LMNB1_HUMAN
ID LMNB1_HUMAN Reviewed; 586 AA.
AC P20700; B2R6J6; Q3SYN7; Q96EI6;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=Lamin-B1;
DE Flags: Precursor;
GN Name=LMNB1; Synonyms=LMN2, LMNB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2325650; DOI=10.1128/mcb.10.5.2164-2175.1990;
RA Pollard K.M., Chan E.K.L., Grant B.J., Sullivan K.F., Tan E.M., Glass C.A.;
RT "In vitro posttranslational modification of lamin B cloned from a human T-
RT cell line.";
RL Mol. Cell. Biol. 10:2164-2175(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7557986; DOI=10.1006/geno.1995.1036;
RA Lin F., Worman H.J.;
RT "Structural organization of the human gene (LMNB1) encoding nuclear lamin
RT B1.";
RL Genomics 27:230-236(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 2-10; 15-26; 43-49; 80-90; 103-109; 112-123; 125-191;
RP 198-220; 235-250; 259-271; 277-290; 300-312; 321-330; 351-387; 475-483 AND
RP 517-528, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 52-67; 80-90; 112-123; 146-156; 198-208; 210-220;
RP 300-312; 321-330; 351-378 AND 458-473, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP ISOPRENYLATION AT CYS-583.
RX PubMed=2684976; DOI=10.1016/s0021-9258(19)47079-8;
RA Farnsworth C.C., Wolda S.L., Gelb M.H., Glomset J.A.;
RT "Human lamin B contains a farnesylated cysteine residue.";
RL J. Biol. Chem. 264:20422-20429(1989).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-575, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20 AND SER-23, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [12]
RP INVOLVEMENT IN ADLD.
RX PubMed=16951681; DOI=10.1038/ng1872;
RA Padiath Q.S., Saigoh K., Schiffmann R., Asahara H., Yamada T., Koeppen A.,
RA Hogan K., Ptacek L.J., Fu Y.-H.;
RT "Lamin B1 duplications cause autosomal dominant leukodystrophy.";
RL Nat. Genet. 38:1114-1123(2006).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-23 AND THR-575, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-157; LYS-271 AND LYS-483, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT THR-3; THR-5; SER-23; SER-375 AND THR-575, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-210 AND THR-575, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5; THR-20; SER-23; THR-25;
RP SER-28; SER-200; SER-210; SER-232; SER-278; SER-302; SER-375; SER-534 AND
RP THR-575, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-23 AND THR-575, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [24]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-14, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-102; LYS-241 AND LYS-261, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-241, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [27]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-145; LYS-241 AND LYS-261, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [28]
RP INTERACTION WITH SPAG4 AND SEPT12.
RX PubMed=25775403; DOI=10.1371/journal.pone.0120722;
RA Yeh C.H., Kuo P.L., Wang Y.Y., Wu Y.Y., Chen M.F., Lin D.Y., Lai T.H.,
RA Chiang H.S., Lin Y.H.;
RT "SEPT12/SPAG4/LAMINB1 complexes are required for maintaining the integrity
RT of the nuclear envelope in postmeiotic male germ cells.";
RL PLoS ONE 10:E0120722-E0120722(2015).
RN [29]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-102; LYS-123; LYS-145; LYS-157;
RP LYS-181; LYS-241; LYS-261; LYS-271; LYS-312; LYS-330; LYS-532 AND LYS-547,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 311-388, X-RAY CRYSTALLOGRAPHY
RP (2.0 ANGSTROMS) OF 428-550, DISULFIDE BOND, AND SUBUNIT.
RX PubMed=22265972; DOI=10.1016/j.febslet.2012.01.007;
RA Ruan J., Xu C., Bian C., Lam R., Wang J.P., Kania J., Min J., Zang J.;
RT "Crystal structures of the coil 2B fragment and the globular tail domain of
RT human lamin B1.";
RL FEBS Lett. 586:314-318(2012).
RN [31]
RP VARIANT VAL-436.
