LMNB1_MOUSE
ID LMNB1_MOUSE Reviewed; 588 AA.
AC P14733; Q61791;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Lamin-B1;
DE Flags: Precursor;
GN Name=Lmnb1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=3243285;
RA Hoeger T.H., Krohne G., Franke W.W.;
RT "Amino acid sequence and molecular characterization of murine lamin B as
RT deduced from cDNA clones.";
RL Eur. J. Cell Biol. 47:283-290(1988).
RN [2]
RP SEQUENCE REVISION.
RA Hoeger T.H.;
RL Submitted (OCT-1989) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C3H/He;
RX PubMed=8586436; DOI=10.1006/geno.1995.9868;
RA Maeno H., Sugimoto K., Nakajima N.;
RT "Genomic structure of the mouse gene (Lmnb1) encoding nuclear lamin B1.";
RL Genomics 30:342-346(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND THR-21, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-112; LYS-272 AND LYS-331, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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:0000250|UniProtKB:P20700}.
CC -!- SUBUNIT: Homodimer. Interacts with lamin-associated polypeptides IA, IB
CC and 2. Interacts with SPAG4 and SEPT12 (By similarity).
CC {ECO:0000250|UniProtKB:P20700}.
CC -!- SUBCELLULAR LOCATION: Nucleus lamina {ECO:0000250|UniProtKB:P20700}.
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 -!- 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}.
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DR EMBL; X16705; CAA34677.1; -; mRNA.
DR EMBL; M35153; AAC96023.1; ALT_SEQ; mRNA.
DR EMBL; D50080; BAA08784.1; -; Genomic_DNA.
DR EMBL; BC052729; AAH52729.1; -; mRNA.
DR EMBL; BC058392; AAH58392.1; -; mRNA.
DR CCDS; CCDS29261.1; -.
DR PIR; S07720; S07720.
DR RefSeq; NP_034851.2; NM_010721.2.
DR AlphaFoldDB; P14733; -.
DR BMRB; P14733; -.
DR SMR; P14733; -.
DR BioGRID; 201177; 24.
DR IntAct; P14733; 16.
DR MINT; P14733; -.
DR STRING; 10090.ENSMUSP00000025486; -.
DR iPTMnet; P14733; -.
DR PhosphoSitePlus; P14733; -.
DR SwissPalm; P14733; -.
DR REPRODUCTION-2DPAGE; IPI00230394; -.
DR SWISS-2DPAGE; P14733; -.
DR EPD; P14733; -.
DR jPOST; P14733; -.
DR MaxQB; P14733; -.
DR PaxDb; P14733; -.
DR PeptideAtlas; P14733; -.
DR PRIDE; P14733; -.
DR ProteomicsDB; 286220; -.
DR Antibodypedia; 3937; 820 antibodies from 48 providers.
DR DNASU; 16906; -.
DR Ensembl; ENSMUST00000025486; ENSMUSP00000025486; ENSMUSG00000024590.
DR GeneID; 16906; -.
DR KEGG; mmu:16906; -.
DR UCSC; uc012bdd.2; mouse.
DR CTD; 4001; -.
DR MGI; MGI:96795; Lmnb1.
DR VEuPathDB; HostDB:ENSMUSG00000024590; -.
DR eggNOG; KOG0977; Eukaryota.
DR GeneTree; ENSGT00940000157199; -.
DR HOGENOM; CLU_012560_9_2_1; -.
DR InParanoid; P14733; -.
DR OMA; IGQWAIK; -.
DR OrthoDB; 701388at2759; -.
DR PhylomeDB; P14733; -.
DR TreeFam; TF101181; -.
DR Reactome; R-MMU-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR Reactome; R-MMU-352238; Breakdown of the nuclear lamina.
DR Reactome; R-MMU-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR BioGRID-ORCS; 16906; 13 hits in 77 CRISPR screens.
DR ChiTaRS; Lmnb1; mouse.
DR PRO; PR:P14733; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; P14733; protein.
DR Bgee; ENSMUSG00000024590; Expressed in ventricular zone and 232 other tissues.
