LMNB2_HUMAN
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 03-AUG-2022, entry version 214.
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 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 [23]
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 [24]
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 [25]
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 [26]
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 [27]
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 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:33033404}.
CC -!- SUBUNIT: Interacts with TMEM43. {ECO:0000250}.
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=6; IntAct=EBI-2830427, EBI-351935;
CC Q03252; P20700: LMNB1; NbExp=5; 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.
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 -!- 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 -!- SEQUENCE CAUTION:
CC Sequence=AAH06551.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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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 PDB; 5BNW; X-ray; 2.40 A; D=403-415.
DR PDBsum; 2LLL; -.
DR PDBsum; 5BNW; -.
DR AlphaFoldDB; Q03252; -.
DR BMRB; Q03252; -.
DR SMR; Q03252; -.
DR BioGRID; 124281; 213.
DR DIP; DIP-57724N; -.
DR IntAct; Q03252; 63.
DR MINT; Q03252; -.
DR STRING; 9606.ENSP00000327054; -.
DR GlyGen; Q03252; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q03252; -.
DR MetOSite; Q03252; -.
DR PhosphoSitePlus; Q03252; -.
DR SwissPalm; Q03252; -.
DR BioMuta; LMNB2; -.
DR DMDM; 23503078; -.
DR REPRODUCTION-2DPAGE; IPI00009771; -.
DR EPD; Q03252; -.
DR jPOST; Q03252; -.
DR MassIVE; Q03252; -.
DR MaxQB; Q03252; -.
DR PaxDb; Q03252; -.
DR PeptideAtlas; Q03252; -.
DR PRIDE; Q03252; -.
DR ProteomicsDB; 58204; -.
DR ABCD; Q03252; 3 sequenced antibodies.
DR Antibodypedia; 10783; 364 antibodies from 37 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 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; 701388at2759; -.
DR PhylomeDB; Q03252; -.
DR TreeFam; TF101181; -.
DR PathwayCommons; Q03252; -.
DR SignaLink; Q03252; -.
DR BioGRID-ORCS; 84823; 17 hits in 1081 CRISPR screens.
DR ChiTaRS; LMNB2; human.
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 114 other 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 assembly; 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 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; Coiled coil; Direct protein sequencing;
KW Disease variant; Epilepsy; Intellectual disability; Intermediate filament;
KW Isopeptide bond; Lipoprotein; Methylation; Neurodegeneration; Nucleus;
KW Phosphoprotein; Prenylation; Primary microcephaly; 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"
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 406..429
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 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"
FT LIPID 617
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
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)"
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)"
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