RX PubMed=24686783; DOI=10.1038/nn.3688;
RA Johnson J.O., Pioro E.P., Boehringer A., Chia R., Feit H., Renton A.E.,
RA Pliner H.A., Abramzon Y., Marangi G., Winborn B.J., Gibbs J.R., Nalls M.A.,
RA Morgan S., Shoai M., Hardy J., Pittman A., Orrell R.W., Malaspina A.,
RA Sidle K.C., Fratta P., Harms M.B., Baloh R.H., Pestronk A., Weihl C.C.,
RA Rogaeva E., Zinman L., Drory V.E., Borghero G., Mora G., Calvo A.,
RA Rothstein J.D., Drepper C., Sendtner M., Singleton A.B., Taylor J.P.,
RA Cookson M.R., Restagno G., Sabatelli M., Bowser R., Chio A., Traynor B.J.;
RT "Mutations in the matrin 3 gene cause familial amyotrophic lateral
RT sclerosis.";
RL Nat. Neurosci. 17:664-666(2014).
RN [32]
RP VARIANT ADLD TRP-29.
RX PubMed=28716252; DOI=10.1016/j.jns.2017.06.027;
RA Pedroso J.L., Munford V., Bastos A.U., Castro L.P., Marussi V.H.R.,
RA Silva G.S., Arita J.H., Menck C.F.M., Barsottini O.G.;
RT "LMNB1 mutation causes cerebellar involvement and a genome instability
RT defect.";
RL J. Neurol. Sci. 379:249-252(2017).
RN [33]
RP INVOLVEMENT IN MCPH26, VARIANTS MCPH26 GLU-33; TRP-42 AND GLY-152, VARIANT
RP THR-33, CHARACTERIZATION OF VARIANTS MCPH26 GLU-33; TRP-42 AND GLY-152,
RP CHARACTERIZATION OF VARIANT ADLD TRP-29, CHARACTERIZATION OF VARIANT
RP THR-33, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=32910914; DOI=10.1016/j.ajhg.2020.08.015;
RA Cristofoli F., Moss T., Moore H.W., Devriendt K., Flanagan-Steet H.,
RA May M., Jones J., Roelens F., Fons C., Fernandez A., Martorell L.,
RA Selicorni A., Maitz S., Vitiello G., Van der Hoeven G., Skinner S.A.,
RA Bollen M., Vermeesch J.R., Steet R., Van Esch H.;
RT "De Novo Variants in LMNB1 Cause Pronounced Syndromic Microcephaly and
RT Disruption of Nuclear Envelope Integrity.";
RL Am. J. Hum. Genet. 107:753-762(2020).
RN [34]
RP INVOLVEMENT IN MCPH26, VARIANTS MCPH26 LYS-33 DEL AND PRO-90, AND
RP CHARACTERIZATION OF VARIANTS MCPH26 GLU-33; LYS-33 DEL AND PRO-90.
RX PubMed=33033404; DOI=10.1038/s41436-020-00980-3;
RG Genomics England Research Consortium;
RA Parry D.A., Martin C.A., Greene P., Marsh J.A., Blyth M., Cox H.,
RA Donnelly D., Greenhalgh L., Greville-Heygate S., Harrison V., Lachlan K.,
RA McKenna C., Quigley A.J., Rea G., Robertson L., Suri M., Jackson A.P.;
RT "Heterozygous lamin B1 and lamin B2 variants cause primary microcephaly and
RT define a novel laminopathy.";
RL Genet. Med. 23:408-414(2021).
CC -!- FUNCTION: Lamins are components of the nuclear lamina, a fibrous layer
CC on the nucleoplasmic side of the inner nuclear membrane, which is
CC thought to provide a framework for the nuclear envelope and may also
CC interact with chromatin. {ECO:0000269|PubMed:28716252,
CC ECO:0000269|PubMed:32910914}.
CC -!- SUBUNIT: Homodimer. Interacts with lamin-associated polypeptides IA, IB
CC and 2. Interacts with SPAG4 and SEPT12. {ECO:0000269|PubMed:22265972,
CC ECO:0000269|PubMed:25775403}.
