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 04-NOV-2026, entry version 241. 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, AND METHYLATION 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 ADLDTY. 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 FUNCTION, AND INTERACTION WITH SUN5. RX PubMed=38870534; DOI=10.1093/molehr/gaae022; RA Zhang Y., Liu G., Huang L., He X., Su Y., Nie X., Mao Z., Xing X.; RT "SUN5 interacts with nuclear membrane LaminB1 and cytoskeletal GTPase RT Septin12 mediating the sperm head-and-tail junction."; RL Mol. Hum. Reprod. 30:0-0(2024). RN [31] {ECO:0007744|PDB:3TYY, ECO:0007744|PDB:3UMN} RP X-RAY CRYSTALLOGRAPHY, 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 [32] {ECO:0007744|PDB:5BNW} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH OGT, AND GLYCOSYLATION AT THR-399. RX PubMed=26237509; DOI=10.1038/nsmb.3063; RA Pathak S., Alonso J., Schimpl M., Rafie K., Blair D.E., Borodkin V.S., RA Albarbarawi O., van Aalten D.M.F.; RT "The active site of O-GlcNAc transferase imposes constraints on substrate RT sequence."; RL Nat. Struct. Mol. Biol. 22:744-750(2015). RN [33] {ECO:0007744|PDB:5VVX} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH OGA, GLYCOSYLATION AT THR-399, AND RP DEGLYCOSYLATION AT THR-399. RX PubMed=28939839; DOI=10.1038/s41467-017-00865-1; RA Li B., Li H., Hu C.W., Jiang J.; RT "Structural insights into the substrate binding adaptability and RT specificity of human O-GlcNAcase."; RL Nat. Commun. 8:666-666(2017). RN [34] {ECO:0007744|PDB:7DTG} RP X-RAY CRYSTALLOGRAPHY, AND SUBUNIT. RX PubMed=33706103; DOI=10.1016/j.bbrc.2021.02.102; RA Ahn J., Lee J., Jeong S., Kang S.M., Park B.J., Ha N.C.; RT "Beta-strand-mediated dimeric formation of the Ig-like domains of human RT lamin A/C and B1."; RL Biochem. Biophys. Res. Commun. 550:191-196(2021). RN [35] 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 [36] RP VARIANT ADLDTY 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 [37] 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 ADLDTY 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 [38] 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). RN [39] RP INVOLVEMENT IN ADLDAT AND ADLDTY. RX PubMed=39078102; DOI=10.1002/ana.27038; RA Dimartino P., Zadorozhna M., Yumiceba V., Basile A., Cani I., Melo U.S., RA Henck J., Breur M., Tonon C., Lodi R., Brusco A., Pippucci T., Koufi F.D., RA Boschetti E., Ramazzotti G., Manzoli L., Ratti S., Pinto E Vairo F., RA Delatycki M.B., Vaula G., Cortelli P., Bugiani M., Spielmann M., RA Giorgio E.; RT "Structural Variants at the LMNB1 Locus: Deciphering Pathomechanisms in RT Autosomal Dominant Adult-Onset Demyelinating Leukodystrophy."; RL Ann. Neurol. 96:855-870(2024). CC -!- FUNCTION: Lamins are intermediate filament proteins that assemble into CC a filamentous meshwork, and which constitute the major components of CC the nuclear lamina, a fibrous layer on the nucleoplasmic side of the CC inner nuclear membrane (PubMed:28716252, PubMed:32910914). Lamins CC provide a framework for the nuclear envelope, bridging the nuclear CC envelope and chromatin, thereby playing an important role in nuclear CC assembly, chromatin organization, nuclear membrane and telomere CC dynamics (PubMed:28716252, PubMed:32910914). The structural integrity CC of the lamina is strictly controlled by the cell cycle, as seen by the CC disintegration and formation of the nuclear envelope in prophase and CC telophase, respectively (PubMed:28716252, PubMed:32910914). Plays a CC role in sperm morphological development during late stages of CC spermiogenesis, particularly the anchoring of the sperm head to the CC tail (PubMed:38870534). Component of the LMNB1/SUN5/SEPT12 bridge that CC connects the sperm proximal centriole to the implantation fossa, the CC bridge functions to prevent detachment of the proximal centriole from CC the posterior nucleus during spermiogenesis (PubMed:38870534). CC {ECO:0000269|PubMed:28716252, ECO:0000269|PubMed:32910914, CC ECO:0000269|PubMed:38870534}. CC -!