyopathy, and partial lipodystrophy.";
Structure 10:811-823(2002).
[51]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 305-387.
PubMed=15476822; DOI=10.1016/j.jmb.2004.08.093;
Strelkov S.V., Schumacher J., Burkhard P., Aebi U., Herrmann H.;
"Crystal structure of the human lamin A coil 2B dimer: implications for the
head-to-tail association of nuclear lamins.";
J. Mol. Biol. 343:1067-1080(2004).
[52]
VARIANTS EDMD2 TRP-453; PRO-527 AND PRO-530, AND FUNCTION.
PubMed=10080180; DOI=10.1038/6799;
Bonne G., Di Barletta M.R., Varnous S., Becane H.-M., Hammouda E.-H.,
Merlini L., Muntoni F., Greenberg C.R., Gary F., Urtizberea J.-A.,
Duboc D., Fardeau M., Toniolo D., Schwartz K.;
"Mutations in the gene encoding lamin A/C cause autosomal dominant Emery-
Dreifuss muscular dystrophy.";
Nat. Genet. 21:285-288(1999).
[53]
VARIANTS CMD1A GLY-60; ARG-85; LYS-195 AND GLY-203, AND FUNCTION.
PubMed=10580070; DOI=10.1056/nejm199912023412302;
Fatkin D., MacRae C., Sasaki T., Wolff M.R., Porcu M., Frenneaux M.,
Atherton J., Vidaillet H.J. Jr., Spudich S., De Girolami U., Seidman J.G.,
Seidman C.E.;
"Missense mutations in the rod domain of the lamin A/C gene as causes of
dilated cardiomyopathy and conduction-system disease.";
N. Engl. J. Med. 341:1715-1724(1999).
[54]
VARIANTS FPLD2 ASP-465; GLN-482; TRP-482 AND HIS-582.
PubMed=10739751; DOI=10.1086/302836;
Speckman R.A., Garg A., Du F., Bennett L., Veile R., Arioglu E.,
Taylor S.I., Lovett M., Bowcock A.M.;
"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.";
Am. J. Hum. Genet. 66:1192-1198(2000).
[55]
ERRATUM OF PUBMED:10739751.
Speckman R.A., Garg A., Du F., Bennett L., Veile R., Arioglu E.,
Taylor S.I., Lovett M., Bowcock A.M.;
Am. J. Hum. Genet. 67:775-775(2000).
[56]
VARIANTS EDMD2 TYR-222; GLN-249; GLN-336; TRP-453; THR-469; PRO-527 AND
LYS-528.
PubMed=10739764; DOI=10.1086/302869;
Raffaele di Barletta M., Ricci E., Galluzzi G., Tonali P., Mora M.,
Morandi L., Romorini A., Voit T., Orstavik K.H., Merlini L., Trevisan C.,
Biancalana V., Housmanowa-Petrusewicz I., Bione S., Ricotti R.,
Schwartz K., Bonne G., Toniolo D.;
"Different mutations in the LMNA gene cause autosomal dominant and
autosomal recessive Emery-Dreifuss muscular dystrophy.";
Am. J. Hum. Genet. 66:1407-1412(2000).
[57]
VARIANTS EDMD2 CYS-45; PRO-50; SER-63; GLU-112 DEL; PRO-222; GLU-232;
GLN-249; LYS-261 DEL; PRO-294; LYS-358; LYS-371; LYS-386; TRP-453; LYS-456;
SER-520; PRO-527 AND LYS-528.
PubMed=10939567;
DOI=10.1002/1531-8249(200008)48:2<170::aid-ana6>3.0.co;2-j;
Bonne G., Mercuri E., Muchir A., Urtizberea A., Becane H.M., Recan D.,
Merlini L., Wehnert M., Boor R., Reuner U., Vorgerd M., Wicklein E.M.,
Eymard B., Duboc D., Penisson-Besnier I., Cuisset J.M., Ferrer X.,
Desguerre I., Lacombe D., Bushby K., Pollitt C., Toniolo D., Fardeau M.,
Schwartz K., Muntoni F.;
"Clinical and molecular genetic spectrum of autosomal dominant Emery-
Dreifuss muscular dystrophy due to mutations of the lamin A/C gene.";
Ann. Neurol. 48:170-180(2000).
[58]
VARIANT FPLD2 GLN-482.
PubMed=10587585; DOI=10.1093/hmg/9.1.109;
Cao H., Hegele R.A.;
"Nuclear lamin A/C R482Q mutation in Canadian kindreds with Dunnigan-type
familial partial lipodystrophy.";
Hum. Mol. Genet. 9:109-112(2000).
[59]
VARIANTS EDMD2 LYS-208 DEL AND HIS-377, AND FUNCTION.
PubMed=10814726; DOI=10.1093/hmg/9.9.1453;
Muchir A., Bonne G., van der Kooi A.J., van Meegen M., Baas F.,
Bolhuis P.A., de Visser M., Schwartz K.;
"Identification of mutations in the gene encoding lamins A/C in autosomal
dominant limb girdle muscular dystrophy with atrioventricular conduction
disturbances (LGMD1B).";
Hum. Mol. Genet. 9:1453-1459(2000).
[60]
VARIANTS FPLD2 LEU-482 AND TRP-482.
PubMed=10655060; DOI=10.1038/72807;
Shackleton S., Lloyd D.J., Jackson S.N.J., Evans R., Niermeijer M.F.,
Singh B.M., Schmidt H., Brabant G., Kumar S., Durrington P.N., Gregory S.,
O'Rahilly S., Trembath R.C.;
"LMNA, encoding lamin A/C, is mutated in partial lipodystrophy.";
Nat. Genet. 24:153-156(2000).
[61]
VARIANTS EDMD2 PRO-150 AND LYS-261 DEL.
PubMed=10908904; DOI=10.1212/wnl.55.2.275;
Felice K.J., Schwartz R.C., Brown C.A., Leicher C.R., Grunnet M.L.;
"Autosomal dominant Emery-Dreifuss dystrophy due to mutations in rod domain
of the lamin A/C gene.";
Neurology 55:275-280(2000).
[62]
VARIANTS EDMD2 PRO-25; THR-43; SER-50; PRO-133; 196-ARG--THR-199 DELINS
SER; GLN-249; LYS-261 DEL; LYS-358; TRP-453; ILE-456; PRO-527 AND HIS-624.
PubMed=11503164; DOI=10.1002/ajmg.1463;
Brown C.A., Lanning R.W., McKinney K.Q., Salvino A.R., Cherniske E.,
Crowe C.A., Darras B.T., Gominak S., Greenberg C.R., Grosmann C.,
Heydemann P., Mendell J.R., Pober B.R., Sasaki T., Shapiro F.,
Simpson D.A., Suchowersky O., Spence J.E.;
"Novel and recurrent mutations in lamin A/C in patients with Emery-Dreifuss
muscular dystrophy.";
Am. J. Med. Genet. 102:359-367(2001).
[63]
VARIANT CMD1A LYS-203.
PubMed=11561226; DOI=10.1054/jcaf.2001.26339;
Jakobs P.M., Hanson E.L., Crispell K.A., Toy W., Keegan H., Schilling K.,
Icenogle T.B., Litt M., Hershberger R.E.;
"Novel lamin A/C mutations in two families with dilated cardiomyopathy and
conduction system disease.";
J. Card. Fail. 7:249-256(2001).
[64]
CHARACTERIZATION OF VARIANTS CMD1A GLY-60; ARG-85; LYS-195 AND GLY-203,
CHARACTERIZATION OF VARIANTS EDMD2 LYS-358; LYS-371; LYS-386; TRP-453;
SER-520; PRO-527; LYS-528 AND PRO-530, AND CHARACTERIZATION OF VARIANTS
FPLD2 GLN-482; TRP-482 AND ASN-486.
PubMed=11792809;
Oestlund C., Bonne G., Schwartz K., Worman H.J.;
"Properties of lamin A mutants found in Emery-Dreifuss muscular dystrophy,
cardiomyopathy and Dunnigan-type partial lipodystrophy.";
J. Cell Sci. 114:4435-4445(2001).
[65]
VARIANT EDMD2 HIS-481.
PubMed=11525883; DOI=10.1016/s0960-8966(01)00207-3;
Kitaguchi T., Matsubara S., Sato M., Miyamoto K., Hirai S., Schwartz K.,
Bonne G.;
"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.";
Neuromuscul. Disord. 11:542-546(2001).
[66]
VARIANT CMD1A PRO-215.
PubMed=12486434; DOI=10.1067/mhj.2002.126737;
Hershberger R.E., Hanson E.L., Jakobs P.M., Keegan H., Coates K.,
Bousman S., Litt M.;
"A novel lamin A/C mutation in a family with dilated cardiomyopathy,
prominent conduction system disease, and need for permanent pacemaker
implantation.";
Am. Heart J. 144:1081-1086(2002).
[67]
VARIANT CMT2B1 CYS-298, AND FUNCTION.
PubMed=11799477; DOI=10.1086/339274;
De Sandre-Giovannoli A., Chaouch M., Kozlov S., Vallat J.-M., Tazir M.,
Kassouri N., Szepetowski P., Hammadouche T., Vandenberghe A., Stewart C.L.,
Grid D., Levy N.;
"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.";
Am. J. Hum. Genet. 70:726-736(2002).
[68]
ERRATUM OF PUBMED:11799477.
De Sandre-Giovannoli A., Chaouch M., Kozlov S., Vallat J.-M., Tazir M.,
Kassouri N., Szepetowski P., Hammadouche T., Vandenberghe A., Stewart C.L.,
Grid D., Levy N.;
Am. J. Hum. Genet. 70:1075-1075(2002).
[69]
VARIANT MADA HIS-527, AND FUNCTION.
PubMed=12075506; DOI=10.1086/341908;
Novelli G., Muchir A., Sangiuolo F., Helbling-Leclerc A., D'Apice M.R.,
Massart C., Capon F., Sbraccia P., Federici M., Lauro R., Tudisco C.,
Pallotta R., Scarano G., Dallapiccola B., Merlini L., Bonne G.;
"Mandibuloacral dysplasia is caused by a mutation in LMNA-encoding lamin
A/C.";
Am. J. Hum. Genet. 71:426-431(2002).
[70]
VARIANTS FPLD2 TRP-28 AND GLY-62.
PubMed=12015247; DOI=10.1016/s0002-9343(02)01070-7;
Garg A., Speckman R.A., Bowcock A.M.;
"Multisystem dystrophy syndrome due to novel missense mutations in the
amino-terminal head and alpha-helical rod domains of the lamin A/C gene.";
Am. J. Med. 112:549-555(2002).
[71]
VARIANTS CMD1A GLU-97; TRP-190 AND LYS-317.
PubMed=11897440; DOI=10.1016/s0735-1097(02)01724-2;
Arbustini E., Pilotto A., Repetto A., Grasso M., Negri A., Diegoli M.,
Campana C., Scelsi L., Baldini E., Gavazzi A., Tavazzi L.;
"Autosomal dominant dilated cardiomyopathy with atrioventricular block: a
lamin A/C defect-related disease.";
J. Am. Coll. Cardiol. 39:981-990(2002).
[72]
VARIANT EDMD2 GLN-249, AND VARIANT EDMD2 LEU-377.
PubMed=12032588; DOI=10.1007/s100380200029;
Ki C.-S., Hong J.S., Jeong G.-Y., Ahn K.J., Choi K.-M., Kim D.-K.,
Kim J.-W.;
"Identification of lamin A/C (LMNA) gene mutations in Korean patients with
autosomal dominant Emery-Dreifuss muscular dystrophy and limb-girdle
muscular dystrophy 1B.";
J. Hum. Genet. 47:225-228(2002).
[73]
VARIANTS FPLD2 GLY-60 AND PRO-527.
PubMed=12196663; DOI=10.1212/wnl.59.4.620;
van der Kooi A.J., Bonne G., Eymard B., Duboc D., Talim B.,
Van der Valk M., Reiss P., Richard P., Demay L., Merlini L., Schwartz K.,
Busch H.F.M., de Visser M.;
"Lamin A/C mutations with lipodystrophy, cardiac abnormalities, and
muscular dystrophy.";
Neurology 59:620-623(2002).
[74]
VARIANTS EDMD2 LYS-32 DEL; ASN-63; GLN-336; GLN-343 AND CYS-401.
PubMed=12467752; DOI=10.1016/s0960-8966(02)00178-5;
Vytopil M., Ricci E., Dello Russo A., Hanisch F., Neudecker S., Zierz S.,
Ricotti R., Demay L., Richard P., Wehnert M., Bonne G., Merlini L.,
Toniolo D.;
"Frequent low penetrance mutations in the Lamin A/C gene, causing Emery
Dreifuss muscular dystrophy.";
Neuromuscul. Disord. 12:958-963(2002).
[75]
VARIANT CMD1A CYS-541.
PubMed=14675861; DOI=10.1016/s1388-9842(03)00149-1;
Forissier J.-F., Bonne G., Bouchier C., Duboscq-Bidot L., Richard P.,
Wisnewski C., Briault S., Moraine C., Dubourg O., Schwartz K., Komajda M.;
"Apical left ventricular aneurysm without atrio-ventricular block due to a
lamin A/C gene mutation.";
Eur. J. Heart Fail. 5:821-825(2003).
[76]
VARIANT EDMD2 HIS-377.
PubMed=12673789; DOI=10.1002/humu.10170;
Charniot J.-C., Pascal C., Bouchier C., Sebillon P., Salama J.,
Duboscq-Bidot L., Peuchmaurd M., Desnos M., Artigou J.-Y., Komajda M.;
"Functional consequences of an LMNA mutation associated with a new cardiac
and non-cardiac phenotype.";
Hum. Mutat. 21:473-481(2003).
[77]
VARIANTS CMD1A LEU-89; HIS-377 AND LEU-573.
PubMed=12628721; DOI=10.1016/s0735-1097(02)02954-6;
Familial dilated cardiomyopathy registry research group;
Taylor M.R.G., Fain P.R., Sinagra G., Robinson M.L., Robertson A.D.,
Carniel E., Di Lenarda A., Bohlmeyer T.J., Ferguson D.A., Brodsky G.L.,
Boucek M.M., Lascor J., Moss A.C., Li W.-L.P., Stetler G.L., Muntoni F.,
Bristow M.R., Mestroni L.;
"Natural history of dilated cardiomyopathy due to lamin A/C gene
mutations.";
J. Am. Coll. Cardiol. 41:771-780(2003).
[78]
ERRATUM OF PUBMED:12628721.
Familial dilated cardiomyopathy registry research group;
Taylor M.R.G., Fain P.R., Sinagra G., Robinson M.L., Robertson A.D.,
Carniel E., Di Lenarda A., Bohlmeyer T.J., Ferguson D.A., Brodsky G.L.,
Boucek M.M., Lascor J., Moss A.C., Li W.-L.P., Stetler G.L., Muntoni F.,
Bristow M.R., Mestroni L.;
J. Am. Coll. Cardiol. 42:590-590(2003).
[79]
VARIANT FPLD2 LEU-133.
PubMed=12629077; DOI=10.1210/jc.2002-021506;
Caux F., Dubosclard E., Lascols O., Buendia B., Chazouilleres O., Cohen A.,
Courvalin J.-C., Laroche L., Capeau J., Vigouroux C., Christin-Maitre S.;
"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.";
J. Clin. Endocrinol. Metab. 88:1006-1013(2003).
[80]
VARIANTS HGPS CYS-471; CYS-527 AND SER-608.
PubMed=12768443; DOI=10.1007/s10038-003-0025-3;
Cao H., Hegele R.A.;
"LMNA is mutated in Hutchinson-Gilford progeria (MIM 176670) but not in
Wiedemann-Rautenstrauch progeroid syndrome (MIM 264090).";
J. Hum. Genet. 48:271-274(2003).
[81]
VARIANT CMD1A LYS-161.
PubMed=12920062; DOI=10.1136/jmg.40.8.560;
Sebillon P., Bouchier C., Bidot L.D., Bonne G., Ahamed K., Charron P.,
Drouin-Garraud V., Millaire A., Desrumeaux G., Benaiche A., Charniot J.-C.,
Schwartz K., Villard E., Komajda M.;
"Expanding the phenotype of LMNA mutations in dilated cardiomyopathy and
functional consequences of these mutations.";
J. Med. Genet. 40:560-567(2003).
[82]
VARIANTS EDMD2 GLY-25; LYS-32 DEL; VAL-35; GLY-65; GLU-112 DEL; PRO-248;
GLN-249; CYS-267; VAL-446; TRP-453; ARG-528 AND HIS-541, AND VARIANT CMD1A
CYS-435.
