LMNB2_MOUSE
ID LMNB2_MOUSE Reviewed; 596 AA.
AC P21619; P48680; Q8CGB1;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Lamin-B2;
DE Flags: Precursor;
GN Name=Lmnb2;
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] (ISOFORM B2).
RX PubMed=2102682; DOI=10.1007/bf01726689;
RA Hoeger T.H., Zatloukal K., Waizenegger I., Krohne G.;
RT "Characterization of a second highly conserved B-type lamin present in
RT cells previously thought to contain only a single B-type lamin.";
RL Chromosoma 99:379-390(1990).
RN [2]
RP ERRATUM OF PUBMED:2102682.
RX PubMed=2102440; DOI=10.1007/bf00337604;
RA Hoeger T.H., Zatloukal K., Waizenegger I., Krohne G.;
RL Chromosoma 100:67-69(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B3).
RX PubMed=8094052; DOI=10.1002/j.1460-2075.1993.tb05635.x;
RA Furukawa K., Hotta Y.;
RT "cDNA cloning of a germ cell specific lamin B3 from mouse spermatocytes and
RT analysis of its function by ectopic expression in somatic cells.";
RL EMBO J. 12:97-106(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
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 PROTEIN SEQUENCE OF 165-172; 254-262 AND 482-491.
RX PubMed=1939065; DOI=10.1016/s0021-9258(18)54886-9;
RA Kasahara K., Chida K., Tsunenaga M., Kohno Y., Ikuta T., Kuroki T.;
RT "Identification of lamin B2 as a substrate of protein kinase C in BALB/MK-2
RT mouse keratinocytes.";
RL J. Biol. Chem. 266:20018-20023(1991).
RN [6]
RP PROTEIN SEQUENCE OF 182-206; 234-286; 290-319; 364-401 AND 470-496.
RX PubMed=2311764; DOI=10.1016/0014-5793(90)80592-7;
RA Weber K., Plessmann U., Traub P.;
RT "Protein chemical analysis of purified murine lamin B identifies two
RT distinct polypeptides B1 and B2.";
RL FEBS Lett. 261:361-364(1990).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [8]
RP INTERACTION WITH TMEM43.
RX PubMed=18230648; DOI=10.1242/jcs.019281;
RA Bengtsson L., Otto H.;
RT "LUMA interacts with emerin and influences its distribution at the inner
RT nuclear membrane.";
RL J. Cell Sci. 121:536-548(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, and Spleen;
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 [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-413, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
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:Q03252}.
CC -!- SUBUNIT: Interacts with TMEM43. {ECO:0000269|PubMed:18230648}.
CC -!- SUBCELLULAR LOCATION: Nucleus lamina {ECO:0000250|UniProtKB:Q03252}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B2;
CC IsoId=P21619-1; Sequence=Displayed;
CC Name=B3;
CC IsoId=P21619-2, P48680-1;
CC Sequence=VSP_017070;
CC -!- TISSUE SPECIFICITY: Isoform B3 is germ cell specific.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH42430.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH51985.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X54098; CAA38032.1; -; mRNA.
DR EMBL; D13455; BAA02708.1; -; mRNA.
DR EMBL; BC042430; AAH42430.1; ALT_INIT; mRNA.
DR EMBL; BC051985; AAH51985.1; ALT_INIT; mRNA.
DR CCDS; CCDS83733.1; -. [P21619-2]
DR PIR; B48315; B48315.
DR PIR; S28419; S28419.
DR RefSeq; NP_001334069.1; NM_001347140.1. [P21619-2]
DR RefSeq; NP_034852.2; NM_010722.5.
DR AlphaFoldDB; P21619; -.
DR SMR; P21619; -.
DR BioGRID; 201178; 11.
DR IntAct; P21619; 4.
DR MINT; P21619; -.
DR STRING; 10090.ENSMUSP00000057291; -.
DR iPTMnet; P21619; -.
DR PhosphoSitePlus; P21619; -.
DR EPD; P21619; -.
DR jPOST; P21619; -.
DR MaxQB; P21619; -.
DR PaxDb; P21619; -.
DR PeptideAtlas; P21619; -.
DR PRIDE; P21619; -.
DR ProteomicsDB; 286221; -. [P21619-1]
DR ProteomicsDB; 286222; -. [P21619-2]
DR Antibodypedia; 10783; 364 antibodies from 37 providers.
DR DNASU; 16907; -.
DR Ensembl; ENSMUST00000105332; ENSMUSP00000100969; ENSMUSG00000062075. [P21619-2]
DR Ensembl; ENSMUST00000179022; ENSMUSP00000136524; ENSMUSG00000062075. [P21619-1]
DR GeneID; 16907; -.
DR KEGG; mmu:16907; -.
DR UCSC; uc007gfk.1; mouse. [P21619-1]
DR CTD; 84823; -.
DR MGI; MGI:96796; Lmnb2.
DR VEuPathDB; HostDB:ENSMUSG00000062075; -.
