ID   LMNB2_HUMAN             Reviewed;         620 AA.
AC   Q03252; O75292; Q14734; Q96DF6;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   11-NOV-2015, sequence version 4.
DT   05-FEB-2025, entry version 228.
DE   RecName: Full=Lamin-B2;
DE   Flags: Precursor;
GN   Name=LMNB2; Synonyms=LMN2;
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 [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Muscle;
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   [4]
RP   PROTEIN SEQUENCE OF 94-104; 131-150; 152-161; 192-202; 236-244; 294-306;
RP   345-372; 486-496 AND 530-555, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Fetal brain cortex;
RA   Lubec G., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 105-620, AND NUCLEOTIDE SEQUENCE [GENOMIC
RP   DNA] OF 531-620.
RX   PubMed=1630457; DOI=10.1128/mcb.12.8.3499-3506.1992;
RA   Biamonti G., Giacca M., Perini G., Contreas G., Zentilin L., Weighardt F.,
RA   Guerra M., Valle G.D., Saccone S., Riva S., Falaschi A.;
RT   "The gene for a novel human lamin maps at a highly transcribed locus of
RT   chromosome 19 which replicates at the onset of S-phase.";
RL   Mol. Cell. Biol. 12:3499-3506(1992).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34, 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   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=T-cell;
RX   PubMed=19367720; DOI=10.1021/pr800500r;
RA   Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT   "Phosphorylation analysis of primary human T lymphocytes using sequential
RT   IMAC and titanium oxide enrichment.";
RL   J. Proteome Res. 7:5167-5176(2008).
RN   [9]
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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34; SER-37; SER-422; SER-424
RP   AND SER-426, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34, 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   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81, AND IDENTIFICATION BY MASS
RP   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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34, AND IDENTIFICATION BY
RP   MASS 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   [15]
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   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420; SER-422; SER-424 AND
RP   SER-426, AND 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   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-23; THR-34; SER-37; SER-316
RP   AND SER-497, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34, AND IDENTIFICATION BY
RP   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   [19]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-77; LYS-81 AND LYS-195, 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   [20]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [21]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-77; LYS-81; LYS-195; LYS-255 AND
RP   LYS-489, 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   [22]
RP   GLYCOSYLATION AT THR-413.
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   [23]
RP   INVOLVEMENT IN MCPH27, VARIANTS MCPH27 HIS-54 AND LYS-398, CHARACTERIZATION
RP   OF VARIANTS MCPH27 HIS-54 AND LYS-398, FUNCTION, AND SUBCELLULAR LOCATION.
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   [24]
RP   VARIANT APLD THR-427, AND VARIANT GLN-235.
RX   PubMed=16826530; DOI=10.1086/505885;
RA   Hegele R.A., Cao H., Liu D.M., Costain G.A., Charlton-Menys V.,
RA   Rodger N.W., Durrington P.N.;
RT   "Sequencing of the reannotated LMNB2 gene reveals novel mutations in
RT   patients with acquired partial lipodystrophy.";
RL   Am. J. Hum. Genet. 79:383-389(2006).
RN   [25]
RP   VARIANT [LARGE SCALE ANALYSIS] TRP-236.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [26]
RP   VARIANT APLD HIS-252.
RX   PubMed=22768673; DOI=10.1515/jpem-2012-0007;
RA   Gao J., Li Y., Fu X., Luo X.;
RT   "A Chinese patient with acquired partial lipodystrophy caused by a novel
RT   mutation with LMNB2 gene.";
RL   J. Pediatr. Endocrinol. Metab. 25:375-377(2012).
RN   [27]
RP   VARIANT EPM9 TYR-157, AND CHARACTERIZATION OF VARIANT EPM9 TYR-157.
RX   PubMed=25954030; DOI=10.1093/hmg/ddv171;
RA   Damiano J.A., Afawi Z., Bahlo M., Mauermann M., Misk A., Arsov T.,
RA   Oliver K.L., Dahl H.H., Shearer A.E., Smith R.J., Hall N.E., Mahmood K.,
RA   Leventer R.J., Scheffer I.E., Muona M., Lehesjoki A.E., Korczyn A.D.,
RA   Herrmann H., Berkovic S.F., Hildebrand M.S.;
RT   "Mutation of the nuclear lamin gene LMNB2 in progressive myoclonus epilepsy
RT   with early ataxia.";
RL   Hum. Mol. Genet. 24:4483-4490(2015).
RN   [28]
RP   VARIANT GLN-235.