CC -!- INTERACTION:
CC P20700; A6NC98: CCDC88B; NbExp=3; IntAct=EBI-968218, EBI-347573;
CC P20700; Q9H3R5: CENPH; NbExp=3; IntAct=EBI-968218, EBI-1003700;
CC P20700; Q9NPF5: DMAP1; NbExp=3; IntAct=EBI-968218, EBI-399105;
CC P20700; Q9Y6X4: FAM169A; NbExp=3; IntAct=EBI-968218, EBI-1220497;
CC P20700; P52294: KPNA1; NbExp=4; IntAct=EBI-968218, EBI-358383;
CC P20700; O60684: KPNA6; NbExp=3; IntAct=EBI-968218, EBI-359923;
CC P20700; P02545: LMNA; NbExp=10; IntAct=EBI-968218, EBI-351935;
CC P20700; P02545-1: LMNA; NbExp=5; IntAct=EBI-968218, EBI-351949;
CC P20700; P02545-2: LMNA; NbExp=19; IntAct=EBI-968218, EBI-351953;
CC P20700; Q03252: LMNB2; NbExp=5; IntAct=EBI-968218, EBI-2830427;
CC P20700; Q8TC57: M1AP; NbExp=3; IntAct=EBI-968218, EBI-748182;
CC P20700; Q9GZQ8: MAP1LC3B; NbExp=14; IntAct=EBI-968218, EBI-373144;
CC P20700; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-968218, EBI-10232538;
CC P20700; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-968218, EBI-1105153;
CC P20700; O95295: SNAPIN; NbExp=3; IntAct=EBI-968218, EBI-296723;
CC P20700; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-968218, EBI-11952721;
CC P20700; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-968218, EBI-10180829;
CC P20700; Q05322: VP24; Xeno; NbExp=6; IntAct=EBI-968218, EBI-6153153;
CC -!- SUBCELLULAR LOCATION: Nucleus lamina {ECO:0000269|PubMed:28716252,
CC ECO:0000269|PubMed:32910914}.
CC -!- PTM: B-type lamins undergo a series of modifications, such as
CC farnesylation and phosphorylation. Increased phosphorylation of the
CC lamins occurs before envelope disintegration and probably plays a role
CC in regulating lamin associations.
CC -!- DISEASE: Leukodystrophy, demyelinating, autosomal dominant, adult-onset
CC (ADLD) [MIM:169500]: A slowly progressive and fatal demyelinating
CC leukodystrophy, presenting in the fourth or fifth decade of life.
CC Clinically characterized by early autonomic abnormalities, pyramidal
CC and cerebellar dysfunction, and symmetric demyelination of the CNS. It
CC differs from multiple sclerosis and other demyelinating disorders in
CC that neuropathology shows preservation of oligodendroglia in the
CC presence of subtotal demyelination and lack of astrogliosis.
CC {ECO:0000269|PubMed:16951681, ECO:0000269|PubMed:28716252,
CC ECO:0000269|PubMed:32910914}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Microcephaly 26, primary, autosomal dominant (MCPH26)
CC [MIM:619179]: A form of microcephaly, a disease defined as a head
CC circumference more than 3 standard deviations below the age, sex and
CC ethnically matched mean. Brain weight is markedly reduced and the
CC cerebral cortex is disproportionately small. MCPH26 is an autosomal
CC dominant, progressive form apparent at birth or in early infancy. It is
CC associated with relative short stature, variable severity of
CC intellectual disability, and neurological features as the core
CC symptoms. Brain imaging shows a simplified gyral pattern of the cortex
CC and abnormal corpus callosum in some patients.
CC {ECO:0000269|PubMed:32910914, ECO:0000269|PubMed:33033404}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: The structural integrity of the lamina is strictly
CC controlled by the cell cycle, as seen by the disintegration and
CC formation of the nuclear envelope in prophase and telophase,
CC respectively.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M34458; AAA36162.1; -; mRNA.
DR EMBL; L37747; AAC37575.1; -; Genomic_DNA.
DR EMBL; L37737; AAC37575.1; JOINED; Genomic_DNA.
DR EMBL; L37738; AAC37575.1; JOINED; Genomic_DNA.
DR EMBL; L37739; AAC37575.1; JOINED; Genomic_DNA.
DR EMBL; L37740; AAC37575.1; JOINED; Genomic_DNA.
DR EMBL; L37741; AAC37575.1; JOINED; Genomic_DNA.
DR EMBL; L37742; AAC37575.1; JOINED; Genomic_DNA.
DR EMBL; L37743; AAC37575.1; JOINED; Genomic_DNA.
DR EMBL; L37744; AAC37575.1; JOINED; Genomic_DNA.