- SUBUNIT: Homodimer (PubMed:22265972, PubMed:33706103). Lamin dimers CC then assemble into dimeric head-to-tail polymers. Ultimately, two head- CC to-tail polymers assemble laterally into a protofilament with a CC uniformly shaped rod of 3.5 nm in diameter (By similarity). Interacts CC with SPAG4 and SEPT12 (PubMed:25775403). Interacts with FAM170A (By CC similarity). Interacts with SUN5; the interaction acts as a bridge CC between LMNB1 and the Septin complex; which functions to maintain the CC sperm head-to-tail junction during late stages of spermiogenesis CC (PubMed:38870534). {ECO:0000250|UniProtKB:P14733, CC ECO:0000269|PubMed:22265972, ECO:0000269|PubMed:25775403, CC ECO:0000269|PubMed:33706103, ECO:0000269|PubMed:38870534}. 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=5; IntAct=EBI-968218, EBI-358383; CC P20700; O15131: KPNA5; NbExp=3; IntAct=EBI-968218, EBI-540602; CC P20700; O60684: KPNA6; NbExp=4; IntAct=EBI-968218, EBI-359923; CC P20700; P02545: LMNA; NbExp=23; 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=8; 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}. Note=Expressed in the posterior part of CC the nucleus during mid-steps of spermiogenesis, expression becomes more CC localized to the implantation fossa in later stages (By similarity). CC Expressed at the neck region in mature sperm (By similarity). CC {ECO:0000250|UniProtKB:P14733}. 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. {ECO:0000269|PubMed:2684976}. CC -!- PTM: Phosphorylation plays a key role in lamin organization, CC subcellular localization and nuclear envelope disintegration. CC Phosphorylation by CDK1 at Ser-23 and Ser-393 at the onset of mitosis CC drives lamin disassembly and nuclear envelope breakdown. CC {ECO:0000250|UniProtKB:P02545}. CC -!- DISEASE: Leukodystrophy, demyelinating, adult-onset, autosomal CC dominant, typical (ADLDTY) [MIM:169500]: A slowly progressive and fatal CC demyelinating leukodystrophy, presenting in the fourth or fifth decade CC of life. Clinically characterized by early autonomic abnormalities, CC pyramidal and cerebellar dysfunction, and symmetric demyelination of CC the CNS. It differs from multiple sclerosis and other demyelinating CC disorders in that neuropathology shows preservation of oligodendroglia CC in the 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. The disease is caused by CC heterozygous tandem genomic duplications that result in an extra copy CC of the LMNB1 gene and also affect regulatory elements of other genes. CC {ECO:0000269|PubMed:16951681, ECO:0000269|PubMed:39078102}. CC -!- DISEASE: Leukodystrophy, demyelinating, adult-onset, autosomal CC dominant, atypical (ADLDAT) [MIM:621061]: An autosomal dominant, slowly CC progressive disorder characterized by pyramidal signs with muscle CC weakness, spasticity, dysarthria, dysautonomia, and demyelinating CC leukodystrophy affecting the cerebrum and cortico-spinal tracts while CC sparing the cerebellum. Patients usually do not present with autonomic CC symptoms. {ECO:0000269|PubMed:39078102}. Note=The disease is caused by CC variants affecting the gene represented in this entry. The disease is CC caused by abnormal LMNB1 expression due to heterozygous deletions CC involving regulatory elements upstream of LMNB1. It can also be caused CC by inverted duplications involving LMNB1, as reported in one patient. CC {ECO:0000269|PubMed:39078102}. 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 -!- 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_005573.4. 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; 5BNW; X-ray; 2.40 A; D=389-401. 