RX   PubMed=27535533; DOI=10.1038/nature19057;
RG   Exome Aggregation Consortium;
RA   Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E., Fennell T.,
RA   O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B., Tukiainen T.,
RA   Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K., Zhao F., Zou J.,
RA   Pierce-Hoffman E., Berghout J., Cooper D.N., Deflaux N., DePristo M.,
RA   Do R., Flannick J., Fromer M., Gauthier L., Goldstein J., Gupta N.,
RA   Howrigan D., Kiezun A., Kurki M.I., Moonshine A.L., Natarajan P.,
RA   Orozco L., Peloso G.M., Poplin R., Rivas M.A., Ruano-Rubio V., Rose S.A.,
RA   Ruderfer D.M., Shakir K., Stenson P.D., Stevens C., Thomas B.P., Tiao G.,
RA   Tusie-Luna M.T., Weisburd B., Won H.H., Yu D., Altshuler D.M.,
RA   Ardissino D., Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
RA   Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S., Laakso M.,
RA   McCarroll S., McCarthy M.I., McGovern D., McPherson R., Neale B.M.,
RA   Palotie A., Purcell S.M., Saleheen D., Scharf J.M., Sklar P.,
RA   Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C., Wilson J.G.,
RA   Daly M.J., MacArthur D.G.;
RT   "Analysis of protein-coding genetic variation in 60,706 humans.";
RL   Nature 536:285-291(2016).
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:33033404). Lamins provide a framework
CC       for the nuclear envelope, bridging the nuclear envelope and chromatin,
CC       thereby playing an important role in nuclear assembly, chromatin
CC       organization, nuclear membrane and telomere dynamics (PubMed:33033404).
CC       The structural integrity of the lamina is strictly controlled by the
CC       cell cycle, as seen by the disintegration and formation of the nuclear
CC       envelope in prophase and telophase, respectively (PubMed:33033404).
CC       {ECO:0000269|PubMed:33033404}.
CC   -!- SUBUNIT: Dimer (By similarity). Lamin dimers then assemble into dimeric
CC       head-to-tail polymers (By similarity). Ultimately, two head-to-tail
CC       polymers assemble laterally into a protofilament with a uniformly
CC       shaped rod of 3.5 nm in diameter (By similarity). Interacts with TMEM43
CC       (By similarity). {ECO:0000250|UniProtKB:P21619}.
CC   -!- INTERACTION:
CC       Q03252; A2BDD9: AMOT; NbExp=3; IntAct=EBI-2830427, EBI-17286414;
CC       Q03252; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-2830427, EBI-746752;
CC       Q03252; P35219: CA8; NbExp=3; IntAct=EBI-2830427, EBI-718700;
CC       Q03252; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-2830427, EBI-744556;
CC       Q03252; A6NC98: CCDC88B; NbExp=3; IntAct=EBI-2830427, EBI-347573;
CC       Q03252; Q16543: CDC37; NbExp=3; IntAct=EBI-2830427, EBI-295634;
CC       Q03252; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-2830427, EBI-2349927;
CC       Q03252; P07954: FH; NbExp=3; IntAct=EBI-2830427, EBI-1050358;
CC       Q03252; Q08379: GOLGA2; NbExp=3; IntAct=EBI-2830427, EBI-618309;
CC       Q03252; P02545: LMNA; NbExp=10; IntAct=EBI-2830427, EBI-351935;
CC       Q03252; P20700: LMNB1; NbExp=8; IntAct=EBI-2830427, EBI-968218;
CC       Q03252; Q03252: LMNB2; NbExp=3; IntAct=EBI-2830427, EBI-2830427;
CC       Q03252; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-2830427, EBI-1216080;
CC       Q03252; P55081: MFAP1; NbExp=3; IntAct=EBI-2830427, EBI-1048159;
CC       Q03252; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-2830427, EBI-10172526;
CC       Q03252; O14753: OVOL1; NbExp=3; IntAct=EBI-2830427, EBI-3917713;
CC       Q03252; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-2830427, EBI-14066006;
CC       Q03252; P78424: POU6F2; NbExp=3; IntAct=EBI-2830427, EBI-12029004;
CC       Q03252; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-2830427, EBI-1105153;
CC       Q03252; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-2830427, EBI-1105213;
CC       Q03252; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-2830427, EBI-741515;
CC       Q03252; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-2830427, EBI-11952721;
CC       Q03252; P14373: TRIM27; NbExp=3; IntAct=EBI-2830427, EBI-719493;
CC       Q03252; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-2830427, EBI-10241197;
CC       Q03252; O75604: USP2; NbExp=3; IntAct=EBI-2830427, EBI-743272;
CC       Q03252; Q9Y3C0: WASHC3; NbExp=3; IntAct=EBI-2830427, EBI-712969;
CC       Q03252; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-2830427, EBI-14104088;
CC       Q03252; Q15911-2: ZFHX3; NbExp=3; IntAct=EBI-2830427, EBI-10237226;
CC   -!- SUBCELLULAR LOCATION: Nucleus lamina {ECO:0000305|PubMed:33033404}.