DR Genevisible; P14733; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005638; C:lamin filament; IDA:MGI.
DR GO; GO:0005635; C:nuclear envelope; IDA:BHF-UCL.
DR GO; GO:0005637; C:nuclear inner membrane; IDA:MGI.
DR GO; GO:0005652; C:nuclear lamina; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; IDA:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:MGI.
DR GO; GO:0008432; F:JUN kinase binding; NAS:BHF-UCL.
DR GO; GO:0043274; F:phospholipase binding; IPI:BHF-UCL.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:MGI.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:1904609; P:cellular response to monosodium L-glutamate; ISO:MGI.
DR GO; GO:0031507; P:heterochromatin assembly; IBA:GO_Central.
DR GO; GO:0006998; P:nuclear envelope organization; ISS: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:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; NAS:BHF-UCL.
DR GO; GO:0046330; P:positive regulation of JNK cascade; NAS:BHF-UCL.
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 Acetylation; Coiled coil; Direct protein sequencing; Disulfide bond;
KW Intermediate filament; Isopeptide bond; Lipoprotein; Methylation; Nucleus;
KW Phosphoprotein; Prenylation; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT CHAIN 2..585
FT /note="Lamin-B1"
FT /id="PRO_0000063817"
FT PROPEP 586..588
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000403467"
FT DOMAIN 33..389
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT DOMAIN 431..547
FT /note="LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01187"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..35
FT /note="Head"
FT REGION 36..70
FT /note="Coil 1A"
FT REGION 71..82
FT /note="Linker 1"
FT REGION 83..216
FT /note="Coil 1B"
FT REGION 217..244
FT /note="Linker 2"
FT REGION 245..387
FT /note="Coil 2"
FT REGION 388..588
FT /note="Tail"
FT REGION 391..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 416..421
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT MOD_RES 5
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT MOD_RES 15
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 21
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 26
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT MOD_RES 112
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70615"
FT MOD_RES 158
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70615"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT MOD_RES 272
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT MOD_RES 331
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT MOD_RES 414
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P21619"
FT MOD_RES 484
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT MOD_RES 585
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 585
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
FT DISULFID 318
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CROSSLNK 103
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT CROSSLNK 124
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT CROSSLNK 146
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT CROSSLNK 158
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT CROSSLNK 182
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT CROSSLNK 242
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT CROSSLNK 262
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT CROSSLNK 272
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT CROSSLNK 313
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT CROSSLNK 331
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT CROSSLNK 533
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT CROSSLNK 548
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT CONFLICT 581
FT /note="S -> W (in Ref. 1; CAA34677/AAC96023)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 588 AA; 66786 MW; 3602BCE63588A32D CRC64;
MATATPVQQQ RAGSRASAPA TPLSPTRLSR LQEKEELREL NDRLAVYIDK VRSLETENSA
LQLQVTEREE VRGRELTGLK ALYETELADA RRALDDTARE RAKLQIELGK FKAEHDQLLL
NYAKKESDLS GAQIKLREYE AALNSKDAAL ATALGDKKSL EGDLEDLKDQ IAQLEASLSA
AKKQLADETL LKVDLENRCQ SLTEDLEFRK NMYEEEINET RRKHETRLVE VDSGRQIEYE
YKLAQALHEM REQHDAQVRL YKEELEQTYH AKLENARLSS EMNTSTVNSA REELMESRMR
IESLSSQLSN LQKESRACLE RIQELEDMLA KERDNSRRML SDREREMAEI RDQMQQQLSD
YEQLLDVKLA LDMEISAYRK LLEGEEERLK LSPSPSSRVT VSRASSSRSV RTTRGKRKRV
DVEESEASSS VSISHSASAT GNVCIEEIDV DGKFIRLKNT SEQDQPMGGW EMIRKIGDTS
VSYKYTSRYV LKAGQTVTVW AANAGVTASP PTDLIWKNQN SWGTGEDVKV ILKNSQGEEV
AQRSTVFKTT IPEEEEEEEE EPIGVAVEEE RFHQQGAPRA SNKSCAIM