PubMed=14684700; DOI=10.1136/jmg.40.12.e132;
Vytopil M., Benedetti S., Ricci E., Galluzzi G., Dello Russo A.,
Merlini L., Boriani G., Gallina M., Morandi L., Politano L., Moggio M.,
Chiveri L., Hausmanova-Petrusewicz I., Ricotti R., Vohanka S., Toman J.,
Toniolo D.;
"Mutation analysis of the lamin A/C gene (LMNA) among patients with
different cardiomuscular phenotypes.";
J. Med. Genet. 40:E132-E132(2003).
[83]
VARIANT CMDHH PRO-57, VARIANT HGPS ARG-140, AND FUNCTION.
PubMed=12927431; DOI=10.1016/s0140-6736(03)14069-x;
Chen L., Lee L., Kudlow B.A., Dos Santos H.G., Sletvold O., Shafeghati Y.,
Botha E.G., Garg A., Hanson N.B., Martin G.M., Mian I.S., Kennedy B.K.,
Oshima J.;
"LMNA mutations in atypical Werner's syndrome.";
Lancet 362:440-445(2003).
[84]
VARIANTS EDMD2 ASN-63; PRO-140; GLN-249; LEU-377; LYS-386 AND PRO-527.
PubMed=12649505; DOI=10.1161/01.str.0000064322.47667.49;
Boriani G., Gallina M., Merlini L., Bonne G., Toniolo D., Amati S.,
Biffi M., Martignani C., Frabetti L., Bonvicini M., Rapezzi C., Branzi A.;
"Clinical relevance of atrial fibrillation/flutter, stroke, pacemaker
implant, and heart failure in Emery-Dreifuss muscular dystrophy: a long-
term longitudinal study.";
Stroke 34:901-908(2003).
[85]
VARIANTS CMD1A TRP-190 AND LEU-349.
PubMed=15219508; DOI=10.1016/j.amjcard.2004.03.029;
Hermida-Prieto M., Monserrat L., Castro-Beiras A., Laredo R., Soler R.,
Peteiro J., Rodriguez E., Bouzas B., Alvarez N., Muniz J., Crespo-Leiro M.;
"Familial dilated cardiomyopathy and isolated left ventricular
noncompaction associated with lamin A/C gene mutations.";
Am. J. Cardiol. 94:50-54(2004).
[86]
VARIANT CMD1A PRO-143.
PubMed=15140538; DOI=10.1016/j.ehj.2004.01.020;
Kaerkkaeinen S., Helioe T., Miettinen R., Tuomainen P., Peltola P.,
Rummukainen J., Ylitalo K., Kaartinen M., Kuusisto J., Toivonen L.,
Nieminen M.S., Laakso M., Peuhkurinen K.;
"A novel mutation, Ser143Pro, in the lamin A/C gene is common in Finnish
patients with familial dilated cardiomyopathy.";
Eur. Heart J. 25:885-893(2004).
[87]
INVOLVEMENT IN LTSCS, AND FUNCTION.
PubMed=15317753; DOI=10.1093/hmg/ddh265;
Navarro C.L., De Sandre-Giovannoli A., Bernard R., Boccaccio I., Boyer A.,
Genevieve D., Hadj-Rabia S., Gaudy-Marqueste C., Smitt H.S., Vabres P.,
Faivre L., Verloes A., Van Essen T., Flori E., Hennekam R., Beemer F.A.,
Laurent N., Le Merrer M., Cau P., Levy N.;
"Lamin A and ZMPSTE24 (FACE-1) defects cause nuclear disorganization and
identify restrictive dermopathy as a lethal neonatal laminopathy.";
Hum. Mol. Genet. 13:2493-2503(2004).
[88]
VARIANT HGPS CYS-644, AND VARIANTS ILE-10 AND VAL-578.
PubMed=15060110; DOI=10.1136/jmg.2003.015651;
Csoka A.B., Cao H., Sammak P.J., Constantinescu D., Schatten G.P.,
Hegele R.A.;
"Novel lamin A/C gene (LMNA) mutations in atypical progeroid syndromes.";
J. Med. Genet. 41:304-308(2004).
[89]
VARIANT HGPS ASN-542.
PubMed=15286156; DOI=10.1136/jmg.2004.019661;
Plasilova M., Chattopadhyay C., Pal P., Schaub N.A., Buechner S.A.,
Mueller H., Miny P., Ghosh A., Heinimann K.;
"Homozygous missense mutation in the lamin A/C gene causes autosomal
recessive Hutchinson-Gilford progeria syndrome.";
J. Med. Genet. 41:609-614(2004).
[90]
VARIANT CMT2 ASP-33, AND VARIANT EDMD2 GLY-33.
PubMed=14985400; DOI=10.1136/jmg.2003.013383;
Goizet C., Yaou R.B., Demay L., Richard P., Bouillot S., Rouanet M.,
Hermosilla E., Le Masson G., Lagueny A., Bonne G., Ferrer X.;
"A new mutation of the lamin A/C gene leading to autosomal dominant axonal
neuropathy, muscular dystrophy, cardiac disease, and leuconychia.";
J. Med. Genet. 41:E29-E29(2004).
[91]
SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS EDMD2 LYS-32 DEL;
SER-63; GLN-249; LYS-358; CYS-401; TRP-453 AND PRO-527, CHARACTERIZATION OF
VARIANTS EDMD2 LYS-208 DEL AND HIS-377, CHARACTERIZATION OF VARIANT FPLD2
LEU-482, AND CHARACTERIZATION OF VARIANT CMD1A CYS-541.
PubMed=15372542; DOI=10.1002/mus.20122;
Muchir A., Medioni J., Laluc M., Massart C., Arimura T., van der Kooi A.J.,
Desguerre I., Mayer M., Ferrer X., Briault S., Hirano M., Worman H.J.,
Mallet A., Wehnert M., Schwartz K., Bonne G.;
"Nuclear envelope alterations in fibroblasts from patients with muscular
dystrophy, cardiomyopathy, and partial lipodystrophy carrying lamin A/C
gene mutations.";
Muscle Nerve 30:444-450(2004).
[92]
VARIANT HGPS PHE-143.
PubMed=15622532; DOI=10.1002/ana.20359;
Kirschner J., Brune T., Wehnert M., Denecke J., Wasner C., Feuer A.,
Marquardt T., Ketelsen U.-P., Wieacker P., Boennemann C.G.,
Korinthenberg R.;
"p.S143F mutation in lamin A/C: a new phenotype combining myopathy and
progeria.";
Ann. Neurol. 57:148-151(2005).
[93]
VARIANT CMDA1 ASN-260.
PubMed=16156025;
Arbustini Eloisa A.E., Pilotto A., Pasotti M., Grasso M., Diegoli M.,
Campana C., Gavazzi A., Alessandra R., Tavazzi L.;
"Gene symbol: LMNA. Disease: cardiomyopathy, dilated, with conduction
defect 1.";
Hum. Genet. 117:298-298(2005).
[94]
VARIANT MADA VAL-529.
PubMed=15998779; DOI=10.1210/jc.2004-2560;
Garg A., Cogulu O., Ozkinay F., Onay H., Agarwal A.K.;
"A novel homozygous Ala529Val LMNA mutation in Turkish patients with
mandibuloacral dysplasia.";
J. Clin. Endocrinol. Metab. 90:5259-5264(2005).
[95]
VARIANT EDMD2 HIS-377, AND VARIANTS EDMD2 ASN-63; PRO-140; GLN-190; GLN-249
AND PRO-527.
PubMed=15744034; DOI=10.1136/jmg.2004.026112;
Cenni V., Sabatelli P., Mattioli E., Marmiroli S., Capanni C., Ognibene A.,
Squarzoni S., Maraldi N.M., Bonne G., Columbaro M., Merlini L.,
Lattanzi G.;
"Lamin A N-terminal phosphorylation is associated with myoblast activation:
impairment in Emery-Dreifuss muscular dystrophy.";
J. Med. Genet. 42:214-220(2005).
[96]
VARIANT MADA LEU-573.
PubMed=16278265; DOI=10.1210/jc.2005-1297;
Van Esch H., Agarwal A.K., Debeer P., Fryns J.-P., Garg A.;
"A homozygous mutation in the lamin A/C gene associated with a novel
syndrome of arthropathy, tendinous calcinosis, and progeroid features.";
J. Clin. Endocrinol. Metab. 91:517-521(2006).
[97]
VARIANT CMDHH ARG-59.
PubMed=17150192; DOI=10.1016/j.bbrc.2006.11.070;
Nguyen D., Leistritz D.F., Turner L., MacGregor D., Ohson K., Dancey P.,
Martin G.M., Oshima J.;
"Collagen expression in fibroblasts with a novel LMNA mutation.";
Biochem. Biophys. Res. Commun. 352:603-608(2007).
[98]
VARIANTS FPLD2 ASN-230; CYS-399 AND LEU-573.
PubMed=17250669; DOI=10.1111/j.1399-0004.2007.00740.x;
Lanktree M., Cao H., Rabkin S.W., Hanna A., Hegele R.A.;
"Novel LMNA mutations seen in patients with familial partial lipodystrophy
subtype 2 (FPLD2; MIM 151660).";
Clin. Genet. 71:183-186(2007).
[99]
VARIANT EDMD2 HIS-377.
PubMed=17136397; DOI=10.1007/s10048-006-0070-0;
Rudnik-Schoeneborn S., Botzenhart E., Eggermann T., Senderek J.,
Schoser B.G.H., Schroeder R., Wehnert M., Wirth B., Zerres K.;
"Mutations of the LMNA gene can mimic autosomal dominant proximal spinal
muscular atrophy.";
Neurogenetics 8:137-142(2007).
[100]
VARIANT PRO-421.
PubMed=17711925; DOI=10.1210/jc.2007-0654;
Decaudain A., Vantyghem M.C., Guerci B., Hecart A.C., Auclair M.,
Reznik Y., Narbonne H., Ducluzeau P.H., Donadille B., Lebbe C.,
Bereziat V., Capeau J., Lascols O., Vigouroux C.;
"New metabolic phenotypes in laminopathies: LMNA mutations in patients with
severe metabolic syndrome.";
J. Clin. Endocrinol. Metab. 92:4835-4844(2007).
[101]
VARIANTS MDCL SER-39; PRO-50; TRP-249; PRO-302; LYS-358; SER-380; PRO-453;
PRO-455 AND ASP-456.
PubMed=18551513; DOI=10.1002/ana.21417;
Quijano-Roy S., Mbieleu B., Bonnemann C.G., Jeannet P.Y., Colomer J.,
Clarke N.F., Cuisset J.M., Roper H., De Meirleir L., D'Amico A.,
Ben Yaou R., Nascimento A., Barois A., Demay L., Bertini E., Ferreiro A.,
Sewry C.A., Romero N.B., Ryan M., Muntoni F., Guicheney P., Richard P.,
Bonne G., Estournet B.;
"De novo LMNA mutations cause a new form of congenital muscular
dystrophy.";
Ann. Neurol. 64:177-186(2008).
[102]
INVOLVEMENT IN HHS-SLOVENIAN, AND FUNCTION.
PubMed=18611980; DOI=10.1136/jmg.2008.060020;
Renou L., Stora S., Yaou R.B., Volk M., Sinkovec M., Demay L., Richard P.,
Peterlin B., Bonne G.;
"Heart-hand syndrome of Slovenian type: a new kind of laminopathy.";
J. Med. Genet. 45:666-671(2008).
[103]
FUNCTION, INTERACTION WITH IFFO1, SUBCELLULAR LOCATION, MUTAGENESIS OF
SER-22; GLU-358 AND ARG-386, AND REGION.
PubMed=31548606; DOI=10.1038/s41556-019-0388-0;
Li W., Bai X., Li J., Zhao Y., Liu J., Zhao H., Liu L., Ding M., Wang Q.,
Shi F.Y., Hou M., Ji J., Gao G., Guo R., Sun Y., Liu Y., Xu D.;
"The nucleoskeleton protein IFFO1 immobilizes broken DNA and suppresses
chromosome translocation during tumorigenesis.";
Nat. Cell Biol. 21:1273-1285(2019).
[104]
VARIANT CMDHH ARG-59.
PubMed=19283854; DOI=10.1002/ajmg.a.32627;
McPherson E., Turner L., Zador I., Reynolds K., Macgregor D.,
Giampietro P.F.;
"Ovarian failure and dilated cardiomyopathy due to a novel lamin
mutation.";
Am. J. Med. Genet. A 149:567-572(2009).
[105]
VARIANTS SER-125; ILE-415 AND PRO-488.
PubMed=19427440; DOI=10.1016/j.amjcard.2009.01.354;
Brauch K.M., Chen L.Y., Olson T.M.;
"Comprehensive mutation scanning of LMNA in 268 patients with lone atrial
fibrillation.";
Am. J. Cardiol. 103:1426-1428(2009).
[106]
VARIANT CMD1A CYS-541.
PubMed=19167105; DOI=10.1016/j.ijcard.2008.12.083;
Saj M., Jankowska A., Lewandowski M., Szwed H., Szperl M., Ploski R.,
Bilinska Z.T.;
"Dilated cardiomyopathy with profound segmental wall motion abnormalities
and ventricular arrhythmia caused by the R541C mutation in the LMNA gene.";
Int. J. Cardiol. 144:E51-E53(2010).
[107]
VARIANTS CMD1A PHE-92; LYS-161; LYS-317 AND ARG-523.
PubMed=21846512; DOI=10.1016/j.ejmg.2011.07.005;
Millat G., Bouvagnet P., Chevalier P., Sebbag L., Dulac A., Dauphin C.,
Jouk P.S., Delrue M.A., Thambo J.B., Le Metayer P., Seronde M.F.,
Faivre L., Eicher J.C., Rousson R.;
"Clinical and mutational spectrum in a cohort of 105 unrelated patients
with dilated cardiomyopathy.";
Eur. J. Med. Genet. 54:E570-E575(2011).
[108]
VARIANT HGPS LYS-138.
PubMed=21791255; DOI=10.1016/j.ejmg.2011.06.012;
Gonzalez-Quereda L., Delgadillo V., Juan-Mateu J., Verdura E.,
Rodriguez M.J., Baiget M., Pineda M., Gallano P.;
"LMNA mutation in progeroid syndrome in association with strokes.";
Eur. J. Med. Genet. 54:E576-E579(2011).
[109]
VARIANTS EDMD2 SER-39; CYS-45; PRO-150; PRO-189; ARG-190 INS; LEU-206;
TRP-249; GLN-249; PRO-268; PRO-271; PRO-294; PRO-295; PRO-303; GLN-355 DEL;
LYS-358; LYS-361; LYS-386; ASP-449; TRP-453; PRO-454; TYR-461; ARG-467;
PRO-527; LYS-528; ARG-528; SER-541; PRO-541; SER-602 AND CYS-644, AND
CHARACTERIZATION OF VARIANTS EDMD2 PRO-25; TRP-249; ILE-456 AND PRO-541.
PubMed=20848652; DOI=10.1002/humu.21361;
Scharner J., Brown C.A., Bower M., Iannaccone S.T., Khatri I.A.,
Escolar D., Gordon E., Felice K., Crowe C.A., Grosmann C., Meriggioli M.N.,
Asamoah A., Gordon O., Gnocchi V.F., Ellis J.A., Mendell J.R., Zammit P.S.;
"Novel LMNA mutations in patients with Emery-Dreifuss muscular dystrophy
and functional characterization of four LMNA mutations.";
Hum. Mutat. 32:152-167(2011).
[110]
VARIANTS ASP-411 AND ASP-631.
PubMed=21724554; DOI=10.1093/hmg/ddr294;
Dutour A., Roll P., Gaborit B., Courrier S., Alessi M.C., Tregouet D.A.,
Angelis F., Robaglia-Schlupp A., Lesavre N., Cau P., Levy N., Badens C.,
Morange P.E.;
"High prevalence of laminopathies among patients with metabolic syndrome.";
Hum. Mol. Genet. 20:3779-3786(2011).
[111]
VARIANT EDMD3 GLN-225, AND FUNCTION.
PubMed=22431096; DOI=10.1002/mus.22324;
Jimenez-Escrig A., Gobernado I., Garcia-Villanueva M., Sanchez-Herranz A.;
"Autosomal recessive Emery-Dreifuss muscular dystrophy caused by a novel
mutation (R225Q) in the lamin A/C gene identified by exome sequencing.";
Muscle Nerve 45:605-610(2012).
[112]
CHARACTERIZATION OF VARIANTS CYS-401; ASP-411; CYS-413; ILE-415; CYS-419;
PRO-421 AND GLY-427, AND INTERACTION WITH SYNE2.
PubMed=23977161; DOI=10.1371/journal.pone.0071850;
Yang L., Munck M., Swamvdinathan K., Kapinos L.E., Noegel A.A., Neumann S.;
"Mutations in LMNA modulate the lamin A--Nesprin-2 interaction and cause
LINC complex alterations.";
PLoS ONE 8:E71850-E71850(2013).
[113]
VARIANT FPLD2 GLU-515.