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:0000250|UniProtKB:P20700}.
CC   -!- PTM: Phosphorylation plays a key role in lamin organization,
CC       subcellular localization and nuclear envelope disintegration.
CC       Phosphorylation by CDK1 at Ser-37 and Ser-407 at the onset of mitosis
CC       drives lamin disassembly and nuclear envelope breakdown.
CC       {ECO:0000250|UniProtKB:P02545}.
CC   -!- DISEASE: Partial acquired lipodystrophy (APLD) [MIM:608709]: A rare
CC       childhood disease characterized by loss of subcutaneous fat from the
CC       face and trunk. Fat deposition on the pelvic girdle and lower limbs is
CC       normal or excessive. Most frequently, onset between 5 and 15 years of
CC       age. Most affected subjects are females and some show no other
CC       abnormality, but many develop glomerulonephritis, diabetes mellitus,
CC       hyperlipidemia, and complement deficiency. Intellectual disability in
CC       some cases. APLD is a sporadic disorder of unknown etiology.
CC       {ECO:0000269|PubMed:16826530, ECO:0000269|PubMed:22768673}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: Epilepsy, progressive myoclonic 9 (EPM9) [MIM:616540]: A form
CC       of progressive myoclonic epilepsy, a clinically and genetically
CC       heterogeneous group of disorders defined by the combination of action
CC       and reflex myoclonus, other types of epileptic seizures, and
CC       progressive neurodegeneration and neurocognitive impairment. EPM9 is an
CC       autosomal recessive form characterized by myoclonus, tonic-clonic
CC       seizures, ataxia, and delayed psychomotor development.
CC       {ECO:0000269|PubMed:25954030}. Note=The disease may be caused by
CC       variants affecting the gene represented in this entry.
CC   -!- DISEASE: Microcephaly 27, primary, autosomal dominant (MCPH27)
CC       [MIM:619180]: 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. MCPH27 is an autosomal
CC       dominant form apparent in early childhood and associated with global
CC       developmental delay, delayed walking, inability to walk, impaired
CC       intellectual development, and poor or absent speech. Brain imaging may
CC       show enlarged ventricles or gyral abnormalities in some patients.
CC       {ECO:0000269|PubMed:33033404}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH06551.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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; BT007441; AAP36109.1; -; mRNA.
DR   EMBL; AC011522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC005624; AAC34573.1; -; Genomic_DNA.
DR   EMBL; BC006551; AAH06551.1; ALT_INIT; mRNA.
DR   EMBL; M94362; AAA80979.1; -; mRNA.
DR   EMBL; M94363; AAB00873.1; ALT_SEQ; Genomic_DNA.
DR   CCDS; CCDS12090.2; -.
DR   RefSeq; NP_116126.3; NM_032737.3.
DR   PDB; 2LLL; NMR; -; A=469-589.
DR   PDBsum; 2LLL; -.
DR   AlphaFoldDB; Q03252; -.
DR   BMRB; Q03252; -.
DR   SMR; Q03252; -.
DR   BioGRID; 124281; 241.
DR   DIP; DIP-57724N; -.
DR   IntAct; Q03252; 104.
DR   MINT; Q03252; -.
DR   STRING; 9606.ENSP00000327054; -.
DR   GlyGen; Q03252; 4 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; Q03252; -.
DR   MetOSite; Q03252; -.
DR   PhosphoSitePlus; Q03252; -.
DR   SwissPalm; Q03252; -.
DR   BioMuta; LMNB2; -.
DR   DMDM; 23503078; -.
DR   REPRODUCTION-2DPAGE; IPI00009771; -.
DR   jPOST; Q03252; -.
DR   MassIVE; Q03252; -.
DR   PaxDb; 9606-ENSP00000327054; -.
DR   PeptideAtlas; Q03252; -.
DR   ProteomicsDB; 58204; -.
DR   Pumba; Q03252; -.
DR   ABCD; Q03252; 3 sequenced antibodies.
DR   Antibodypedia; 10783; 437 antibodies from 38 providers.
DR   DNASU; 84823; -.
DR   Ensembl; ENST00000325327.4; ENSP00000327054.3; ENSG00000176619.13.
DR   GeneID; 84823; -.
DR   KEGG; hsa:84823; -.