DR EMBL; L37745; AAC37575.1; JOINED; Genomic_DNA.
DR EMBL; L37746; AAC37575.1; JOINED; Genomic_DNA.
DR EMBL; AK312603; BAG35493.1; -; mRNA.
DR EMBL; CH471086; EAW48846.1; -; Genomic_DNA.
DR EMBL; BC012295; AAH12295.1; -; mRNA.
DR EMBL; BC103723; AAI03724.1; -; mRNA.
DR CCDS; CCDS4140.1; -.
DR PIR; A34707; VEHULB.
DR RefSeq; NP_005564.1; NM_005573.3.
DR PDB; 2KPW; NMR; -; A=439-549.
DR PDB; 3JT0; X-ray; 2.39 A; A/B=426-558.
DR PDB; 3TYY; X-ray; 2.40 A; A/B=311-388.
DR PDB; 3UMN; X-ray; 2.00 A; A/B/C=428-550.
DR PDB; 5VVX; X-ray; 2.90 A; B/D=389-401.
DR PDB; 7DTG; X-ray; 3.60 A; A/B/C/D/E/F=407-553.
DR PDBsum; 2KPW; -.
DR PDBsum; 3JT0; -.
DR PDBsum; 3TYY; -.
DR PDBsum; 3UMN; -.
DR PDBsum; 5VVX; -.
DR PDBsum; 7DTG; -.
DR AlphaFoldDB; P20700; -.
DR SMR; P20700; -.
DR BioGRID; 110187; 404.
DR CORUM; P20700; -.
DR DIP; DIP-34897N; -.
DR IntAct; P20700; 84.
DR MINT; P20700; -.
DR STRING; 9606.ENSP00000261366; -.
DR GlyGen; P20700; 2 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; P20700; -.
DR MetOSite; P20700; -.
DR PhosphoSitePlus; P20700; -.
DR SwissPalm; P20700; -.
DR BioMuta; LMNB1; -.
DR DMDM; 125953; -.
DR SWISS-2DPAGE; P20700; -.
DR EPD; P20700; -.
DR jPOST; P20700; -.
DR MassIVE; P20700; -.
DR MaxQB; P20700; -.
DR PaxDb; P20700; -.
DR PeptideAtlas; P20700; -.
DR PRIDE; P20700; -.
DR ProteomicsDB; 53773; -.
DR ABCD; P20700; 3 sequenced antibodies.
DR Antibodypedia; 3937; 820 antibodies from 48 providers.
DR CPTC; P20700; 2 antibodies.
DR DNASU; 4001; -.
DR Ensembl; ENST00000261366.10; ENSP00000261366.5; ENSG00000113368.12.
DR GeneID; 4001; -.
DR KEGG; hsa:4001; -.
DR MANE-Select; ENST00000261366.10; ENSP00000261366.5; NM_005573.4; NP_005564.1.
DR UCSC; uc003kud.3; human.
DR CTD; 4001; -.
DR DisGeNET; 4001; -.
DR GeneCards; LMNB1; -.
DR GeneReviews; LMNB1; -.
DR HGNC; HGNC:6637; LMNB1.
DR HPA; ENSG00000113368; Tissue enhanced (bone marrow, lymphoid tissue).
DR MalaCards; LMNB1; -.
DR MIM; 150340; gene.
DR MIM; 169500; phenotype.
DR MIM; 619179; phenotype.
DR neXtProt; NX_P20700; -.
DR OpenTargets; ENSG00000113368; -.
DR Orphanet; 99027; Adult-onset autosomal dominant leukodystrophy.
DR Orphanet; 2514; Autosomal dominant primary microcephaly.
DR PharmGKB; PA30403; -.
DR VEuPathDB; HostDB:ENSG00000113368; -.
DR eggNOG; KOG0977; Eukaryota.
DR GeneTree; ENSGT00940000157199; -.
DR HOGENOM; CLU_012560_9_2_1; -.
DR InParanoid; P20700; -.
DR OMA; IGQWAIK; -.
DR OrthoDB; 701388at2759; -.
DR PhylomeDB; P20700; -.
DR TreeFam; TF101181; -.
DR PathwayCommons; P20700; -.
DR Reactome; R-HSA-1221632; Meiotic synapsis.
DR Reactome; R-HSA-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR Reactome; R-HSA-2980766; Nuclear Envelope Breakdown.