PubMed=24485160; DOI=10.1016/j.diabet.2013.12.008;
Chirico V., Ferrau V., Loddo I., Briuglia S., Amorini M., Salpietro V.,
Lacquaniti A., Salpietro C., Arrigo T.;
"LMNA gene mutation as a model of cardiometabolic dysfunction: from genetic
analysis to treatment response.";
Diabetes Metab. 40:224-228(2014).
[114]
VARIANT EDMD3 SER-24, AND VARIANT EDMD2 CYS-259.
PubMed=27234031; DOI=10.1111/cge.12810;
Fattahi Z., Kalhor Z., Fadaee M., Vazehan R., Parsimehr E., Abolhassani A.,
Beheshtian M., Zamani G., Nafissi S., Nilipour Y., Akbari M.R., Kahrizi K.,
Kariminejad A., Najmabadi H.;
"Improved diagnostic yield of neuromuscular disorders applying clinical
exome sequencing in patients arising from a consanguineous population.";
Clin. Genet. 91:386-402(2017).
-!- FUNCTION: Lamins are components of the nuclear lamina, a fibrous layer
on the nucleoplasmic side of the inner nuclear membrane, which is
thought to provide a framework for the nuclear envelope and may also
interact with chromatin. Lamin A and C are present in equal amounts in
the lamina of mammals. 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). Plays
an important role in nuclear assembly, chromatin organization, nuclear
membrane and telomere dynamics. Required for normal development of
peripheral nervous system and skeletal muscle and for muscle satellite
cell proliferation (PubMed:10080180, PubMed:22431096, PubMed:10814726,
PubMed:11799477, PubMed:18551513). 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:22431096, ECO:0000269|PubMed:23666920,
ECO:0000269|PubMed:31548606}.
-!- FUNCTION: Prelamin-A/C can accelerate smooth muscle cell senescence. It
acts to disrupt mitosis and induce DNA damage in vascular smooth muscle
cells (VSMCs), leading to mitotic failure, genomic instability, and
premature senescence.
-!- SUBUNIT: Homodimer of lamin A and lamin C. Interacts with lamin-
associated polypeptides IA, IB and TMPO-alpha, RB1 and with emerin.
Interacts with SREBF1, SREBF2, SUN2 and TMEM43. Interacts with TMEM201
(By similarity). Proteolytically processed isoform A interacts with
NARF. Interacts with SUN1. Prelamin-A/C interacts with EMD. Interacts
with MLIP. Interacts with DMPK; may regulate nuclear envelope
stability. Interacts with SUV39H1; the interaction increases stability
of SUV39H1. Interacts with SYNE2. Interacts with ITSN1 isoform 2
(PubMed:29599122). Interacts with IFFO1; enables the formation of an
interior nucleoskeleton that is recruited to DNA double-strand breaks
(PubMed:31548606). {ECO:0000250, ECO:0000269|PubMed:10514485,
ECO:0000269|PubMed:12475961, ECO:0000269|PubMed:19323649,
ECO:0000269|PubMed:19933576, ECO:0000269|PubMed:21498514,
ECO:0000269|PubMed:21949239, ECO:0000269|PubMed:23695662,
ECO:0000269|PubMed:23977161, ECO:0000269|PubMed:29599122,
ECO:0000269|PubMed:31548606}.
-!- INTERACTION:
P02545; Q6H8Q1-8: ABLIM2; NbExp=3; IntAct=EBI-351935, EBI-16436655;
P02545; P18054: ALOX12; NbExp=4; IntAct=EBI-351935, EBI-1633210;
P02545; Q96DX5: ASB9; NbExp=3; IntAct=EBI-351935, EBI-745641;
P02545; Q8WXF7: ATL1; NbExp=3; IntAct=EBI-351935, EBI-2410266;
P02545; P46379-2: BAG6; NbExp=3; IntAct=EBI-351935, EBI-10988864;
P02545; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-351935, EBI-742750;
P02545; Q9ULD4-2: BRPF3; NbExp=3; IntAct=EBI-351935, EBI-23662416;
P02545; Q96GN5-2: CDCA7L; NbExp=3; IntAct=EBI-351935, EBI-9091443;
P02545; Q9UII6: DUSP13; NbExp=7; IntAct=EBI-351935, EBI-749800;
P02545; P50402: EMD; NbExp=6; IntAct=EBI-351935, EBI-489887;
P02545; Q3B820: FAM161A; NbExp=3; IntAct=EBI-351935, EBI-719941;
P02545; A6H8Z2-3: FAM221B; NbExp=3; IntAct=EBI-351935, EBI-25843965;
P02545; P58499: FAM3B; NbExp=3; IntAct=EBI-351935, EBI-12955347;
P02545; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-351935, EBI-8468186;
P02545; Q8NEA9: GMCL2; NbExp=3; IntAct=EBI-351935, EBI-745707;
P02545; P16104: H2AX; NbExp=3; IntAct=EBI-351935, EBI-494830;
P02545; Q71DI3: H3C15; NbExp=6; IntAct=EBI-351935, EBI-750650;
P02545; Q0D2I5-5: IFFO1; NbExp=4; IntAct=EBI-351935, EBI-21251044;
P02545; Q13123: IK; NbExp=3; IntAct=EBI-351935, EBI-713456;
P02545; Q14005-2: IL16; NbExp=3; IntAct=EBI-351935, EBI-17178971;
P02545; Q96EL1: INKA1; NbExp=3; IntAct=EBI-351935, EBI-10285157;
P02545; Q8NA54: IQUB; NbExp=3; IntAct=EBI-351935, EBI-10220600;
P02545; Q99612: KLF6; NbExp=3; IntAct=EBI-351935, EBI-714994;
P02545; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-351935, EBI-10172290;
P02545; P20700: LMNB1; NbExp=10; IntAct=EBI-351935, EBI-968218;
P02545; Q03252: LMNB2; NbExp=6; IntAct=EBI-351935, EBI-2830427;
P02545; O76041: NEBL; NbExp=3; IntAct=EBI-351935, EBI-2880203;
P02545; Q12986: NFX1; NbExp=3; IntAct=EBI-351935, EBI-2130062;
P02545; Q9Y239: NOD1; NbExp=3; IntAct=EBI-351935, EBI-1051262;
P02545; Q13133-3: NR1H3; NbExp=3; IntAct=EBI-351935, EBI-11952806;
P02545; Q9BZ95-3: NSD3; NbExp=3; IntAct=EBI-351935, EBI-22002759;
P02545; Q6X4W1-6: NSMF; NbExp=3; IntAct=EBI-351935, EBI-25842707;
P02545; Q3SX64: ODF3L2; NbExp=3; IntAct=EBI-351935, EBI-6660184;
P02545; Q96RG2: PASK; NbExp=2; IntAct=EBI-351935, EBI-1042651;
P02545; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-351935, EBI-11022007;
P02545; Q96FA3: PELI1; NbExp=3; IntAct=EBI-351935, EBI-448369;
P02545; O75925: PIAS1; NbExp=3; IntAct=EBI-351935, EBI-629434;
P02545; Q03181-2: PPARD; NbExp=3; IntAct=EBI-351935, EBI-10223258;
P02545; Q9NWB1-5: RBFOX1; NbExp=3; IntAct=EBI-351935, EBI-12123390;
P02545; Q8TCX5: RHPN1; NbExp=3; IntAct=EBI-351935, EBI-746325;
P02545; Q8WVD3: RNF138; NbExp=3; IntAct=EBI-351935, EBI-749039;
P02545; P62701: RPS4X; NbExp=3; IntAct=EBI-351935, EBI-354303;
P02545; Q6ZNE9: RUFY4; NbExp=3; IntAct=EBI-351935, EBI-10181525;
P02545; Q8N488: RYBP; NbExp=3; IntAct=EBI-351935, EBI-752324;
P02545; Q8IYM2: SLFN12; NbExp=3; IntAct=EBI-351935, EBI-2822550;
P02545; Q13573: SNW1; NbExp=4; IntAct=EBI-351935, EBI-632715;
P02545; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-351935, EBI-5235340;
P02545; Q7Z698: SPRED2; NbExp=3; IntAct=EBI-351935, EBI-7082156;
P02545; O75886: STAM2; NbExp=3; IntAct=EBI-351935, EBI-373258;
P02545; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-351935, EBI-357085;
P02545; Q9UH99: SUN2; NbExp=4; IntAct=EBI-351935, EBI-1044964;
P02545; Q8WXH0-1: SYNE2; NbExp=3; IntAct=EBI-351935, EBI-6170976;
P02545; P54274-2: TERF1; NbExp=3; IntAct=EBI-351935, EBI-711018;
P02545; P42166: TMPO; NbExp=4; IntAct=EBI-351935, EBI-395393;
P02545; Q96KP6: TNIP3; NbExp=3; IntAct=EBI-351935, EBI-2509913;
P02545; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-351935, EBI-11525489;
P02545; Q5VYS8-5: TUT7; NbExp=3; IntAct=EBI-351935, EBI-9088812;
P02545; Q04323-2: UBXN1; NbExp=3; IntAct=EBI-351935, EBI-11530712;
P02545; Q9Y4E8-2: USP15; NbExp=3; IntAct=EBI-351935, EBI-12041225;
P02545; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-351935, EBI-11975223;
P02545; P63104: YWHAZ; NbExp=2; IntAct=EBI-351935, EBI-347088;
P02545; P10074: ZBTB48; NbExp=3; IntAct=EBI-351935, EBI-744864;
P02545; Q6ZN57: ZFP2; NbExp=3; IntAct=EBI-351935, EBI-7236323;
P02545; Q8WW38: ZFPM2; NbExp=3; IntAct=EBI-351935, EBI-947213;
P02545; Q15776: ZKSCAN8; NbExp=3; IntAct=EBI-351935, EBI-2602314;
P02545; P17024: ZNF20; NbExp=3; IntAct=EBI-351935, EBI-717634;
P02545; Q14585: ZNF345; NbExp=3; IntAct=EBI-351935, EBI-2818408;
P02545; Q9C0F3: ZNF436; NbExp=3; IntAct=EBI-351935, EBI-8489702;
P02545; Q8N0Y2-2: ZNF444; NbExp=3; IntAct=EBI-351935, EBI-12010736;
P02545; Q96MN9-2: ZNF488; NbExp=3; IntAct=EBI-351935, EBI-25831733;
P02545; Q6ZNH5: ZNF497; NbExp=3; IntAct=EBI-351935, EBI-10486136;
P02545; Q8TBZ8: ZNF564; NbExp=3; IntAct=EBI-351935, EBI-10273713;
P02545; Q7Z3I7: ZNF572; NbExp=3; IntAct=EBI-351935, EBI-10172590;
P02545; Q96LX8: ZNF597; NbExp=3; IntAct=EBI-351935, EBI-9091553;
P02545; Q9BS31: ZNF649; NbExp=3; IntAct=EBI-351935, EBI-4395789;
P02545; O43309: ZSCAN12; NbExp=3; IntAct=EBI-351935, EBI-1210440;
P02545; P10073: ZSCAN22; NbExp=3; IntAct=EBI-351935, EBI-10178224;
P02545; P10215: NEC1; Xeno; NbExp=2; IntAct=EBI-351935, EBI-7183650;
P02545; P10218: NEC2; Xeno; NbExp=2; IntAct=EBI-351935, EBI-7183680;
P02545-1; P50402: EMD; NbExp=4; IntAct=EBI-351949, EBI-489887;
P02545-1; P20700: LMNB1; NbExp=5; IntAct=EBI-351949, EBI-968218;
P02545-1; PRO_0000314029 [P36956]: SREBF1; NbExp=6; IntAct=EBI-351949, EBI-22057616;
P02545-1; O75844: ZMPSTE24; NbExp=2; IntAct=EBI-351949, EBI-1056377;
P02545-2; Q9HC96: CAPN10; NbExp=3; IntAct=EBI-351953, EBI-3915761;
P02545-2; Q9UNS2: COPS3; NbExp=3; IntAct=EBI-351953, EBI-350590;
P02545-2; Q0D2I5: IFFO1; NbExp=2; IntAct=EBI-351953, EBI-742894;
P02545-2; P02545-2: LMNA; NbExp=4; IntAct=EBI-351953, EBI-351953;
P02545-2; P20700: LMNB1; NbExp=19; IntAct=EBI-351953, EBI-968218;
P02545-2; O75925: PIAS1; NbExp=3; IntAct=EBI-351953, EBI-629434;
P02545-2; Q8N0S2: SYCE1; NbExp=3; IntAct=EBI-351953, EBI-6872807;
P02545-2; Q9GZS3: WDR61; NbExp=3; IntAct=EBI-351953, EBI-358545;
P02545-6; Q71DI3: H3C15; NbExp=3; IntAct=EBI-9034379, EBI-750650;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15372542,
ECO:0000269|PubMed:31548606}. Nucleus envelope
{ECO:0000269|PubMed:29599122}. Nucleus lamina. Nucleus, nucleoplasm.
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. EMD is
required for proper localization of non-farnesylated prelamin-A/C.
-!- SUBCELLULAR LOCATION: [Isoform C]: Nucleus speckle
{ECO:0000269|PubMed:16061563}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=A; Synonyms=Lamin A;
IsoId=P02545-1; Sequence=Displayed;
Name=C; Synonyms=Lamin C;
IsoId=P02545-2; Sequence=VSP_002469, VSP_002470;
Name=ADelta10; Synonyms=Lamin ADelta10;
IsoId=P02545-3; Sequence=VSP_002468;
Name=4;
IsoId=P02545-4; Sequence=VSP_045977, VSP_045978, VSP_045979;
Name=5;
IsoId=P02545-5; Sequence=VSP_053503, VSP_053504;
Name=6; Synonyms=Progerin;
IsoId=P02545-6; Sequence=VSP_053505;
-!- TISSUE SPECIFICITY: In the arteries, prelamin-A/C accumulation is not
observed in young healthy vessels but is prevalent in medial vascular
smooth muscle cells (VSMCs) from aged individuals and in
atherosclerotic lesions, where it often colocalizes with senescent and
degenerate VSMCs. Prelamin-A/C expression increases with age and
disease. In normal aging, the accumulation of prelamin-A/C is caused in
part by the down-regulation of ZMPSTE24/FACE1 in response to oxidative
stress. {ECO:0000269|PubMed:20458013}.
-!- PTM: Increased phosphorylation of the lamins occurs before envelope
disintegration and probably plays a role in regulating lamin
associations. Phosphorylation status of S-22 determines its
localization between double-strand break (DSB) sites and the nuclear
matrix (PubMed:31548606). {ECO:0000269|PubMed:31548606,
ECO:0000269|Ref.9}.
-!- PTM: Proteolytic cleavage of the C-terminal of 18 residues of prelamin-
A/C results in the production of lamin-A/C. The prelamin-A/C maturation
pathway includes farnesylation of CAAX motif, ZMPSTE24/FACE1 mediated
cleavage of the last three amino acids, methylation of the C-terminal
cysteine and endoproteolytic removal of the last 15 C-terminal amino
acids. Proteolytic cleavage requires prior farnesylation and
methylation, and absence of these blocks cleavage.
{ECO:0000269|PubMed:20458013, ECO:0000269|PubMed:8175923,
ECO:0000269|PubMed:9030603}.
-!- PTM: Sumoylation is necessary for the localization to the nuclear
envelope. {ECO:0000269|PubMed:18606848}.
-!- PTM: Farnesylation of prelamin-A/C facilitates nuclear envelope
targeting.
-!- 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:10080180,
ECO:0000269|PubMed:10739764, ECO:0000269|PubMed:10814726,
ECO:0000269|PubMed:10908904, ECO:0000269|PubMed:10939567,
ECO:0000269|PubMed:11503164, ECO:0000269|PubMed:11525883,
ECO:0000269|PubMed:11792809, ECO:0000269|PubMed:12032588,
ECO:0000269|PubMed:12467752, ECO:0000269|PubMed:12649505,
ECO:0000269|PubMed:12673789, ECO:0000269|PubMed:14684700,
ECO:0000269|PubMed:14985400, ECO:0000269|PubMed:15372542,
ECO:0000269|PubMed:15744034, ECO:0000269|PubMed:17136397,
ECO:0000269|PubMed:19933576, ECO:0000269|PubMed:20848652,
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: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]: A
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 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 mental retardation, 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: Lethal tight skin contracture syndrome (LTSCS) [MIM:275210]:
Rare disorder mainly characterized by intrauterine growth retardation,
tight and rigid skin with erosions, prominent superficial vasculature
and epidermal hyperkeratosis, facial features (small mouth, small
pinched nose and micrognathia), sparse/absent eyelashes and eyebrows,
mineralization defects of the skull, thin dysplastic clavicles,
pulmonary hypoplasia, multiple joint contractures and an early neonatal
lethal course. Liveborn children usually die within the first week of
life. The overall prevalence of consanguineous cases suggested an
autosomal recessive inheritance. {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}.
-!- MISCELLANEOUS: There are three types of lamins in human cells: A, B,
and C.
-!- MISCELLANEOUS: 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.