DR   MANE-Select; ENST00000325327.4; ENSP00000327054.3; NM_032737.4; NP_116126.3.
DR   AGR; HGNC:6638; -.
DR   CTD; 84823; -.
DR   DisGeNET; 84823; -.
DR   GeneCards; LMNB2; -.
DR   HGNC; HGNC:6638; LMNB2.
DR   HPA; ENSG00000176619; Low tissue specificity.
DR   MalaCards; LMNB2; -.
DR   MIM; 150341; gene.
DR   MIM; 608709; phenotype.
DR   MIM; 616540; phenotype.
DR   MIM; 619180; phenotype.
DR   neXtProt; NX_Q03252; -.
DR   OpenTargets; ENSG00000176619; -.
DR   Orphanet; 79087; Acquired partial lipodystrophy.
DR   Orphanet; 457265; Progressive myoclonic epilepsy type 9.
DR   PharmGKB; PA30404; -.
DR   VEuPathDB; HostDB:ENSG00000176619; -.
DR   eggNOG; KOG0977; Eukaryota.
DR   GeneTree; ENSGT00940000160274; -.
DR   InParanoid; Q03252; -.
DR   OMA; EMTQMRD; -.
DR   OrthoDB; 102442at2759; -.
DR   PhylomeDB; Q03252; -.
DR   TreeFam; TF101181; -.
DR   PathwayCommons; Q03252; -.
DR   SignaLink; Q03252; -.
DR   BioGRID-ORCS; 84823; 17 hits in 1159 CRISPR screens.
DR   ChiTaRS; LMNB2; human.
DR   EvolutionaryTrace; Q03252; -.
DR   GenomeRNAi; 84823; -.
DR   Pharos; Q03252; Tbio.
DR   PRO; PR:Q03252; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q03252; protein.
DR   Bgee; ENSG00000176619; Expressed in ventricular zone and 116 other cell types or tissues.
DR   GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR   GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR   GO; GO:0005652; C:nuclear lamina; IBA:GO_Central.
DR   GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR   GO; GO:0031507; P:heterochromatin formation; IBA:GO_Central.
DR   GO; GO:0006998; P:nuclear envelope organization; IBA:GO_Central.
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; 2.60.40.1260:FF:000001; Lamin A/C; 1.
DR   FunFam; 1.20.5.170:FF:000076; Lamin B2; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 2.60.40.1260; Lamin Tail domain; 1.
DR   Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 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   PANTHER; PTHR45721; LAMIN DM0-RELATED; 1.
DR   PANTHER; PTHR45721:SF2; LAMIN-B2; 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; Coiled coil; Direct protein sequencing;
KW   Disease variant; Epilepsy; Glycoprotein; Intellectual disability;
KW   Intermediate filament; Isopeptide bond; Lipoprotein; Methylation;
KW   Neurodegeneration; Nucleus; Phosphoprotein; Prenylation;
KW   Primary microcephaly; Proteomics identification; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..617
FT                   /note="Lamin-B2"
FT                   /id="PRO_0000063820"
FT   PROPEP          618..620
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P20700"
FT                   /id="PRO_0000403470"
FT   DOMAIN          46..402
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   DOMAIN          462..579
FT                   /note="LTD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01187"
FT   REGION          1..48
FT                   /note="Head"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          49..83
FT                   /note="Coil 1A"
FT   REGION          84..95
FT                   /note="Linker 1"
FT   REGION          96..229
FT                   /note="Coil 1B"
FT   REGION          230..256
FT                   /note="Linker 2"
FT   REGION          257..400
FT                   /note="Coil 2"
FT   REGION          399..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          401..620
FT                   /note="Tail"
FT   REGION          581..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           435..440
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        588..601
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..620
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         23
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         34
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         37
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         81
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         316
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         407
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02545"
FT   MOD_RES         420
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         422
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:21406692"
FT   MOD_RES         424
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:21406692"
FT   MOD_RES         426
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:21406692"
FT   MOD_RES         433
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P21619"
FT   MOD_RES         497