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 AlphaFoldDB; P20700; -. DR SMR; P20700; -. DR BioGRID; 110187; 646. DR CORUM; P20700; -. DR DIP; DIP-34897N; -. DR FunCoup; P20700; 2728. DR IntAct; P20700; 235. DR NDEx; IQUERY-CP-LMNB1; 5 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000261366; -. DR BindingDB; P20700; -. DR ChEMBL; CHEMBL5725026; -. DR GlyCosmos; P20700; 5 sites, 3 glycans. DR GlyGen; P20700; 5 sites, 1 N-linked glycan (1 site), 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 CPTAC; CPTAC-5900; -. DR CPTAC; CPTAC-5901; -. DR CPTAC; CPTAC-5902; -. DR jPOST; P20700; -. DR MassIVE; P20700; -. DR PaxDb; 9606-ENSP00000261366; -. DR PeptideAtlas; P20700; -. DR ProteomicsDB; 53773; -. DR Pumba; P20700; -. DR ABCD; P20700; 3 sequenced antibodies. DR Antibodypedia; 3937; 938 antibodies from 52 providers. DR CPTC; P20700; 2 antibodies. DR DNASU; 4001; -. DR Ensembl; ENST00000261366.10; ENSP00000261366.5; ENSG00000113368.13. 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 AGR; HGNC:6637; -. DR ClinPGx; PA30403; -. 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 MIM; 621061; phenotype. DR OpenTargets; ENSG00000113368; -. DR Orphanet; 99027; Adult-onset autosomal dominant leukodystrophy. DR Orphanet; 2514; Autosomal dominant primary microcephaly. DR VEuPathDB; HostDB:ENSG00000113368; -. DR eggNOG; KOG0977; Eukaryota. DR GeneTree; ENSGT00940000157199; -. DR HOGENOM; CLU_012560_9_2_1; -. DR InParanoid; P20700; -. DR OMA; AAANRNC; -. DR OrthoDB; 102442at2759; -. DR PAN-GO; P20700; 7 GO annotations based on evolutionary models. DR PhylomeDB; P20700; -. 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; Depolymerization 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 Agora; ENSG00000113368; -. DR BioGRID-ORCS; 4001; 91 hits in 1166 CRISPR screens. DR CD-CODE; 232F8A39; P-body. DR CD-CODE; 91857CE7; Nucleolus. DR CD-CODE; DEE660B4; Stress granule. 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 145 other cell types or tissues. DR ExpressionAtlas; P20700; baseline and differential. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005635; C:nuclear envelope; TAS:Reactome. DR GO; GO:0005652; C:nuclear lamina; IMP:UniProtKB. 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:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central. DR GO; GO:0160123; F:structural constituent of nuclear lamina; TAS:UniProtKB. DR GO; GO:0031507; P:heterochromatin formation; 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 FunFam; 1.20.5.170:FF:000033; Lamin A/C; 1. DR FunFam; 1.20.5.1160:FF:000007; Lamin B1; 1. DR FunFam; 2.60.40.1260:FF:000002; Lamin B1; 1. DR Gene3D; 1.20.5.170; -; 1. DR Gene3D; 2.60.40.1260; Lamin Tail domain; 1. DR Gene3D; 1.20.5.500; Single helix bin; 1. DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 2. 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 PANTHER; PTHR45721; LAMIN DM0-RELATED; 1. DR PANTHER; PTHR45721:SF3; LAMIN-B1; 1. DR Pfam; PF00038; Filament; 1. DR Pfam; PF00932; LTD; 1. DR SMART; SM01391; Filament; 1. DR SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2. DR SUPFAM; SSF74853; Lamin A/C globular tail domain; 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; Glycoprotein; KW Intellectual disability; Intermediate filament; Isopeptide bond; KW Leukodystrophy; Lipoprotein; Methylation; Nucleus; Phosphoprotein; KW Prenylation; Primary microcephaly; Proteomics identification; KW 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 390..409 FT /note="Low complexity" 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 393 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P02545" 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|PubMed:2684976" FT LIPID 583 FT /note="S-farnesyl cysteine" FT /evidence="ECO:0000269|PubMed:2684976" FT CARBOHYD 399 FT /note="O-linked (GlcNAc) threonine" FT /evidence="ECO:0000269|PubMed:26237509, FT ECO:0000269|PubMed:28939839" 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 ADLDTY; uncertain significance; no effect FT on localization to nuclear lamina; 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; dbSNP:rs1750497172)" 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; dbSNP:rs1245844735)" 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; dbSNP:rs1750506249)" 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; dbSNP:rs935132421)" 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 uncertain 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 //