-!- MISCELLANEOUS: [Isoform 6]: Disease-associated isoform. Polymorphism at
codon 608 results in activation of a cryptic splice donor site within
exon 11, resulting in a truncated protein product that lacks the site
for endoproteolytic cleavage. {ECO:0000305}.
-!- SIMILARITY: Belongs to the intermediate filament family.
{ECO:0000255|PROSITE-ProRule:PRU01188}.
-!- SEQUENCE CAUTION:
Sequence=CAA27173.1; Type=Frameshift; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Human Intermediate Filament Mutation Database;
URL="http://www.interfil.org";
---------------------------------------------------------------------------
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EMBL; X03444; CAA27173.1; ALT_FRAME; mRNA.
EMBL; X03445; CAA27174.1; -; mRNA.
EMBL; M13451; AAA36164.1; -; mRNA.
EMBL; M13452; AAA36160.1; -; mRNA.
EMBL; AY847597; AAW32540.1; -; mRNA.
EMBL; AY847595; AAW32538.1; -; mRNA.
EMBL; AY357727; AAR29466.1; -; mRNA.
EMBL; AK295390; BAG58344.1; -; mRNA.
EMBL; AL135927; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL355388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL356734; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW52997.1; -; Genomic_DNA.
EMBL; CH471121; EAW52999.1; -; Genomic_DNA.
EMBL; BC000511; AAH00511.1; -; mRNA.
EMBL; BC003162; AAH03162.1; -; mRNA.
EMBL; BC014507; AAH14507.1; -; mRNA.
EMBL; AF381029; AAK59326.1; -; mRNA.
CCDS; CCDS1129.1; -. [P02545-1]
CCDS; CCDS1131.1; -. [P02545-2]
CCDS; CCDS58038.1; -. [P02545-4]
CCDS; CCDS72941.1; -. [P02545-6]
PIR; A02961; VEHULA.
PIR; A02962; VEHULC.
RefSeq; NP_001244303.1; NM_001257374.2. [P02545-4]
RefSeq; NP_001269553.1; NM_001282624.1.
RefSeq; NP_001269554.1; NM_001282625.1. [P02545-2]
RefSeq; NP_001269555.1; NM_001282626.1. [P02545-6]
RefSeq; NP_005563.1; NM_005572.3. [P02545-2]
RefSeq; NP_733821.1; NM_170707.3. [P02545-1]
RefSeq; NP_733822.1; NM_170708.3. [P02545-3]
PDB; 1IFR; X-ray; 1.40 A; A=436-552.
PDB; 1IVT; NMR; -; A=428-549.
PDB; 1X8Y; X-ray; 2.20 A; A=305-387.
PDB; 2XV5; X-ray; 2.40 A; A/B=328-398.
PDB; 2YPT; X-ray; 3.80 A; F/G/H/I=661-664.
PDB; 3GEF; X-ray; 1.50 A; A/B/C/D=436-552.
PDB; 3V4Q; X-ray; 3.06 A; A=313-386.
PDB; 3V4W; X-ray; 3.70 A; A=313-386.
PDB; 3V5B; X-ray; 3.00 A; A=313-386.
PDB; 6GHD; X-ray; 2.10 A; B/F=428-546.
PDB; 6JLB; X-ray; 3.21 A; A/B/C/D=1-300.
PDB; 6RPR; X-ray; 2.26 A; B=430-545.
PDB; 6SNZ; X-ray; 2.60 A; A/B/C/D=65-222.
PDB; 6YF5; X-ray; 1.83 A; A/B/C/D=17-70.
PDB; 6YJD; X-ray; 2.90 A; A=329-403.
PDBsum; 1IFR; -.
PDBsum; 1IVT; -.
PDBsum; 1X8Y; -.
PDBsum; 2XV5; -.
PDBsum; 2YPT; -.
PDBsum; 3GEF; -.
PDBsum; 3V4Q; -.
PDBsum; 3V4W; -.
PDBsum; 3V5B; -.
PDBsum; 6GHD; -.
PDBsum; 6JLB; -.
PDBsum; 6RPR; -.
PDBsum; 6SNZ; -.
PDBsum; 6YF5; -.
PDBsum; 6YJD; -.
BMRB; P02545; -.
SMR; P02545; -.
BioGRID; 110186; 915.
CORUM; P02545; -.
DIP; DIP-32948N; -.
DIP; DIP-58162N; -.
IntAct; P02545; 353.
MINT; P02545; -.
STRING; 9606.ENSP00000357283; -.
ChEMBL; CHEMBL1293235; -.
GlyConnect; 2876; 1 O-Linked glycan (2 sites). [P02545-3]
GlyGen; P02545; 1 site, 1 O-linked glycan (1 site).
iPTMnet; P02545; -.
MetOSite; P02545; -.
PhosphoSitePlus; P02545; -.
SwissPalm; P02545; -.
BioMuta; LMNA; -.
DMDM; 125962; -.
REPRODUCTION-2DPAGE; IPI00021405; -.
REPRODUCTION-2DPAGE; IPI00216952; -.
REPRODUCTION-2DPAGE; P02545; -.
SWISS-2DPAGE; P02545; -.
CPTAC; CPTAC-399; -.
CPTAC; CPTAC-400; -.
CPTAC; CPTAC-973; -.
CPTAC; CPTAC-974; -.
EPD; P02545; -.
jPOST; P02545; -.
MassIVE; P02545; -.
MaxQB; P02545; -.
PaxDb; P02545; -.
PeptideAtlas; P02545; -.
PRIDE; P02545; -.
ProteomicsDB; 13394; -.
ProteomicsDB; 18441; -.
ProteomicsDB; 51530; -. [P02545-1]
ProteomicsDB; 51531; -. [P02545-2]
ProteomicsDB; 51532; -. [P02545-3]
ProteomicsDB; 67698; -.
TopDownProteomics; P02545-1; -. [P02545-1]
TopDownProteomics; P02545-2; -. [P02545-2]
TopDownProteomics; P02545-4; -. [P02545-4]
Antibodypedia; 1676; 1608 antibodies.
DNASU; 4000; -.
Ensembl; ENST00000361308; ENSP00000355292; ENSG00000160789. [P02545-1]
Ensembl; ENST00000368299; ENSP00000357282; ENSG00000160789. [P02545-6]
Ensembl; ENST00000368300; ENSP00000357283; ENSG00000160789. [P02545-1]
Ensembl; ENST00000368301; ENSP00000357284; ENSG00000160789. [P02545-2]
Ensembl; ENST00000448611; ENSP00000395597; ENSG00000160789. [P02545-4]
Ensembl; ENST00000473598; ENSP00000421821; ENSG00000160789. [P02545-5]
Ensembl; ENST00000675939; ENSP00000502256; ENSG00000160789. [P02545-1]
Ensembl; ENST00000676385; ENSP00000502091; ENSG00000160789. [P02545-3]
Ensembl; ENST00000677389; ENSP00000503633; ENSG00000160789. [P02545-2]
GeneID; 4000; -.
KEGG; hsa:4000; -.
UCSC; uc001fnf.3; human. [P02545-1]
CTD; 4000; -.
DisGeNET; 4000; -.
GeneCards; LMNA; -.
GeneReviews; LMNA; -.
HGNC; HGNC:6636; LMNA.
HPA; ENSG00000160789; Low tissue specificity.
MalaCards; LMNA; -.
MIM; 115200; phenotype.
MIM; 150330; gene.
MIM; 151660; phenotype.
MIM; 176670; phenotype.
MIM; 181350; phenotype.
MIM; 212112; phenotype.
MIM; 248370; phenotype.
MIM; 275210; phenotype.
MIM; 605588; phenotype.
MIM; 610140; phenotype.
MIM; 613205; phenotype.
MIM; 616516; phenotype.
neXtProt; NX_P02545; -.
OpenTargets; ENSG00000160789; -.
Orphanet; 79474; Atypical Werner syndrome.
Orphanet; 98853; Autosomal dominant Emery-Dreifuss muscular dystrophy.
Orphanet; 98855; Autosomal recessive Emery-Dreifuss muscular dystrophy.
Orphanet; 280365; Autosomal semi-dominant severe lipodystrophic laminopathy.
Orphanet; 98856; Charcot-Marie-Tooth disease type 2B1.
Orphanet; 157973; Congenital muscular dystrophy due to LMNA mutation.
Orphanet; 2229; Dilated cardiomyopathy-hypergonadotropic hypogonadism syndrome.
Orphanet; 300751; Familial dilated cardiomyopathy with conduction defect due to LMNA mutation.
Orphanet; 293899; Familial isolated arrhythmogenic ventricular dysplasia, biventricular form.
Orphanet; 293888; Familial isolated arrhythmogenic ventricular dysplasia, left dominant form.
Orphanet; 293910; Familial isolated arrhythmogenic ventricular dysplasia, right dominant form.
Orphanet; 2348; Familial partial lipodystrophy, Dunnigan type.
Orphanet; 79084; Familial partial lipodystrophy, Koebberling type.
Orphanet; 168796; Heart-hand syndrome, Slovenian type.
Orphanet; 740; Hutchinson-Gilford progeria syndrome.
Orphanet; 54260; Left ventricular noncompaction.
Orphanet; 363618; LMNA-related cardiocutaneous progeria syndrome.
Orphanet; 90153; Mandibuloacral dysplasia with type A lipodystrophy.
Orphanet; 1662; Restrictive dermopathy.
PharmGKB; PA231; -.
VEuPathDB; HostDB:ENSG00000160789.19; -.
eggNOG; KOG0977; Eukaryota.
GeneTree; ENSGT00940000157244; -.
HOGENOM; CLU_012560_9_1_1; -.
InParanoid; P02545; -.
OMA; CGQPAEK; -.
OrthoDB; 701388at2759; -.
PhylomeDB; P02545; -.
TreeFam; TF101181; -.
PathwayCommons; P02545; -.
Reactome; R-HSA-1221632; Meiotic synapsis. [P02545-2]
Reactome; R-HSA-2980766; Nuclear Envelope Breakdown.
Reactome; R-HSA-2995383; Initiation of Nuclear Envelope (NE) Reformation.
Reactome; R-HSA-352238; Breakdown of the nuclear lamina. [P02545-1]
Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
Reactome; R-HSA-4419969; Depolymerisation of the Nuclear Lamina.
Reactome; R-HSA-6802952; Signaling by BRAF and RAF fusions.
Reactome; R-HSA-8862803; Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models. [P02545-1]
SIGNOR; P02545; -.
BioGRID-ORCS; 4000; 81 hits in 1001 CRISPR screens.
ChiTaRS; LMNA; human.
EvolutionaryTrace; P02545; -.
GeneWiki; LMNA; -.
GenomeRNAi; 4000; -.
Pharos; P02545; Tbio.
PRO; PR:P02545; -.
Proteomes; UP000005640; Chromosome 1.
RNAct; P02545; protein.
Bgee; ENSG00000160789; Expressed in mucosa of stomach and 252 other tissues.
ExpressionAtlas; P02545; baseline and differential.
Genevisible; P02545; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005882; C:intermediate filament; TAS:UniProtKB.
GO; GO:0005638; C:lamin filament; TAS:UniProtKB.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
GO; GO:0005652; C:nuclear lamina; TAS:UniProtKB.
GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; HDA:UniProtKB.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:CAFA.
GO; GO:0005634; C:nucleus; IDA:ARUK-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005198; F:structural molecule activity; TAS:UniProtKB.
GO; GO:0034613; P:cellular protein localization; IMP:CAFA.
GO; GO:0071456; P:cellular response to hypoxia; IEP:UniProtKB.
GO; GO:1990683; P:DNA double-strand break attachment to nuclear envelope; IDA:UniProtKB.
GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; ISS:BHF-UCL.
GO; GO:0036498; P:IRE1-mediated unfolded protein response; TAS:Reactome.
GO; GO:0007084; P:mitotic nuclear envelope reassembly; TAS:Reactome.
GO; GO:0007517; P:muscle organ development; IMP:UniProtKB.
GO; GO:1903243; P:negative regulation of cardiac muscle hypertrophy in response to stress; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:CAFA.
GO; GO:0006998; P:nuclear envelope organization; IMP:CAFA.
GO; GO:0090343; P:positive regulation of cell aging; IDA:UniProtKB.
GO; GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
GO; GO:0030334; P:regulation of cell migration; ISS:BHF-UCL.
GO; GO:0032204; P:regulation of telomere maintenance; IMP:BHF-UCL.
DisProt; DP00716; -.
Gene3D; 1.20.5.1160; -; 1.
Gene3D; 2.60.40.1260; -; 1.
InterPro; IPR018039; IF_conserved.
InterPro; IPR039008; IF_rod_dom.
InterPro; IPR042180; IF_rod_dom_coil1B.
InterPro; IPR001322; Lamin_tail_dom.
InterPro; IPR036415; Lamin_tail_dom_sf.
Pfam; PF00038; Filament; 1.
Pfam; PF00932; LTD; 1.
SMART; SM01391; Filament; 1.
SUPFAM; SSF74853; SSF74853; 1.
PROSITE; PS00226; IF_ROD_1; 1.
PROSITE; PS51842; IF_ROD_2; 1.
PROSITE; PS51841; LTD; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cardiomyopathy;
Charcot-Marie-Tooth disease; Coiled coil; Congenital muscular dystrophy;
Direct protein sequencing; Disease variant;
Emery-Dreifuss muscular dystrophy; Intermediate filament; Isopeptide bond;
Limb-girdle muscular dystrophy; Lipoprotein; Methylation;
Neurodegeneration; Neuropathy; Nucleus; Phosphoprotein; Prenylation;
Reference proteome; Ubl conjugation.