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         617
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250|UniProtKB:P20700"
FT   LIPID           617
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P20700"
FT   CARBOHYD        413
FT                   /note="O-linked (GlcNAc) threonine"
FT                   /evidence="ECO:0000269|PubMed:26237509"
FT   CROSSLNK        77
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        81
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:25755297,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        195
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        255
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        489
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VARIANT         54
FT                   /note="N -> H (in MCPH27; increased aggregation; changed
FT                   nuclear envelope organization; dbSNP:rs1972096108)"
FT                   /evidence="ECO:0000269|PubMed:33033404"
FT                   /id="VAR_085504"
FT   VARIANT         157
FT                   /note="H -> Y (in EPM9; disrupts fibrillar formation;
FT                   dbSNP:rs797045143)"
FT                   /evidence="ECO:0000269|PubMed:25954030"
FT                   /id="VAR_074170"
FT   VARIANT         235
FT                   /note="R -> Q (may be a risk factor for partial acquired
FT                   lipodystrophy; dbSNP:rs121912497)"
FT                   /evidence="ECO:0000269|PubMed:16826530,
FT                   ECO:0000269|PubMed:27535533"
FT                   /id="VAR_031063"
FT   VARIANT         236
FT                   /note="R -> W (in a colorectal cancer sample; somatic
FT                   mutation; dbSNP:rs774297966)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036370"
FT   VARIANT         252
FT                   /note="Y -> H (in APLD)"
FT                   /evidence="ECO:0000269|PubMed:22768673"
FT                   /id="VAR_074171"
FT   VARIANT         398
FT                   /note="E -> K (in MCPH27; increased aggregation; changed
FT                   nuclear envelope organization; dbSNP:rs1971791380)"
FT                   /evidence="ECO:0000269|PubMed:33033404"
FT                   /id="VAR_085505"
FT   VARIANT         427
FT                   /note="A -> T (in APLD; dbSNP:rs57521499)"
FT                   /evidence="ECO:0000269|PubMed:16826530"
FT                   /id="VAR_031064"
FT   CONFLICT        401
FT                   /note="R -> S (in Ref. 5; AAA80979)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        439..475
FT                   /note="LEVEEPLGSGPSVLGTGTGGSGGFHLAQQASASGSVS -> WRWRSPWQRPK
FT                   RPGHGHGWQRWLPPGPAGLGLGQRH (in Ref. 5; AAA80979)"
FT                   /evidence="ECO:0000305"
FT   STRAND          473..479
FT                   /evidence="ECO:0007829|PDB:2LLL"
FT   STRAND          484..490
FT                   /evidence="ECO:0007829|PDB:2LLL"
FT   STRAND          492..494
FT                   /evidence="ECO:0007829|PDB:2LLL"
FT   STRAND          502..507
FT                   /evidence="ECO:0007829|PDB:2LLL"
FT   STRAND          512..516
FT                   /evidence="ECO:0007829|PDB:2LLL"
FT   STRAND          528..533
FT                   /evidence="ECO:0007829|PDB:2LLL"
FT   HELIX           534..536
FT                   /evidence="ECO:0007829|PDB:2LLL"
FT   TURN            542..544
FT                   /evidence="ECO:0007829|PDB:2LLL"
FT   STRAND          545..548
FT                   /evidence="ECO:0007829|PDB:2LLL"
FT   STRAND          552..555
FT                   /evidence="ECO:0007829|PDB:2LLL"
FT   STRAND          558..565
FT                   /evidence="ECO:0007829|PDB:2LLL"
FT   STRAND          571..580
FT                   /evidence="ECO:0007829|PDB:2LLL"
SQ   SEQUENCE   620 AA;  69948 MW;  A8799BB12B6242B9 CRC64;
     MSPPSPGRRR EQRRPRAAAT MATPLPGRAG GPATPLSPTR LSRLQEKEEL RELNDRLAHY
     IDRVRALELE NDRLLLKISE KEEVTTREVS GIKALYESEL ADARRVLDET ARERARLQIE
     IGKLRAELDE VNKSAKKREG ELTVAQGRVK DLESLFHRSE VELAAALSDK RGLESDVAEL
     RAQLAKAEDG HAVAKKQLEK ETLMRVDLEN RCQSLQEELD FRKSVFEEEV RETRRRHERR
     LVEVDSSRQQ EYDFKMAQAL EELRSQHDEQ VRLYKLELEQ TYQAKLDSAK LSSDQNDKAA
     SAAREELKEA RMRLESLSYQ LSGLQKQASA AEDRIRELEE AMAGERDKFR KMLDAKEQEM
     TEMRDVMQQQ LAEYQELLDV KLALDMEINA YRKLLEGEEE RLKLSPSPSS RVTVSRATSS
     SSGSLSATGR LGRSKRKRLE VEEPLGSGPS VLGTGTGGSG GFHLAQQASA SGSVSIEEID
     LEGKFVQLKN NSDKDQSLGN WRIKRQVLEG EEIAYKFTPK YILRAGQMVT VWAAGAGVAH
     SPPSTLVWKG QSSWGTGESF RTVLVNADGE EVAMRTVKKS SVMRENENGE EEEEEAEFGE
     EDLFHQQGDP RTTSRGCYVM
//