DR Reactome; R-HSA-2995383; Initiation of Nuclear Envelope (NE) Reformation.
DR Reactome; R-HSA-352238; Breakdown of the nuclear lamina.
DR Reactome; R-HSA-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-HSA-8862803; Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models.
DR Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
DR Reactome; R-HSA-9013405; RHOD GTPase cycle.
DR Reactome; R-HSA-9035034; RHOF GTPase cycle.
DR SignaLink; P20700; -.
DR SIGNOR; P20700; -.
DR BioGRID-ORCS; 4001; 71 hits in 1087 CRISPR screens.
DR ChiTaRS; LMNB1; human.
DR EvolutionaryTrace; P20700; -.
DR GeneWiki; LMNB1; -.
DR GenomeRNAi; 4001; -.
DR Pharos; P20700; Tbio.
DR PRO; PR:P20700; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P20700; protein.
DR Bgee; ENSG00000113368; Expressed in ventricular zone and 143 other tissues.
DR ExpressionAtlas; P20700; baseline and differential.
DR Genevisible; P20700; HS.
DR GO; GO:0005638; C:lamin filament; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; TAS:Reactome.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:Ensembl.
DR GO; GO:0005652; C:nuclear lamina; IMP:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:CAFA.
DR GO; GO:0043274; F:phospholipase binding; IEA:Ensembl.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IEA:Ensembl.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; TAS:ProtInc.
DR GO; GO:0031507; P:heterochromatin assembly; IBA:GO_Central.
DR GO; GO:0006998; P:nuclear envelope organization; IMP:UniProtKB.
DR GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR GO; GO:0051664; P:nuclear pore localization; IBA:GO_Central.
DR GO; GO:0090435; P:protein localization to nuclear envelope; IBA:GO_Central.
DR Gene3D; 2.60.40.1260; -; 1.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR001322; Lamin_tail_dom.
DR InterPro; IPR036415; Lamin_tail_dom_sf.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF00932; LTD; 1.
DR SMART; SM01391; Filament; 1.
DR SUPFAM; SSF74853; SSF74853; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
DR PROSITE; PS51841; LTD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosomal rearrangement; Coiled coil;
KW Direct protein sequencing; Disease variant; Disulfide bond;
KW Intellectual disability; Intermediate filament; Isopeptide bond;
KW Leukodystrophy; Lipoprotein; Methylation; Nucleus; Phosphoprotein;
KW Prenylation; Primary microcephaly; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895"
FT CHAIN 2..583
FT /note="Lamin-B1"
FT /id="PRO_0000063816"
FT PROPEP 584..586
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000393945"
FT DOMAIN 32..388
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT DOMAIN 430..546
FT /note="LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01187"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..34
FT /note="Head"
FT REGION 35..69
FT /note="Coil 1A"
FT REGION 70..81
FT /note="Linker 1"
FT REGION 82..215
FT /note="Coil 1B"
FT REGION 216..243
FT /note="Linker 2"
FT REGION 244..386
FT /note="Coil 2"
FT REGION 387..586
FT /note="Tail"
FT REGION 388..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 415..420
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 392..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 5
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 14
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 20
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 25
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 111
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P14733"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70615"
FT MOD_RES 157
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70615"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 271
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 330
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14733"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 413
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P21619"
FT MOD_RES 483
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 575
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 583