CHAIN 1..661
/note="Prelamin-A/C"
/id="PRO_0000398835"
CHAIN 1..646
/note="Lamin-A/C"
/id="PRO_0000063810"
PROPEP 647..661
/note="Removed in Lamin-A/C form"
/id="PRO_0000398836"
PROPEP 662..664
/note="Removed in Prelamin-A/C form and in Lamin-A/C form"
/id="PRO_0000403442"
DOMAIN 31..387
/note="IF rod"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
DOMAIN 428..545
/note="LTD"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01187"
REGION 1..130
/note="Interaction with MLIP"
/evidence="ECO:0000269|PubMed:21498514"
REGION 1..33
/note="Head"
REGION 1..25
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 34..70
/note="Coil 1A"
REGION 71..80
/note="Linker 1"
REGION 81..218
/note="Coil 1B"
REGION 219..242
/note="Linker 2"
REGION 243..383
/note="Coil 2"
REGION 259..331
/note="Necessary and sufficient for the interaction with
IFFO1"
/evidence="ECO:0000269|PubMed:31548606"
REGION 384..664
/note="Tail"
REGION 384..442
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 552..576
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 598..619
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOTIF 417..422
/note="Nuclear localization signal"
/evidence="ECO:0000255"
COMPBIAS 391..417
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
SITE 266
/note="Heptad change of phase"
SITE 325
/note="Stutter"
/evidence="ECO:0000250"
SITE 330
/note="Heptad change of phase"
SITE 646..647
/note="Cleavage; by endoprotease"
MOD_RES 1
/note="N-acetylmethionine"
/evidence="ECO:0007744|PubMed:20068231"
MOD_RES 3
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:20068231"
MOD_RES 12
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
ECO:0007744|PubMed:24275569"
MOD_RES 18
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648"
MOD_RES 19
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:16964243,
ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
MOD_RES 22
/note="Phosphoserine"
/evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:16964243,
ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
MOD_RES 32
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P48678"
MOD_RES 32
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P48678"
MOD_RES 51
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 66
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 71
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 107
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 108
/note="N6-acetyllysine"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 123
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P48678"
MOD_RES 135
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P48678"
MOD_RES 155
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P48678"
MOD_RES 171
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P48678"
MOD_RES 171
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P48678"
MOD_RES 201
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P48678"
MOD_RES 212
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
MOD_RES 260
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P48678"
MOD_RES 270
/note="N6-acetyllysine; alternate"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 277
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:17081983,
ECO:0007744|PubMed:20068231"
MOD_RES 301
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
ECO:0007744|PubMed:24275569"
MOD_RES 307
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:24275569"
MOD_RES 311
/note="N6-acetyllysine; alternate"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 390
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:16964243,
ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
ECO:0007744|PubMed:24275569"
MOD_RES 392
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:16964243,
ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
MOD_RES 395
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:16964243,
ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:24275569"
MOD_RES 398
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 403
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:24275569"
MOD_RES 404
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
MOD_RES 407
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P48678"
MOD_RES 414
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
MOD_RES 429
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 431
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:20068231"
MOD_RES 450
/note="N6-acetyllysine; alternate"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 457
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P48678"
MOD_RES 458
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
MOD_RES 463
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
MOD_RES 496
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:P48679"
MOD_RES 505
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:20068231"
MOD_RES 510
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:P48679"
MOD_RES 533
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 546
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P48678"
MOD_RES 548
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:P48678"
MOD_RES 568
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P48678"
MOD_RES 571
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P48678"
MOD_RES 612
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:24275569"
MOD_RES 613
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 616
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P48678"
MOD_RES 619
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 628
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:16964243,
ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18220336,
ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:23186163"
MOD_RES 632
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:16964243,
ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
MOD_RES 636
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:16964243,
ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
ECO:0007744|PubMed:24275569"
MOD_RES 652
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:20068231"
MOD_RES 661
/note="Cysteine methyl ester"
/evidence="ECO:0000269|PubMed:8175923,
ECO:0000269|PubMed:9030603"
LIPID 661
/note="S-farnesyl cysteine"
/evidence="ECO:0000269|PubMed:8175923,
ECO:0000269|PubMed:9030603"
CROSSLNK 32
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 97
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:25218447,
ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
CROSSLNK 171
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 201
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO); alternate"
CROSSLNK 201
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 208
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:25218447,
ECO:0007744|PubMed:28112733"
CROSSLNK 219
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 233
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:25114211,
ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
ECO:0007744|PubMed:28112733"
CROSSLNK 260
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0007744|PubMed:25755297,
ECO:0007744|PubMed:28112733"
CROSSLNK 270
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0007744|PubMed:25755297,
ECO:0007744|PubMed:28112733"
CROSSLNK 311
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0007744|PubMed:25218447,
ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
CROSSLNK 366
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 378
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:25218447,
ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
ECO:0007744|PubMed:28112733"
CROSSLNK 417
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:25218447,
ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
CROSSLNK 420
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:25218447,
ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
ECO:0007744|PubMed:28112733"
CROSSLNK 450
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 470
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 486
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 597
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO1); alternate"
/evidence="ECO:0007744|PubMed:25114211"
CROSSLNK 597
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0007744|PubMed:25114211,
ECO:0007744|PubMed:28112733"
VAR_SEQ 1..99
/note="Missing (in isoform 5)"
/evidence="ECO:0000305"
/id="VSP_053503"
VAR_SEQ 1..7
/note="METPSQR -> MGNSEGC (in isoform 4)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_045977"
VAR_SEQ 8..119
/note="Missing (in isoform 4)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_045978"
VAR_SEQ 100..119
/note="ARLQLELSKVREEFKELKAR -> MDLEAWDPHLEPDAEAMVDG (in
isoform 5)"
/evidence="ECO:0000305"
/id="VSP_053504"
VAR_SEQ 537..566
/note="Missing (in isoform ADelta10)"
/evidence="ECO:0000303|PubMed:8621584"
/id="VSP_002468"
VAR_SEQ 567..572
/note="GSHCSS -> VSGSRR (in isoform C)"
/evidence="ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:3453101, ECO:0000303|PubMed:3462705"
/id="VSP_002469"
VAR_SEQ 573..664
/note="Missing (in isoform C)"
/evidence="ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:3453101, ECO:0000303|PubMed:3462705"
/id="VSP_002470"
VAR_SEQ 607..656
/note="Missing (in isoform 6)"
/evidence="ECO:0000303|Ref.4"
/id="VSP_053505"
VAR_SEQ 664
/note="M -> IQEMGMRWEVEEGRRKVSLSCLP (in isoform 4)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_045979"
VARIANT 10
/note="T -> I (in an atypical progeroid patient; diagnosed
as Seip syndrome; unknown pathological significance;
dbSNP:rs57077886)"
/evidence="ECO:0000269|PubMed:15060110"
/id="VAR_039745"
VARIANT 24
/note="T -> S (in EDMD3)"
/evidence="ECO:0000269|PubMed:27234031"
/id="VAR_076562"
VARIANT 25
/note="R -> G (in EDMD2; dbSNP:rs58327533)"
/evidence="ECO:0000269|PubMed:14684700"
/id="VAR_039746"
VARIANT 25
/note="R -> P (in EDMD2; mis-localized in the nucleus;
causes nuclear deformations and LMNB1 redistribution;
dbSNP:rs61578124)"
/evidence="ECO:0000269|PubMed:11503164,
ECO:0000269|PubMed:20848652"
/id="VAR_039747"
VARIANT 28
/note="R -> W (in FPLD2; dbSNP:rs59914820)"
/evidence="ECO:0000269|PubMed:12015247"
/id="VAR_039748"
VARIANT 32
/note="Missing (in EDMD2; abnormal nuclear localization in
a honeycomb expression pattern in about 11% of cultured
skin fibroblasts from heterozygous patients; no effect on
protein level)"
/evidence="ECO:0000269|PubMed:12467752,
ECO:0000269|PubMed:14684700, ECO:0000269|PubMed:15372542"
/id="VAR_039749"
VARIANT 33
/note="E -> D (in CMT2; autosomal dominant form;
dbSNP:rs57966821)"
/evidence="ECO:0000269|PubMed:14985400"
/id="VAR_039750"
VARIANT 33
/note="E -> G (in EDMD2; dbSNP:rs267607614)"
/evidence="ECO:0000269|PubMed:14985400"
/id="VAR_039751"
VARIANT 35
/note="L -> V (in EDMD2; dbSNP:rs56694480)"
/evidence="ECO:0000269|PubMed:14684700"
/id="VAR_039752"
VARIANT 39
/note="N -> S (in MDCL and EDMD2; dbSNP:rs57983345)"
/evidence="ECO:0000269|PubMed:18551513,
ECO:0000269|PubMed:20848652"
/id="VAR_063588"
VARIANT 43
/note="A -> T (in EDMD2; dbSNP:rs60446065)"
/evidence="ECO:0000269|PubMed:11503164"
/id="VAR_039753"
VARIANT 45
/note="Y -> C (in EDMD2; dbSNP:rs58436778)"
/evidence="ECO:0000269|PubMed:10939567,
ECO:0000269|PubMed:20848652"
/id="VAR_009971"
VARIANT 50
/note="R -> P (in EDMD2 and MDCL; dbSNP:rs60695352)"
/evidence="ECO:0000269|PubMed:10939567,
ECO:0000269|PubMed:18551513"
/id="VAR_009972"
VARIANT 50
/note="R -> S (in EDMD2; dbSNP:rs59931416)"
/evidence="ECO:0000269|PubMed:11503164"
/id="VAR_039754"
VARIANT 57
/note="A -> P (in CMDHH; phenotype originally designated as
atypical Werner syndrome; dbSNP:rs28928903)"
/evidence="ECO:0000269|PubMed:12927431"
/id="VAR_017656"
VARIANT 59
/note="L -> R (in CMDHH; dbSNP:rs58922911)"
/evidence="ECO:0000269|PubMed:17150192,
ECO:0000269|PubMed:19283854"
/id="VAR_064055"
VARIANT 60
/note="R -> G (in CMD1A and FPLD2; interacts with itself
and with wild-type LMNA and LMNB1; no decrease in the
stability compared with wild-type; dbSNP:rs28928900)"
/evidence="ECO:0000269|PubMed:10580070,
ECO:0000269|PubMed:11792809, ECO:0000269|PubMed:12196663"
/id="VAR_034706"
VARIANT 62
/note="R -> G (in FPLD2; dbSNP:rs56793579)"
/evidence="ECO:0000269|PubMed:12015247"
/id="VAR_039755"
VARIANT 63
/note="I -> N (in EDMD2; dbSNP:rs57793737)"
/evidence="ECO:0000269|PubMed:12467752,
ECO:0000269|PubMed:12649505, ECO:0000269|PubMed:15744034"
/id="VAR_039756"
VARIANT 63
/note="I -> S (in EDMD2; no effect on protein level; no
obvious effect on nuclear morphology in cultured skin
fibroblasts from heterozygous patients; dbSNP:rs57793737)"
/evidence="ECO:0000269|PubMed:10939567,
ECO:0000269|PubMed:15372542"
/id="VAR_009974"
VARIANT 65
/note="E -> G (in EDMD2)"
/evidence="ECO:0000269|PubMed:14684700"
/id="VAR_039757"
VARIANT 85
/note="L -> R (in CMD1A; interacts with itself and with
wild-type LMNA and LMNB1; no decrease in the stability
compared with wild-type; dbSNP:rs28933090)"
/evidence="ECO:0000269|PubMed:10580070,
ECO:0000269|PubMed:11792809"
/id="VAR_009975"
VARIANT 89
/note="R -> L (in CMD1A; dramatically aberrant localization
with almost no nuclear rim staining and formation of
intranuclear foci; dbSNP:rs59040894)"
/evidence="ECO:0000269|PubMed:12628721,
ECO:0000269|PubMed:20160190"
/id="VAR_039758"
VARIANT 92
/note="L -> F (in CMD1A; dbSNP:rs267607560)"
/evidence="ECO:0000269|PubMed:21846512"
/id="VAR_067257"
VARIANT 97
/note="K -> E (in CMD1A; dbSNP:rs59065411)"
/evidence="ECO:0000269|PubMed:11897440"
/id="VAR_039759"
VARIANT 101
/note="R -> P (in CMD1A; dramatically aberrant localization
with almost no nuclear rim staining and formation of
intranuclear foci; dbSNP:rs267607568)"
/evidence="ECO:0000269|PubMed:20160190"
/id="VAR_070174"
VARIANT 112
/note="Missing (in EDMD2)"
/evidence="ECO:0000269|PubMed:10939567,
ECO:0000269|PubMed:14684700"
/id="VAR_009976"
VARIANT 125
/note="G -> S (found in patients with atrial fibrillation;
unknown pathological significance; dbSNP:rs267607605)"
/evidence="ECO:0000269|PubMed:19427440"
/id="VAR_072817"
VARIANT 133
/note="R -> L (in FPLD2; dbSNP:rs60864230)"
/evidence="ECO:0000269|PubMed:12629077"
/id="VAR_016913"
VARIANT 133
/note="R -> P (in EDMD2; dbSNP:rs60864230)"
/evidence="ECO:0000269|PubMed:11503164"
/id="VAR_017657"
VARIANT 138
/note="E -> K (in HGPS; might be associated with early and
severe strokes; dbSNP:rs267607649)"
/evidence="ECO:0000269|PubMed:21791255"
/id="VAR_070175"
VARIANT 140
/note="L -> P (in EDMD2; dbSNP:rs60652225)"
/evidence="ECO:0000269|PubMed:12649505,
ECO:0000269|PubMed:15744034"
/id="VAR_039760"
VARIANT 140
/note="L -> R (in HGPS; phenotype originally designated as
atypical Werner syndrome; dbSNP:rs60652225)"
/evidence="ECO:0000269|PubMed:12927431"
/id="VAR_017658"
VARIANT 143
/note="S -> F (in HGPS; dbSNP:rs58912633)"
/evidence="ECO:0000269|PubMed:15622532"
/id="VAR_034707"
VARIANT 143
/note="S -> P (in CMD1A; dbSNP:rs61661343)"
/evidence="ECO:0000269|PubMed:15140538"
/id="VAR_039761"
VARIANT 145
/note="E -> K (in HGPS; atypical; dbSNP:rs60310264)"
/evidence="ECO:0000269|PubMed:12714972"
/id="VAR_017659"
VARIANT 150
/note="T -> P (in EDMD2; dbSNP:rs58917027)"
/evidence="ECO:0000269|PubMed:10908904,
ECO:0000269|PubMed:20848652"
/id="VAR_039762"
VARIANT 161
/note="E -> K (in CMD1A; dbSNP:rs28933093)"
/evidence="ECO:0000269|PubMed:12920062,
ECO:0000269|PubMed:21846512"
/id="VAR_017660"
VARIANT 166
/note="R -> P (in CMD1A; dramatically aberrant localization
with almost no nuclear rim staining and formation of
intranuclear foci; dbSNP:rs267607570)"
/evidence="ECO:0000269|PubMed:20160190"
/id="VAR_070176"
VARIANT 189
/note="R -> P (in EDMD2; found also in a patient with limb-
girdle muscular dystrophy; sporadic; dbSNP:rs267607643)"
/evidence="ECO:0000269|PubMed:20848652"
/id="VAR_064962"
VARIANT 190
/note="R -> Q (in EDMD2 and CMD1A; aberrant localization
with decreased nuclear rim staining and increased formation
of intranuclear foci; dbSNP:rs267607571)"
/evidence="ECO:0000269|PubMed:15744034,
ECO:0000269|PubMed:20160190"
/id="VAR_039763"
VARIANT 190
/note="R -> RR (in EDMD2)"
/evidence="ECO:0000269|PubMed:20848652"
/id="VAR_064963"
VARIANT 190
/note="R -> W (in CMD1A; dbSNP:rs59026483)"
/evidence="ECO:0000269|PubMed:11897440,
ECO:0000269|PubMed:15219508, ECO:0000269|PubMed:16061563"
/id="VAR_039764"
VARIANT 192
/note="D -> G (in CMD1A; dramatically increases the size of
intranuclear speckles and reduces their number; this
phenotype is only partially reversed by coexpression of the
G-192 mutation and wild-type lamin-C; precludes insertion
of lamin-C into the nuclear envelope when co-transfected
with the G-192 LMNA; G-192 lamin-C expression totally
disrupts the SUMO1 pattern; dbSNP:rs57045855)"
/evidence="ECO:0000269|PubMed:16061563"
/id="VAR_039765"
VARIANT 195
/note="N -> K (in CMD1A; dramatically aberrant localization
with decreased nuclear rim staining and formation of
intranuclear foci; distribution of endogenous LMNA, LMNB1
and LMNB2 are altered in cells expressing this mutant;
causes an increased loss of endogenous EMD from the nuclear
envelope; interacts with itself and with wild-type LMNA and
LMNB1; no decrease in the stability compared with wild-
type; dbSNP:rs28933091)"
/evidence="ECO:0000269|PubMed:10580070,
ECO:0000269|PubMed:11792809"
/id="VAR_009977"
VARIANT 196..199
/note="RLQT -> S (in EDMD2)"
/evidence="ECO:0000269|PubMed:11503164"
/id="VAR_039766"
VARIANT 203
/note="E -> G (in CMD1A; interacts with itself and with
wild-type LMNA and LMNB1; no decrease in the stability
compared with wild-type; decreased sumoylation; aberrant
localization with decreased nuclear rim staining and
formation of intranuclear foci; associated with increased
cell death; dbSNP:rs28933092)"
/evidence="ECO:0000269|PubMed:10580070,
ECO:0000269|PubMed:11792809, ECO:0000269|PubMed:18606848"
/id="VAR_009978"
VARIANT 203
/note="E -> K (in CMD1A; decreased sumoylation; aberrant
localization with decreased nuclear rim staining and
formation of intranuclear foci; associated with increased
cell death; dbSNP:rs61195471)"
/evidence="ECO:0000269|PubMed:11561226,
ECO:0000269|PubMed:18606848, ECO:0000269|PubMed:20160190"
/id="VAR_039767"
VARIANT 206
/note="F -> L (in EDMD2; dbSNP:rs267607629)"
/evidence="ECO:0000269|PubMed:20848652"
/id="VAR_064964"
VARIANT 208
/note="Missing (in EDMD2; no obvious effect on nuclear
morphology in cultured skin fibroblasts from heterozygous
patients; no effect on protein level)"
/evidence="ECO:0000269|PubMed:10814726,
ECO:0000269|PubMed:15372542"
/id="VAR_034708"
VARIANT 210
/note="I -> S (in CMD1A; dramatically aberrant localization
with almost no nuclear rim staining and increased formation
of intranuclear foci; dbSNP:rs267607572)"
/evidence="ECO:0000269|PubMed:20160190"
/id="VAR_070177"
VARIANT 215
/note="L -> P (in CMD1A; aberrant localization with
decreased nuclear rim staining and formation of
intranuclear foci; dbSNP:rs61295588)"
/evidence="ECO:0000269|PubMed:12486434,
ECO:0000269|PubMed:20160190"
/id="VAR_039768"
VARIANT 222
/note="H -> P (in EDMD2; dbSNP:rs58034145)"
/evidence="ECO:0000269|PubMed:10939567"
/id="VAR_039769"
VARIANT 222
/note="H -> Y (in EDMD2; dbSNP:rs28928901)"
/evidence="ECO:0000269|PubMed:10739764"
/id="VAR_009979"
VARIANT 225
/note="R -> Q (in EDMD3; dbSNP:rs199474724)"
/evidence="ECO:0000269|PubMed:22431096"
/id="VAR_067697"
VARIANT 230
/note="D -> N (in FPLD2; dbSNP:rs61214927)"
/evidence="ECO:0000269|PubMed:17250669"
/id="VAR_039770"
VARIANT 232
/note="G -> E (in EDMD2; dbSNP:rs57207746)"
/evidence="ECO:0000269|PubMed:10939567"
/id="VAR_039771"
VARIANT 248
/note="L -> P (in EDMD2; dbSNP:rs58850446)"
/evidence="ECO:0000269|PubMed:14684700"
/id="VAR_039772"
VARIANT 249
/note="R -> Q (in EDMD2; no obvious effect on nuclear
morphology in cultured skin fibroblasts from heterozygous
patients; no effect on protein level; dbSNP:rs59332535)"
/evidence="ECO:0000269|PubMed:10739764,
ECO:0000269|PubMed:10939567, ECO:0000269|PubMed:11503164,
ECO:0000269|PubMed:12032588, ECO:0000269|PubMed:12649505,
ECO:0000269|PubMed:14684700, ECO:0000269|PubMed:15372542,
ECO:0000269|PubMed:15744034, ECO:0000269|PubMed:20848652"
/id="VAR_009980"
VARIANT 249
/note="R -> W (in MDCL and EDMD2; mislocalized in the
nucleus; causes nuclear deformations and LMNB1
redistribution; dbSNP:rs121912496)"
/evidence="ECO:0000269|PubMed:18551513,
ECO:0000269|PubMed:20848652"
/id="VAR_063589"
VARIANT 259
/note="Y -> C (in EDMD2)"
/evidence="ECO:0000269|PubMed:27234031"
/id="VAR_076563"
VARIANT 260
/note="K -> N (in CMDA1)"
/evidence="ECO:0000269|PubMed:16156025"
/id="VAR_039773"
VARIANT 261
/note="Missing (in EDMD2)"
/evidence="ECO:0000269|PubMed:10908904,
ECO:0000269|PubMed:10939567, ECO:0000269|PubMed:11503164"
/id="VAR_009981"
VARIANT 267
/note="Y -> C (in EDMD2; dbSNP:rs57048196)"
/evidence="ECO:0000269|PubMed:14684700"
/id="VAR_039774"
VARIANT 268
/note="S -> P (in EDMD2; dbSNP:rs267607630)"
/evidence="ECO:0000269|PubMed:20848652"
/id="VAR_064965"
VARIANT 271
/note="L -> P (in EDMD2; dbSNP:rs267607641)"
/evidence="ECO:0000269|PubMed:20848652"
/id="VAR_064966"
VARIANT 294
/note="Q -> P (in EDMD2; dbSNP:rs61616775)"
/evidence="ECO:0000269|PubMed:10939567,
ECO:0000269|PubMed:20848652"
/id="VAR_009982"
VARIANT 295
/note="S -> P (in EDMD2; dbSNP:rs267607633)"
/evidence="ECO:0000269|PubMed:20848652"
/id="VAR_064967"
VARIANT 298
/note="R -> C (in CMT2B1; dbSNP:rs59885338)"
/evidence="ECO:0000269|PubMed:11799477"
/id="VAR_017661"
VARIANT 300
/note="D -> G (in HGPS; atypical form with late onset;
abnormal nuclear morphology with single or multple blebs,
lobulation and occasional ringed or donut shaped nuclei;
dbSNP:rs79907212)"
/evidence="ECO:0000269|PubMed:23666920"
/id="VAR_070178"
VARIANT 302
/note="L -> P (in MDCL; dbSNP:rs267607596)"
/evidence="ECO:0000269|PubMed:18551513"
/id="VAR_063590"
VARIANT 303
/note="S -> P (in EDMD2; dbSNP:rs61527854)"
/evidence="ECO:0000269|PubMed:20848652"
/id="VAR_064968"
VARIANT 317
/note="E -> K (in CMD1A; dbSNP:rs56816490)"
/evidence="ECO:0000269|PubMed:11897440,
ECO:0000269|PubMed:21846512"
/id="VAR_039775"
VARIANT 318
/note="A -> T (in CMD1A; no effect on nuclear morphology
and lamin A localization; dbSNP:rs267607574)"
/evidence="ECO:0000269|PubMed:20160190"
/id="VAR_070179"
VARIANT 336
/note="R -> Q (in EDMD2; dbSNP:rs58105277)"
/evidence="ECO:0000269|PubMed:10739764,
ECO:0000269|PubMed:12467752"
/id="VAR_009983"
VARIANT 343
/note="R -> Q (in EDMD2; dbSNP:rs61177390)"
/evidence="ECO:0000269|PubMed:12467752"
/id="VAR_009984"
VARIANT 349
/note="R -> L (in CMD1A; dbSNP:rs58789393)"
/evidence="ECO:0000269|PubMed:15219508"
/id="VAR_039776"
VARIANT 355
/note="Missing (in EDMD2)"
/evidence="ECO:0000269|PubMed:20848652"
/id="VAR_064969"
VARIANT 358
/note="E -> K (in EDMD2 and MDCL; aberrant localization
with decreased nuclear rim staining and formation of
intranuclear foci when transfected in C2C12 myoblasts; no
obvious effect on nuclear morphology in cultured skin
fibroblasts from heterozygous patients; distribution of
endogenous LMNA, LMNB1 and LMNB2 are altered in cells
expressing this mutant; interacts with itself and with
wild-type LMNA and LMNB1; no effect on protein level;
dbSNP:rs60458016)"
/evidence="ECO:0000269|PubMed:10939567,
ECO:0000269|PubMed:11503164, ECO:0000269|PubMed:11792809,
ECO:0000269|PubMed:15372542, ECO:0000269|PubMed:18551513,
ECO:0000269|PubMed:20848652"
/id="VAR_009985"
VARIANT 361
/note="E -> K (in EDMD2; dbSNP:rs267607634)"
/evidence="ECO:0000269|PubMed:20848652"
/id="VAR_064970"
VARIANT 371
/note="M -> K (in EDMD2; dramatically aberrant localization
with decreased nuclear rim staining and formation of
intranuclear foci; distribution of endogenous LMNA, LMNB1
and LMNB2 are altered in cells expressing this mutant;
causes an increased loss of endogenous EMD from the nuclear
envelope; interacts with itself and with wild-type LMNA and
LMNB1; no decrease in the stability compared with wild-
type; dbSNP:rs59653062)"
/evidence="ECO:0000269|PubMed:10939567,
ECO:0000269|PubMed:11792809"
/id="VAR_009986"
VARIANT 377
/note="R -> H (in EDMD2; no obvious effect on nuclear
morphology in cultured skin fibroblasts from heterozygous
patients; no effect on protein level; dbSNP:rs61672878)"
/evidence="ECO:0000269|PubMed:10814726,
ECO:0000269|PubMed:12628721, ECO:0000269|PubMed:12673789,
ECO:0000269|PubMed:15372542, ECO:0000269|PubMed:15744034,
ECO:0000269|PubMed:17136397"
/id="VAR_016205"
VARIANT 377
/note="R -> L (in EDMD2; dbSNP:rs61672878)"
/evidence="ECO:0000269|PubMed:12032588,
ECO:0000269|PubMed:12649505"
/id="VAR_039777"
VARIANT 380
/note="L -> S (in MDCL; dbSNP:rs121912495)"
/evidence="ECO:0000269|PubMed:18551513"
/id="VAR_063591"
VARIANT 386
/note="R -> K (in EDMD2; dramatically aberrant localization
with decreased nuclear rim staining and formation of
intranuclear foci; distribution of endogenous LMNA, LMNB1
and LMNB2 are altered in cells expressing this mutant;
causes an increased loss of endogenous EMD from the nuclear
envelope; interacts with itself and with wild-type LMNA and
LMNB1; no decrease in the stability compared with wild-
type; dbSNP:rs267607545)"
/evidence="ECO:0000269|PubMed:10939567,
ECO:0000269|PubMed:11792809, ECO:0000269|PubMed:12649505,
ECO:0000269|PubMed:20848652"
/id="VAR_009987"
VARIANT 388
/note="R -> H (in CMD1A; no effect on nuclear morphology
but restricts lamin A to the cytoplasm; dbSNP:rs267607576)"
/evidence="ECO:0000269|PubMed:20160190"
/id="VAR_070180"
VARIANT 399
/note="R -> C (in FPLD2 and CMD1A; no effect on nuclear
morphology and lamin A localization; dbSNP:rs58672172)"
/evidence="ECO:0000269|PubMed:17250669,
ECO:0000269|PubMed:20160190"
/id="VAR_039778"
VARIANT 401
/note="R -> C (in EDMD2; abnormal nuclear localization in a
honeycomb expression pattern in about 22% of cultured skin
fibroblasts from heterozygous patients; enhances the
interaction with SYNE2; no effect on nuclear localization;
no effect on protein level; dbSNP:rs61094188)"
/evidence="ECO:0000269|PubMed:12467752,
ECO:0000269|PubMed:15372542, ECO:0000269|PubMed:23977161"
/id="VAR_072818"
VARIANT 411
/note="G -> D (probable disease-associated variant found in
patients with metabolic syndromes; no effect on nuclear
lamin A localization; no effect on the interaction with
SYNE2; dbSNP:rs267607647)"
/evidence="ECO:0000269|PubMed:21724554,
ECO:0000269|PubMed:23977161"
/id="VAR_072819"
VARIANT 413
/note="G -> C (found in patients with skeletal and cardiac
muscular dystrophies; no effect on nuclear lamin A
localization; no effect on the interaction with SYNE2;
dbSNP:rs766811975)"
/evidence="ECO:0000269|PubMed:23977161"
/id="VAR_072820"
VARIANT 415
/note="V -> I (rare variant; found in patients with atrial
fibrillation; unknown pathological significance; no effect
on nuclear lamin A localization; enhances the interaction
with SYNE2; causes nuclear deformations in heat shock
experiments; dbSNP:rs267607606)"
/evidence="ECO:0000269|PubMed:19427440,
ECO:0000269|PubMed:23977161"
/id="VAR_072821"
VARIANT 419
/note="R -> C (found in patients with lipodystrophy; no
effect on nuclear lamin A localization; no effect on the
interaction with SYNE2; dbSNP:rs755686359)"
/evidence="ECO:0000269|PubMed:23977161"
/id="VAR_072822"
VARIANT 421
/note="L -> P (probable disease-associated variant found in
patient with severe metabolic syndrome; no effect on
nuclear lamin A localization; no effect on the interaction
with SYNE2; dbSNP:rs267607564)"
/evidence="ECO:0000269|PubMed:17711925,
ECO:0000269|PubMed:23977161"
/id="VAR_072823"
VARIANT 427
/note="R -> G (found in patients with skeletal and cardiac
muscular dystrophies; unknown pathological significance; no
effect on nuclear lamin A localization; no effect on the
interaction with SYNE2)"
/evidence="ECO:0000269|PubMed:23977161"
/id="VAR_072824"
VARIANT 435
/note="R -> C (in CMD1A; dbSNP:rs150840924)"
/evidence="ECO:0000269|PubMed:14684700"
/id="VAR_039779"
VARIANT 439
/note="R -> C (in FPLD2; increase in nuclear blebbing and