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 583
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:2684976"
FT DISULFID 317
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:22265972"
FT CROSSLNK 102
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 123
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 145
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 157
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 181
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 241
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 261
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 271
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 312
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 330
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 532
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 547
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 29
FT /note="R -> W (in ADLD; unknown pathological significance;
FT no effect on localization to nuclear lamina;
FT dbSNP:rs1295707923)"
FT /evidence="ECO:0000269|PubMed:28716252,
FT ECO:0000269|PubMed:32910914"
FT /id="VAR_085497"
FT VARIANT 33
FT /note="K -> E (in MCPH26; decreased localization to nuclear
FT lamina; increased aggregation; changed nuclear envelope
FT organization)"
FT /evidence="ECO:0000269|PubMed:32910914,
FT ECO:0000269|PubMed:33033404"
FT /id="VAR_085498"
FT VARIANT 33
FT /note="K -> T (no effect on localization to nuclear lamina;
FT dbSNP:rs1303994586)"
FT /evidence="ECO:0000269|PubMed:32910914"
FT /id="VAR_085499"
FT VARIANT 33
FT /note="Missing (in MCPH26; increased aggregation; changed
FT nuclear envelope organization)"
FT /evidence="ECO:0000269|PubMed:33033404"
FT /id="VAR_085500"
FT VARIANT 42
FT /note="R -> W (in MCPH26; decreased localization to nuclear
FT lamina; changed nuclear envelope organization; increased
FT aggregation)"
FT /evidence="ECO:0000269|PubMed:32910914"
FT /id="VAR_085501"
FT VARIANT 90
FT /note="R -> P (in MCPH26; increased aggregation; changed
FT nuclear envelope organization)"
FT /evidence="ECO:0000269|PubMed:33033404"
FT /id="VAR_085502"
FT VARIANT 152
FT /note="A -> G (in MCPH26; decreased protein abundance;
FT changed localization to nuclear lamina; changed nuclear
FT envelope organization)"
FT /evidence="ECO:0000269|PubMed:32910914"
FT /id="VAR_085503"
FT VARIANT 436
FT /note="A -> V (found in a family with amyotrophic lateral
FT sclerosis carrying a probable causative mutation in MATR3;
FT unknown pathological significance; dbSNP:rs1380634377)"
FT /evidence="ECO:0000269|PubMed:24686783"
FT /id="VAR_071077"
FT VARIANT 501
FT /note="A -> V (in dbSNP:rs36105360)"
FT /id="VAR_031646"
FT CONFLICT 382
FT /note="E -> Q (in Ref. 5; AAH12295)"
FT /evidence="ECO:0000305"
FT HELIX 315..381
FT /evidence="ECO:0007829|PDB:3TYY"
FT STRAND 432..447
FT /evidence="ECO:0007829|PDB:3UMN"
FT STRAND 451..458
FT /evidence="ECO:0007829|PDB:3UMN"
FT STRAND 460..462
FT /evidence="ECO:0007829|PDB:3UMN"
FT STRAND 470..475
FT /evidence="ECO:0007829|PDB:3UMN"
FT STRAND 478..483
FT /evidence="ECO:0007829|PDB:3UMN"
FT STRAND 495..500
FT /evidence="ECO:0007829|PDB:3UMN"
FT TURN 509..511
FT /evidence="ECO:0007829|PDB:3UMN"
FT STRAND 512..515
FT /evidence="ECO:0007829|PDB:3UMN"
FT STRAND 523..525
FT /evidence="ECO:0007829|PDB:3UMN"
FT STRAND 527..532
FT /evidence="ECO:0007829|PDB:3UMN"
FT STRAND 538..546
FT /evidence="ECO:0007829|PDB:3UMN"
SQ SEQUENCE 586 AA; 66408 MW; 73292877745722C4 CRC64;
MATATPVPPR MGSRAGGPTT PLSPTRLSRL QEKEELRELN DRLAVYIDKV RSLETENSAL
QLQVTEREEV RGRELTGLKA LYETELADAR RALDDTARER AKLQIELGKC KAEHDQLLLN
YAKKESDLNG AQIKLREYEA ALNSKDAALA TALGDKKSLE GDLEDLKDQI AQLEASLAAA
KKQLADETLL KVDLENRCQS LTEDLEFRKS MYEEEINETR RKHETRLVEV DSGRQIEYEY
KLAQALHEMR EQHDAQVRLY KEELEQTYHA KLENARLSSE MNTSTVNSAR EELMESRMRI
ESLSSQLSNL QKESRACLER IQELEDLLAK EKDNSRRMLT DKEREMAEIR DQMQQQLNDY
EQLLDVKLAL DMEISAYRKL LEGEEERLKL SPSPSSRVTV SRASSSRSVR TTRGKRKRVD
VEESEASSSV SISHSASATG NVCIEEIDVD GKFIRLKNTS EQDQPMGGWE MIRKIGDTSV
SYKYTSRYVL KAGQTVTIWA ANAGVTASPP TDLIWKNQNS WGTGEDVKVI LKNSQGEEVA
QRSTVFKTTI PEEEEEEEEA AGVVVEEELF HQQGTPRASN RSCAIM