formation of honeycomb-like structures in the nuclei with
no accumulation of prelamin A in skin fibroblasts; causes
oligomerization of the C-terminal globular domain of lamins
A and C under no-reducing conditions and increases binding
affinity for DNA; increases sensitivity to oxidative
stress; no significant differences in stability and
structure compared with the wild-type; dbSNP:rs62636506)"
/evidence="ECO:0000269|PubMed:19220582"
/id="VAR_070181"
VARIANT 446
/note="D -> V (in EDMD2; dbSNP:rs58541611)"
/evidence="ECO:0000269|PubMed:14684700"
/id="VAR_039780"
VARIANT 449
/note="G -> D (in EDMD2; dbSNP:rs267607637)"
/evidence="ECO:0000269|PubMed:20848652"
/id="VAR_064971"
VARIANT 453
/note="R -> P (in MDCL; dbSNP:rs267607598)"
/evidence="ECO:0000269|PubMed:18551513"
/id="VAR_063592"
VARIANT 453
/note="R -> W (in EDMD2; abnormal nuclear localization;
forms nuclear foci in about 8% of cultured skin fibroblasts
from heterozygous patients; interacts with itself and with
wild-type LMNA and LMNB1; no effect on protein level;
dbSNP:rs58932704)"
/evidence="ECO:0000269|PubMed:10080180,
ECO:0000269|PubMed:10739764, ECO:0000269|PubMed:10939567,
ECO:0000269|PubMed:11503164, ECO:0000269|PubMed:11792809,
ECO:0000269|PubMed:14684700, ECO:0000269|PubMed:15372542,
ECO:0000269|PubMed:20848652"
/id="VAR_009988"
VARIANT 454
/note="L -> P (in EDMD2; dbSNP:rs267607638)"
/evidence="ECO:0000269|PubMed:20848652"
/id="VAR_064972"
VARIANT 455
/note="R -> P (in MDCL; dbSNP:rs267607597)"
/evidence="ECO:0000269|PubMed:18551513"
/id="VAR_063593"
VARIANT 456
/note="N -> D (in MDCL; dbSNP:rs267607599)"
/evidence="ECO:0000269|PubMed:18551513"
/id="VAR_063594"
VARIANT 456
/note="N -> I (in EDMD2; mislocalized in the nucleus; does
not alter nuclear size or shape; dbSNP:rs60992550)"
/evidence="ECO:0000269|PubMed:11503164,
ECO:0000269|PubMed:20848652"
/id="VAR_039781"
VARIANT 456
/note="N -> K (in EDMD2; dbSNP:rs61235244)"
/evidence="ECO:0000269|PubMed:10939567"
/id="VAR_039782"
VARIANT 461
/note="D -> Y (in EDMD2; dbSNP:rs267607642)"
/evidence="ECO:0000269|PubMed:20848652"
/id="VAR_064973"
VARIANT 465
/note="G -> D (in FPLD2; dbSNP:rs61282106)"
/evidence="ECO:0000269|PubMed:10739751"
/id="VAR_009989"
VARIANT 467
/note="W -> R (in EDMD2; dbSNP:rs267607639)"
/evidence="ECO:0000269|PubMed:20848652"
/id="VAR_064974"
VARIANT 469
/note="I -> T (in EDMD2; dbSNP:rs57394692)"
/evidence="ECO:0000269|PubMed:10739764"
/id="VAR_009990"
VARIANT 471
/note="R -> C (in HGPS; dbSNP:rs28928902)"
/evidence="ECO:0000269|PubMed:12768443"
/id="VAR_017662"
VARIANT 471
/note="R -> H (in CMD1A; no effect on nuclear morphology
and lamin A localization; dbSNP:rs267607578)"
/evidence="ECO:0000269|PubMed:20160190"
/id="VAR_070182"
VARIANT 481
/note="Y -> H (in EDMD2; dbSNP:rs57747780)"
/evidence="ECO:0000269|PubMed:11525883"
/id="VAR_039783"
VARIANT 482
/note="R -> L (in FPLD2; abnormal nuclear localization in a
honeycomb expression pattern in about 10% of cultured skin
fibroblasts from heterozygous patients; no effect on
protein level; dbSNP:rs11575937)"
/evidence="ECO:0000269|PubMed:10655060,
ECO:0000269|PubMed:15372542"
/id="VAR_009991"
VARIANT 482
/note="R -> Q (in FPLD2; interacts with itself and with
wild-type LMNA and LMNB1; no decrease in the stability
compared with wild-type; dbSNP:rs11575937)"
/evidence="ECO:0000269|PubMed:10587585,
ECO:0000269|PubMed:10739751, ECO:0000269|PubMed:11792809"
/id="VAR_009992"
VARIANT 482
/note="R -> W (in FPLD2; interacts with itself and with
wild-type LMNA and LMNB1; no decrease in the stability
compared with wild-type; decreases binding affinity for
DNA; increases sensitivity to oxidative stress;
dbSNP:rs57920071)"
/evidence="ECO:0000269|PubMed:10655060,
ECO:0000269|PubMed:10739751, ECO:0000269|PubMed:11792809,
ECO:0000269|PubMed:19220582"
/id="VAR_009993"
VARIANT 486
/note="K -> N (in FPLD2; interacts with itself and with
wild-type LMNA and LMNB1; no decrease in the stability
compared with wild-type; dbSNP:rs59981161)"
/evidence="ECO:0000269|PubMed:11792809"
/id="VAR_009994"
VARIANT 488
/note="T -> P (found in patient with atrial fibrillation;
dbSNP:rs267607607)"
/evidence="ECO:0000269|PubMed:19427440"
/id="VAR_072825"
VARIANT 515
/note="K -> E (in FPLD2)"
/evidence="ECO:0000269|PubMed:24485160"
/id="VAR_071968"
VARIANT 520
/note="W -> S (in EDMD2; interacts with itself and with
wild-type LMNA and LMNB1; no decrease in the stability
compared with wild-type; dbSNP:rs58362413)"
/evidence="ECO:0000269|PubMed:10939567,
ECO:0000269|PubMed:11792809"
/id="VAR_039784"
VARIANT 523
/note="G -> R (in CMD1A; unknown pathological significance;
dbSNP:rs201583907)"
/evidence="ECO:0000269|PubMed:21846512"
/id="VAR_067258"
VARIANT 527
/note="R -> C (in HGPS; dbSNP:rs57318642)"
/evidence="ECO:0000269|PubMed:12768443"
/id="VAR_017663"
VARIANT 527
/note="R -> H (in MADA; dbSNP:rs57520892)"
/evidence="ECO:0000269|PubMed:12075506"
/id="VAR_018727"
VARIANT 527
/note="R -> P (in EDMD2 and FPLD2; interacts with itself
and with wild-type LMNA and LMNB1; reduced binding to SUN1;
abnormal nuclear localization; forms nuclear foci in about
13% of cultured skin fibroblasts from heterozygous
patients; no effect on protein level; dbSNP:rs57520892)"
/evidence="ECO:0000269|PubMed:10080180,
ECO:0000269|PubMed:10739764, ECO:0000269|PubMed:10939567,
ECO:0000269|PubMed:11503164, ECO:0000269|PubMed:11792809,
ECO:0000269|PubMed:12196663, ECO:0000269|PubMed:12649505,
ECO:0000269|PubMed:15372542, ECO:0000269|PubMed:15744034,
ECO:0000269|PubMed:19933576, ECO:0000269|PubMed:20848652"
/id="VAR_009995"
VARIANT 528
/note="T -> K (in EDMD2; interacts with itself and with
wild-type LMNA and LMNB1; no decrease in the stability
compared with wild-type; dbSNP:rs57629361)"
/evidence="ECO:0000269|PubMed:10739764,
ECO:0000269|PubMed:10939567, ECO:0000269|PubMed:11792809,
ECO:0000269|PubMed:20848652"
/id="VAR_009996"
VARIANT 528
/note="T -> R (in EDMD2; dbSNP:rs57629361)"
/evidence="ECO:0000269|PubMed:14684700,
ECO:0000269|PubMed:20848652"
/id="VAR_039785"
VARIANT 529
/note="A -> V (in MADA; dbSNP:rs60580541)"
/evidence="ECO:0000269|PubMed:15998779"
/id="VAR_034709"
VARIANT 530
/note="L -> P (in EDMD2; interacts with itself and with
wild-type LMNA and LMNB1; reduced binding to SUN1; no
decrease in the stability compared with wild-type;
dbSNP:rs60934003)"
/evidence="ECO:0000269|PubMed:10080180,
ECO:0000269|PubMed:11792809, ECO:0000269|PubMed:19933576"
/id="VAR_009997"
VARIANT 541
/note="R -> C (in CMD1A; grossly abnormal nuclear shape
with the nuclear envelope producing prominent lobules in
about 10% of cultured skin fibroblasts from heterozygous
patients; dbSNP:rs56984562)"
/evidence="ECO:0000269|PubMed:14675861,
ECO:0000269|PubMed:15372542, ECO:0000269|PubMed:19167105"
/id="VAR_039786"
VARIANT 541
/note="R -> H (in EDMD2; dbSNP:rs61444459)"
/evidence="ECO:0000269|PubMed:14684700"
/id="VAR_039787"
VARIANT 541
/note="R -> P (in EDMD2; mis-localized in the nucleus; does
not alter nuclear size or shape; dbSNP:rs61444459)"
/evidence="ECO:0000269|PubMed:20848652"
/id="VAR_064975"
VARIANT 541
/note="R -> S (in EDMD2 and CMD1A; modest and non-specific
nuclear membrane alterations; the phenotype is entirely
reversed by coexpression of the S-541 mutation and wild-
type lamin-C; dbSNP:rs56984562)"
/evidence="ECO:0000269|PubMed:16061563,
ECO:0000269|PubMed:20848652"
/id="VAR_039788"
VARIANT 542
/note="K -> N (in HGPS; dbSNP:rs56673169)"
/evidence="ECO:0000269|PubMed:15286156"
/id="VAR_034710"
VARIANT 573
/note="S -> L (in CMD1A, FPLD2 and MADA; dbSNP:rs60890628)"
/evidence="ECO:0000269|PubMed:12628721,
ECO:0000269|PubMed:16278265, ECO:0000269|PubMed:17250669"
/id="VAR_039789"
VARIANT 578
/note="E -> V (in an atypical progeroid patient; diagnosed
as Werner syndrome; dbSNP:rs61224243)"
/evidence="ECO:0000269|PubMed:15060110"
/id="VAR_039790"
VARIANT 582
/note="R -> H (in FPLD2; dbSNP:rs57830985)"
/evidence="ECO:0000269|PubMed:10739751"
/id="VAR_009998"
VARIANT 602
/note="G -> S (in EDMD2; dbSNP:rs60662302)"
/evidence="ECO:0000269|PubMed:20848652"
/id="VAR_064976"
VARIANT 608
/note="G -> S (in HGPS; reduced binding to SUN1; may affect
splicing by activating a cryptic splice donor site;
dbSNP:rs61064130)"
/evidence="ECO:0000269|PubMed:12714972,
ECO:0000269|PubMed:12768443, ECO:0000269|PubMed:19933576"
/id="VAR_017664"
VARIANT 624
/note="R -> H (in EDMD2; dbSNP:rs13768)"
/evidence="ECO:0000269|PubMed:11503164"
/id="VAR_039791"
VARIANT 631
/note="G -> D (probable disease-associated variant found in
a patient with metabolic syndrome; dbSNP:rs267607648)"
/evidence="ECO:0000269|PubMed:21724554"
/id="VAR_072826"
VARIANT 644
/note="R -> C (in HGPS and EDMD2; partially inhibits tail
cleavage; dbSNP:rs142000963)"
/evidence="ECO:0000269|PubMed:15060110,
ECO:0000269|PubMed:20848652, ECO:0000269|PubMed:22355414"
/id="VAR_039792"
MUTAGEN 22
/note="S->A: Decreased accumulation to the double-strand
break (DSB) sites."
/evidence="ECO:0000269|PubMed:31548606"
MUTAGEN 22
/note="S->D: Increased accumulation to the double-strand
break (DSB) sites."
/evidence="ECO:0000269|PubMed:31548606"
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 358
/note="E->K: Loss of interaction with IFFO1."
/evidence="ECO:0000269|PubMed:31548606"
MUTAGEN 386
/note="R->M: Loss of interaction with IFFO1."
/evidence="ECO:0000269|PubMed:31548606"
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"
CONFLICT 340
/note="E -> K (in Ref. 5; BAG58344)"
/evidence="ECO:0000305"
STRAND 20..22
/evidence="ECO:0007829|PDB:6YF5"
STRAND 25..27
/evidence="ECO:0007829|PDB:6YF5"
HELIX 28..70
/evidence="ECO:0007829|PDB:6YF5"
HELIX 252..278
/evidence="ECO:0007829|PDB:6JLB"
HELIX 316..384
/evidence="ECO:0007829|PDB:1X8Y"
STRAND 430..436
/evidence="ECO:0007829|PDB:6GHD"
STRAND 438..445
/evidence="ECO:0007829|PDB:1IFR"
STRAND 449..456
/evidence="ECO:0007829|PDB:1IFR"
STRAND 458..460
/evidence="ECO:0007829|PDB:1IFR"
HELIX 464..466
/evidence="ECO:0007829|PDB:1IVT"
STRAND 468..473
/evidence="ECO:0007829|PDB:1IFR"
STRAND 479..482
/evidence="ECO:0007829|PDB:1IFR"
STRAND 494..499
/evidence="ECO:0007829|PDB:1IFR"
HELIX 500..502
/evidence="ECO:0007829|PDB:3GEF"
TURN 508..510
/evidence="ECO:0007829|PDB:1IFR"
STRAND 511..514
/evidence="ECO:0007829|PDB:1IFR"
STRAND 526..531
/evidence="ECO:0007829|PDB:1IFR"
STRAND 537..543
/evidence="ECO:0007829|PDB:1IFR"
CONFLICT P02545-4:556
/note="G -> R (in Ref. 5; BAG58344)"
/evidence="ECO:0000305"
SEQUENCE 664 AA; 74139 MW; E0855F7699F0318B CRC64;
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


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Related Genes :
[LMNA LMN1] Prelamin-A/C [Cleaved into: Lamin-A/C (70 kDa lamin) (Renal carcinoma antigen NY-REN-32)]
[PPP2R5C KIAA0044] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform (PP2A B subunit isoform B'-gamma) (PP2A B subunit isoform B56-gamma) (PP2A B subunit isoform PR61-gamma) (PP2A B subunit isoform R5-gamma) (Renal carcinoma antigen NY-REN-29)
[HSP90AA1 HSP90A HSPC1 HSPCA] Heat shock protein HSP 90-alpha (EC 3.6.4.10) (Heat shock 86 kDa) (HSP 86) (HSP86) (Lipopolysaccharide-associated protein 2) (LAP-2) (LPS-associated protein 2) (Renal carcinoma antigen NY-REN-38)
[Lmna Lmn1] Prelamin-A/C [Cleaved into: Lamin-A/C]
[PLAAT3 HRASLS3 HREV107 PLA2G16] Phospholipase A and acyltransferase 3 (EC 2.3.1.-) (EC 3.1.1.32) (EC 3.1.1.4) (Adipose-specific phospholipase A2) (AdPLA) (Group XVI phospholipase A1/A2) (H-rev 107 protein homolog) (H-REV107) (HREV107-1) (HRAS-like suppressor 1) (HRAS-like suppressor 3) (HRSL3) (HREV107-3) (Renal carcinoma antigen NY-REN-65)
[Lmna Lmn1] Prelamin-A/C [Cleaved into: Lamin-A/C]
[USH1C AIE75] Harmonin (Antigen NY-CO-38/NY-CO-37) (Autoimmune enteropathy-related antigen AIE-75) (Protein PDZ-73) (Renal carcinoma antigen NY-REN-3) (Usher syndrome type-1C protein)
[NEDD9 CASL CASS2] Enhancer of filamentation 1 (hEF1) (CRK-associated substrate-related protein) (CAS-L) (CasL) (Cas scaffolding protein family member 2) (Neural precursor cell expressed developmentally down-regulated protein 9) (NEDD-9) (Renal carcinoma antigen NY-REN-12) (p105) [Cleaved into: Enhancer of filamentation 1 p55]
[TRMT10C MRPP1 RG9MTD1] tRNA methyltransferase 10 homolog C (HBV pre-S2 trans-regulated protein 2) (Mitochondrial ribonuclease P protein 1) (Mitochondrial RNase P protein 1) (RNA (guanine-9-)-methyltransferase domain-containing protein 1) (Renal carcinoma antigen NY-REN-49) (mRNA methyladenosine-N(1)-methyltransferase) (EC 2.1.1.-) (tRNA (adenine(9)-N(1))-methyltransferase) (EC 2.1.1.218) (tRNA (guanine(9)-N(1))-methyltransferase) (EC 2.1.1.221)
[CEP83 CCDC41] Centrosomal protein of 83 kDa (Cep83) (Coiled-coil domain-containing protein 41) (Renal carcinoma antigen NY-REN-58)
[GCC2 KIAA0336 RANBP2L4] GRIP and coiled-coil domain-containing protein 2 (185 kDa Golgi coiled-coil protein) (GCC185) (CLL-associated antigen KW-11) (CTCL tumor antigen se1-1) (Ran-binding protein 2-like 4) (RanBP2L4) (Renal carcinoma antigen NY-REN-53)
[KIF21A KIAA1708 KIF2] Kinesin-like protein KIF21A (Kinesin-like protein KIF2) (Renal carcinoma antigen NY-REN-62)
[ROCK1] Rho-associated protein kinase 1 (EC 2.7.11.1) (Renal carcinoma antigen NY-REN-35) (Rho-associated, coiled-coil-containing protein kinase 1) (Rho-associated, coiled-coil-containing protein kinase I) (ROCK-I) (p160 ROCK-1) (p160ROCK)
[NEK1 KIAA1901] Serine/threonine-protein kinase Nek1 (EC 2.7.11.1) (Never in mitosis A-related kinase 1) (NimA-related protein kinase 1) (Renal carcinoma antigen NY-REN-55)
[MED6 ARC33] Mediator of RNA polymerase II transcription subunit 6 (Activator-recruited cofactor 33 kDa component) (ARC33) (Mediator complex subunit 6) (hMed6) (Renal carcinoma antigen NY-REN-28)
[YTHDF2 HGRG8] YTH domain-containing family protein 2 (DF2) (CLL-associated antigen KW-14) (High-glucose-regulated protein 8) (Renal carcinoma antigen NY-REN-2)
[EPHB2 DRT EPHT3 EPTH3 ERK HEK5 TYRO5] Ephrin type-B receptor 2 (EC 2.7.10.1) (Developmentally-regulated Eph-related tyrosine kinase) (ELK-related tyrosine kinase) (EPH tyrosine kinase 3) (EPH-like kinase 5) (EK5) (hEK5) (Renal carcinoma antigen NY-REN-47) (Tyrosine-protein kinase TYRO5) (Tyrosine-protein kinase receptor EPH-3) [Cleaved into: EphB2/CTF1; EphB2/CTF2]
[STK11 LKB1 PJS] Serine/threonine-protein kinase STK11 (EC 2.7.11.1) (Liver kinase B1) (LKB1) (hLKB1) (Renal carcinoma antigen NY-REN-19)
[LIMS1 PINCH PINCH1] LIM and senescent cell antigen-like-containing domain protein 1 (Particularly interesting new Cys-His protein 1) (PINCH-1) (Renal carcinoma antigen NY-REN-48)
[CTNNA1] Catenin alpha-1 (Alpha E-catenin) (Cadherin-associated protein) (Renal carcinoma antigen NY-REN-13)
[ECI2 DRS1 HCA88 PECI] Enoyl-CoA delta isomerase 2 (EC 5.3.3.8) (DRS-1) (Delta(3),delta(2)-enoyl-CoA isomerase) (D3,D2-enoyl-CoA isomerase) (Diazepam-binding inhibitor-related protein 1) (DBI-related protein 1) (Dodecenoyl-CoA isomerase) (Hepatocellular carcinoma-associated antigen 88) (Peroxisomal 3,2-trans-enoyl-CoA isomerase) (pECI) (Renal carcinoma antigen NY-REN-1)
[IRAK4] Interleukin-1 receptor-associated kinase 4 (IRAK-4) (EC 2.7.11.1) (Renal carcinoma antigen NY-REN-64)
[RBPJ IGKJRB IGKJRB1 RBPJK RBPSUH] Recombining binding protein suppressor of hairless (CBF-1) (J kappa-recombination signal-binding protein) (RBP-J kappa) (RBP-J) (RBP-JK) (Renal carcinoma antigen NY-REN-30)
[RLIM RNF12] E3 ubiquitin-protein ligase RLIM (EC 2.3.2.27) (LIM domain-interacting RING finger protein) (RING finger LIM domain-binding protein) (R-LIM) (RING finger protein 12) (RING-type E3 ubiquitin transferase RLIM) (Renal carcinoma antigen NY-REN-43)
[BCR BCR1 D22S11] Breakpoint cluster region protein (EC 2.7.11.1) (Renal carcinoma antigen NY-REN-26)
[CRYAB CRYA2 HSPB5] Alpha-crystallin B chain (Alpha(B)-crystallin) (Heat shock protein beta-5) (HspB5) (Renal carcinoma antigen NY-REN-27) (Rosenthal fiber component)
[AARS1 AARS] Alanine--tRNA ligase, cytoplasmic (EC 6.1.1.7) (Alanyl-tRNA synthetase) (AlaRS) (Renal carcinoma antigen NY-REN-42)
[nnr nnrD nnrE A3104_11915 A3S30_19665 A3T81_21675 A3U32_23435 A3V03_21575 A3V89_22115 A3W57_22140 A3X15_22160 A3X55_21685 A3Y76_14605 A4N07_22285 A4O05_13700 A4O41_05265 A4R48_22080 A9U69_22255 AAA76_20340 AAB27_18985 AAB79_03070 AAC35_06000 ADQ28_23005 AF497_21520 AGM99_01505 AHN93_01515 AKH62_11790 AL144_04480 AL168_02095 AL184_03665 AQ530_03515 AU613_19740 AVA38_18590 AVC05_01495 AVL16_22555 AWT30_09535 AXX99_06020 B1265_01505 B1398_16630 B1642_23230 B1P38_04920 B2E31_03355 B4V59_03840 B4W90_14915 B6362_05595 B7Q27_01505 B8Y16_05865 B8Z46_22290 B9C90_07460 B9C96_05405 B9M14_07545 B9O84_03660 BBQ66_05585 BIC00_08330 BIC13_14510 BK110_09575 BKM50_11315 BMS46_01505 BMU56_09035 BZ203_06955 BZZ88_08070 C5W43_08230 CA117_06625 CB102_00985 CB119_00985 CB198_09030 CB380_07720 CB535_06910 CB570_00990 CB646_05015 CBM67_21760 CBM76_21380 CBZ90_21695 CC339_04035 CC403_03335 CC453_02040 CC652_09145 CC971_07405 CCP17_01500 CDZ72_03200 CE70_13525 CED07_02655 CEQ70_07505 CFF58_07550 CFF59_07100 CHN22_19910 CIX60_07020 CPS79_03750 CQO33_04955 CSG22_03545 CVR97_09130 D4361_14445 D4387_09005 D4422_03410 D5823_20700 D5N86_01575 D5N95_09780 D5O82_05670 D5P17_06815 D5X47_11065 D5Y28_07745 D6422_22155 D6J79_11255 D8S24_10700 DD95_00965 DLB93_10975 DLR28_11595 DMI89_05845 DMO92_10880 DN165_10610 DNB97_07755 DNM27_05145 DNZ37_05180 DO533_23225 DP680_10960 DPB42_02650 DPD91_03510 DPF41_01580 DPF68_05705 DPS76_03370 DQD22_12500 DQR44_06210 DRM14_08770 DRR75_10500 DRT38_04095 DRT61_07200 DRV05_05125 DSF94_09655 DSG41_17540 DTF68_08880 DU071_23815 DU223_08415 DU657_03970 DU879_06050 DUV75_11535 DWU22_16565 DY580_23265 DYM27_14705 E0935_23310 E1A11_11805 E6W45_09715 EBD14_10340 EBK21_08710 EC404_02370 EEQ30_18160 EER35_22295 EHB09_20270 EL822_04855 ELS01_25275 EPB30_12745 EQG93_06630 EVY71_20440 EW905_04205 F0D96_20705 F2P00_23020 F3Q97_10065 F3R12_05435 F9G02_04855 F9O44_00990 FEM52_07875 FGZ46_01505 FJM64_10520 FQC24_12860 FQX78_09970 G0038_10260 G0040_04475 G0042_07685 G0045_12485 G0047_13855 G0048_12905 G0051_11450 G0052_23590 G0059_11030 G0061_11920 G0062_12500 G0063_16275 G0067_13985 G0069_12775 G0070_08950 G0071_12535 G0072_10310 G0074_12900 G0076_15880 G0077_12835 G0080_14965 G0084_15965 G0086_13840 G0087_12905 G0088_11920 G0089_06320 G0090_22420 G0094_13250 G0100_12665 G0101_09385 G0102_12000 G0111_21240 G0113_13510 G0117_14430 G0123_12905 G0124_09920 G0148_23065 G0157_12325 G0170_23555 G0A05_04765 G0A32_05580 G0A39_06255 G0A43_05040 G0A44_08470 G0A46_12965 G0A50_23545 G0A51_09275 G0A52_05740 G0A53_07565 G0A56_07500 G0A58_07465 G0A60_17995 G0A61_07660 G0A63_04815 G0A66_08960 G0A67_07200 G0A68_05690 G0A70_08885 G0A73_09480 G0A76_08590 G0A79_21840 G0A92_10225 G0A96_08865 G0A97_09115 G0B03_12655 G0B05_09390 G0B07_10975 G0B08_22950 G0B12_10720 G0B96_04785 G0C03_12575 G0C04_15660 G0C34_07535 G0E15_19110 G0E20_06140 G0G84_16105 G0J24_13730 G0J26_12305 G0J27_07115 G0J28_11980 G0J31_06745 G0J33_11145 G0J34_13415 G0J36_08765 G0J37_20200 G0J40_10310 G0J43_01545 G0J44_20410 G0J45_08730 G0J46_15460 G0J47_19830 G0J49_09500 G0J50_01555 G0J51_10340 G0J53_08850 G0J55_19430 G0J58_22670 G0J59_05635 G0J62_17815 G0J65_08725 G0J66_21925 G0J67_22665 G0J69_22465 G0J71_22025 G0J73_03995 G0J76_22400 G0J79_23305 G0J81_19270 G0J82_03865 G0J85_22590 G0J89_01555 G0J92_05645 G0J94_04410 G0J96_06855 G0J97_18065 G0K00_04765 G0K02_10715 G0K03_10995 G0K04_02780 G0K05_22985 G0K07_22440 G0K10_01565 G0K13_11525 G0K15_08960 G0K16_08385 G0K18_04715 G0K19_01430 G0K20_20560 G0K23_09085 G0K25_22280 G0K26_23210 G0K28_09270 G0K30_24080 G0K31_21360 G0K32_21370 G0K33_22125 G0K37_22810 G0K38_06715 G0K39_19020 G0K41_13810 G0K42_10880 G0K44_22730 G0K46_22315 G0K47_08680 G0K48_01555 G0K49_05675 G0K52_04405 G0K53_04950 G0K56_04645 G0K58_19550 G0K59_01555 G0K61_05520 G0K65_10910 G0K68_01545 G0K70_23295 G0K72_19895 G0K74_23665 G0K75_23255 G0K78_05095 G0K80_01550 G0K83_07510 G0K84_09810 G0K85_01555 G0K88_000683 G0K89_000568 G0K90_000508 G0K95_003755 G0L00_001859 G0L02_000638 G0L03_05870 G0L06_06150 G0L07_08375 G0L10_19990 G0L14_06770 G0L15_02230 G0L18_05635 G0L19_08200 G0L20_14575 G0L24_07325 G0L25_04935 G0L29_02685 G0L31_03775 G0L32_04710 G0L34_14860 G0L35_12865 G0L36_13035 G0L37_07105 G0L38_11275 G0L40_12750 G0L42_10750 G0L48_09545 G0L49_06730 G0L51_08560 G0L52_09595 G0L55_08545 G0L59_07010 G0L62_08790 G0L63_08395 G0L65_11350 G0L67_07070 G0L68_21135 G0L70_01495 G0L73_21325 G0L76_10450 G0L77_03505 G0L78_05795 G0L79_07425 G0L83_10615 G0L86_001595 G0L88_06510 G0L89_08150 G0L91_03255 G0L93_04345 G0L96_08625 G0L98_04340 G0M00_03415 G0M02_06865 G0M05_13160 G0M06_001385 G0M13_001162 G0M14_16700 G0M16_07260 G0M18_003813 G0M21_02335 G0M22_001379 G0M25_001199 G0M26_21090 G0M29_001394 G0M30_19890 G0M33_23770 G0M35_21125 G0M36_15025 G0M38_15125 G0M39_17915 G0M41_17560 G0M45_03860 G0M46_001382 G0M48_003206 G0M53_18855 G0M55_07255 G0M56_08145 G0M58_08160 G0M63_07175 G0M65_06665 G0M67_08355 G0N45_22995 G0N48_14040 G0N51_03825 G0N53_22980 G0N55_11400 G0N57_00010 G0N58_23005 G0N59_23010 G0N60_23095 G0N61_09375 G0N62_22990 G0N64_11025 G0N65_22930 G0N66_23085 G0N67_23065 G0N71_04780 G0N75_16110 G0N78_21895 G0N82_10545 G0N84_15350 G0N85_24040 G0N86_23095 G0N88_10630 G0N89_10800 G0N90_22705 G0N92_17760 G0N94_20330 G0N95_23625 G0N98_20980 G0N99_05765 G0O00_05695 G0O10_23100 G0O14_22860 G0O15_07010 G0O18_13745 G0O19_12975 G0O20_05410 G0O22_22985 G0O25_22615 G0O27_09925 G0O31_10850 G0O32_22285 G0O36_10155 G0O37_07040 G0O39_16130 G0O40_13640 G0O41_10340 G0O42_04595 G0O43_15605 G0O44_11700 G0O47_09535 G0O52_22165 G0O55_11440 G0O57_04595 G0O58_14540 G0O59_06805 G0O60_22680 G0O63_06090 G0O66_07220 G0O68_10375 G0O70_11530 G0O71_09735 G0O74_04410 G0O75_09695 G0O77_22825 G0O78_09545 G0O80_11320 G0O81_07145 G0O82_16905 G0O84_11320 G0O85_15450 G0O86_04490 G0O87_13110 G0O88_07290 G0O89_16570 G0O92_14075 G0O93_16785 G0O94_04825 G0O97_23030 G0O99_03030 G0P00_05830 G0P01_06470 G0P02_09955 G0P05_04495 G0P06_22950 G0P08_07305 G0P12_03840 G0P13_16225 G0P17_10905 G0P18_15755 G0P19_12705 G0P24_08485 G0P26_09735 G0P28_11835 G0P30_09670 G0P31_13405 G0P36_11580 G0P37_07140 G0P41_06990 G0P44_09010 G0P45_10700 G0P48_10900 G0P49_04240 G0P52_08565 G0P53_13455 G0P56_10915 G0P57_09940 G0P58_22400 G0P63_18010 G0P65_10045 G0P67_06260 G0P68_03795 G0P69_22335 G0P73_18280 G0P75_23960 G0P76_04350 G1N61_10720 G1N64_12415 G1N66_12405 G1N68_12100 G1N71_13250 G1N72_12410 G1N86_13550 G1N87_12430 G1N91_14270 G1O00_12660 G1O02_13555 G1O04_12420 G1O05_12405 G1O08_13535 G1O10_12410 G1O12_13560 G1O16_13555 G1O17_12180 G1O18_13555 G1O20_13550 G1O23_12420 G1O25_13545 G1O26_13550 G1O27_12485 G1O28_13315 G1O29_12480 G1O32_13540 G1O34_13620 G1O38_13960 G1O40_13560 G1O43_13545 G1O46_12060 G1O48_13325 G1O49_12535 G1O51_13550 G1O53_13615 G1O62_13555 G1O63_13540 G1O65_13325 G1O67_12870 G1O68_11720 G1O69_13110 G1O71_13105 G1O72_11855 G1O76_13635 G1O77_13550 G1O80_13640 G1O81_12410 G1O83_12005 G1O84_13630 G1O87_13635 G1O88_13625 G1O89_13560 G1O90_13630 G1O93_13625 G1O94_13620 G1O96_13625 G1P02_13620 G1P03_13280 G1P06_13300 G1P09_12575 G1P10_13575 G1P12_13625 G1P14_10175 G1P15_13970 G1P17_13640 G1P19_13625 G1P23_13630 G1P24_13545 G1P25_11855 G1P26_13545 G1P29_13260 G1P31_13615 G1P35_13550 G1P36_13545 G1P37_13205 G1P40_12430 G1P44_13550 G1P45_13630 G1P47_12485 G1P48_13630 G1P51_13630 G1P52_13205 G1P53_13205 G1P54_13640 G1P55_13320 G1P56_13610 G1P57_10720 G1P58_13620 G1P59_13635 G1P61_23980 G1P64_13325 G1P67_13625 G1P69_13540 G1P72_12515 G1P75_13570 G1P76_13215 G1P78_12495 G1P83_12225 G1P84_13555 G1P87_13625 G1P90_13360 G1P91_13620 G1Q03_13235 G1Q08_12720 G1Q67_13630 G1Q78_09875 G1Q81_11340 G1Q83_12495 G1Q84_08650 G1Q85_11365 G1Q86_11715 G1Q88_11725 G1Q90_12170 G1Q91_12420 G1Q93_09170 G1Q96_12385 G1Q98_11910 G1Q99_22335 G1R01_13545 G1R02_12655 G1R03_13625 G1R04_13570 G1R08_09245 G1R13_11975 G1R15_09440 G1R20_14345 G1R21_11475 G1R22_11285 G1R23_08760 G1R27_12005 G1R28_13075 G1R29_13635 G1R30_13320 G1R31_12250 G1R36_13635 G1R38_18180 G1R40_12255 G1R42_13550 G1R44_13315 G1R45_09940 G1R47_12850 G1R48_06440 G1R51_12400 G1R53_13630 G1R63_13630 G1R69_09725 G1R87_11980 G1R93_13230 G1S02_12495 G2203_22150 G2212_02390 G2218_05480 G2279_10500 G2290_05710 G2793_13060 G2918_01515 G2951_22815 G3221_001120 G3230_002225 G3231_004971 G3247_000621 G3248_004290 G3254_000657 G3263_001003 G3270_000223 G3275_001976 G3312_001342 G3336_003846 G3357_000830 G3369_001554 G3433_000423 G3460_002051 G3464_000047 G3593_001051 G3A35_04535 G3V06_004409 G3V14_001761 G3V17_001609 G3V21_004148 G3V56_001941 G3V57_003126 G3X03_004298 G4189_001618 G4190_004249 G4192_004192 G4198_004562 G4201_003798 G4202_000501 G4A01_003580 G4A73_001420 G4A83_004704 G4A85_001081 G4A87_001998 G4B68_002875 G4B72_004591 G4B74_004402 G4C74_001467 G4D32_001167 G4D46_001331 G4F88_03160 G4F89_21210 G4F91_20865 G4F92_03160 G4G47_000304 G4G62_000179 G4G67_004715 G4G68_000780 G4G75_001230 G4G76_001971 G4G79_000501 G4G97_000963 G4H00_001841 G4H04_001859 G4H07_000277 G4H08_000970 G4H18_001970 G4H21_002013 G4H24_001959 G4H63_001799 G4I66_002109 G4J07_003114 G4J08_001003 G4J11_003314 G4J12_003592 G4J18_002204 G4J20_000694 G4J37_001805 G4J39_003834 G4J41_001252 G4J45_004787 G4J90_001032 G4K02_004567 G4K03_004658 G4O54_001852 G4O56_000652 G4O59_004375 G4O60_004588 G4O67_004614 G4O69_001138 G4P29_002660 G4P83_002002 G4P85_001270 G4P89_000745 G4P91_004289 G4P93_000925 G4Q12_001216 G4Q28_001959 G4Q31_001958 G4Q50_001423 G4Q52_001423 G4Q59_000925 G4Q60_001509 G4Q63_001410 G4Q67_000417 G4Q94_000976 G4R01_002882 G4R02_000925 G4R15_001414 G4R16_001699 G4W68_001327 G4W73_003000 G4W86_001855 G4W87_002248 G4W88_003688 G4W91_000984 G4Y10_001706 G9269_001321 G9302_002068 G9304_000623 G9305_000797 G9309_000779 G9313_001438 G9314_004671 G9367_002779 G9381_001217 G9C24_000440 G9C41_004428 G9C46_004336 G9C47_004352 G9C49_004415 G9C57_002249 G9C64_001580 G9G03_000673 G9G04_001975 G9G34_002649 G9G36_001047 G9G45_002358 G9G50_004591 G9G62_003596 G9W19_000375 G9W28_000842 G9W45_004104 G9W52_000348 G9W63_004309 G9W65_001966 G9W79_001611 G9W95_001967 G9W96_001102 G9X40_004481 GB021_08410 GB040_02730 GB055_01495 GB076_03915 GB106_04175 GB114_03815 GB120_06665 GB122_01510 GB131_04255 GB139_07780 GB171_05240 GB209_06680 GB221_02485 GB224_18770 GB238_04475 GB280_15095 GB321_14890 GB331_05905 GB339_01505 GB342_22590 GB368_02475 GB372_02445 GB416_20360 GB452_19400 GB459_04825 GB466_07010 GB505_01510 GB510_08155 GB551_22950 GB567_07675 GB645_04690 GBS44_18590 GBS58_08845 GBV53_08360 GBV54_07315 GBV60_03815 GBW03_05075 GBW44_01505 GBW52_23040 GBW76_04840 GBX12_03395 GBX20_03490 GBX46_04595 GBX55_05300 GBX64_06335 GBY13_09745 GBY23_03830 GBY73_10270 GBZ51_12095 GBZ55_06105 GCZ80_05780 GEZ01_12305 GJE27_23785 GJE28_09790 GNA88_000904 GNA97_000970 GNA99_000904 GNB28_004056 GNB36_002380 GNB86_002038 GNC11_002712 GNC19_000953 GNC45_001979 GNC75_001243 GNC95_002115 GND07_000714 GT380_09345 GTH60_13735 GTH62_10815 GTH63_22565 GTH66_18970 GTH67_23365 GTH68_14080 GTH70_07920 GTH72_05435 GTH73_08455 GTH75_09290 GTH78_07295 GTH79_20650 GTH81_19855 GTH85_10175 GTH87_13350 GTH89_08935 GTH90_17910 GTH91_11235 GTH93_14555 GTH94_11265 GTH99_14850 GXC51_01500 GXC56_01500 GXG40_01500 GYI58_05740 GYI62_001805 GYI77_07850 GYJ04_14695 GYJ24_08660 GYJ27_23070 GYJ28_003286 GYJ30_22330 GYJ32_15480 GYJ53_13635 GYJ59_07255 GYJ60_13615 H8S97_22220 KP44_01505 NG06_15025 R035_14735 Z700_13005 ZV33_21500 ZX03_19885 ZY40_08180] Bifunctional NAD(P)H-hydrate repair enzyme (Nicotinamide nucleotide repair protein) [Includes: ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase); NAD(P)H-hydrate epimerase (EC 5.1.99.6)]
[ORF1ab ORF1a orf1ab] 3C-like proteinase (EC 3.4.19.12) (EC 3.4.22.69) (Growth factor-like peptide) (Leader protein) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (Papain-like proteinase) (p65 homolog)
[Pre C,C C core E PC pre-C pre-C/C PreC preC PreC/C preC/C precore-core HBVgp4] Capsid protein (Core antigen) (Core protein) (HBcAg) (p21.5)

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