DR eggNOG; KOG0977; Eukaryota.
DR GeneTree; ENSGT00940000160274; -.
DR HOGENOM; CLU_012560_9_2_1; -.
DR InParanoid; P21619; -.
DR OrthoDB; 701388at2759; -.
DR PhylomeDB; P21619; -.
DR TreeFam; TF101181; -.
DR BioGRID-ORCS; 16907; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Lmnb2; mouse.
DR PRO; PR:P21619; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P21619; protein.
DR Bgee; ENSMUSG00000062075; Expressed in spermatid and 170 other tissues.
DR ExpressionAtlas; P21619; baseline and differential.
DR Genevisible; P21619; MM.
DR GO; GO:0005638; C:lamin filament; IDA:MGI.
DR GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR GO; GO:0005652; C:nuclear lamina; IBA:GO_Central.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
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 Acetylation; Alternative splicing; Coiled coil; Direct protein sequencing;
KW Intermediate filament; Isopeptide bond; Lipoprotein; Methylation; Nucleus;
KW Phosphoprotein; Prenylation; Reference proteome; Ubl conjugation.
FT CHAIN 1..593
FT /note="Lamin-B2"
FT /id="PRO_0000063821"
FT PROPEP 594..596
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000403471"
FT DOMAIN 24..380
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT DOMAIN 438..559
FT /note="LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01187"
FT REGION 1..26
FT /note="Head"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 27..61
FT /note="Coil 1A"
FT REGION 62..73
FT /note="Linker 1"
FT REGION 74..207
FT /note="Coil 1B"
FT REGION 208..234
FT /note="Linker 2"
FT REGION 235..378
FT /note="Coil 2"
FT REGION 376..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..596
FT /note="Tail"
FT REGION 552..596
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 384..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q03252"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03252"
FT MOD_RES 59
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03252"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03252"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03252"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03252"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03252"
FT MOD_RES 413
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03252"
FT MOD_RES 593
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 593
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
FT CROSSLNK 59
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03252"
FT CROSSLNK 173
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q03252"
FT CROSSLNK 233
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q03252"
FT CROSSLNK 465
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q03252"
FT VAR_SEQ 1..206
FT /note="MASLPPHAGPATPLSPTRLSRLQEKEELRELNDRLAHYIDRVRALELENDRL
FT LLRISEKEEVTTREVSGIKTLYESELADARRVLDETARERARLQIEIGKVQAELEEARK
FT SAKKREGELTVAQGRVKDLESLFHRSEAELATALSDKQGLETEVAELRAQLAKAEDGHA
FT VAKKQLEKETLMRVDLENRCQSLQEELAFSKSVFEE -> MGESESMRGTGEGCGRDCP
FT EAARPLMETVEGALPELRGRPLREYVKRRPRGLGKTPVEDPVKSEGAVGYPRTWNNHLR
FT VPTREQ (in isoform B3)"
FT /evidence="ECO:0000303|PubMed:8094052"
FT /id="VSP_017070"
FT CONFLICT 148..149
FT /note="KQ -> NE (in Ref. 1; CAA38032)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="H -> R (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="A -> R (in Ref. 1; CAA38032)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="A -> R (in Ref. 1; CAA38032)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="Missing (in Ref. 1; CAA38032)"
FT /evidence="ECO:0000305"
FT CONFLICT 412..413
FT /note="GR -> RG (in Ref. 1; CAA38032)"
FT /evidence="ECO:0000305"
FT CONFLICT 421..422
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="Missing (in Ref. 1; CAA38032)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 596 AA; 67318 MW; 4FEF5A76FFDF2D96 CRC64;
MASLPPHAGP ATPLSPTRLS RLQEKEELRE LNDRLAHYID RVRALELEND RLLLRISEKE
EVTTREVSGI KTLYESELAD ARRVLDETAR ERARLQIEIG KVQAELEEAR KSAKKREGEL
TVAQGRVKDL ESLFHRSEAE LATALSDKQG LETEVAELRA QLAKAEDGHA VAKKQLEKET
LMRVDLENRC QSLQEELAFS KSVFEEEVRE TRRRHERRLV EVDSSRQQEY DFKMAQALED
LRSQHDEQVR LYRVELEQTY QAKLDNAKLL SDQNDKAAHA AREELKEARM RVESLSYQLL
GLQKQASAAE NHIHELEEAL AGERDKFRKM LDAKEQEMTE VRDAMQQQLA EYQELLDIKL
ALDMEISAYR KLLEGEEERL KLSPSPSSRI TISRATSSSS SSSGVGMSVG QGRGKRRRLE
TEDTSGSPSR ASRVSSGSRL AQQTVATGVV NIDEVDPEGR FVRLKNSSDK DQSLGNWRIK
RQVLEGEDIA YKFTPKYVLR AGQTVTVWAA GAGATHSPPS TLVWKSQTNW GPGESFRTAL
VSADGEEVAV KAAKHSSVQG RENGEEEEEE EAEFGEEDLF HQQGDPRTTS RGCRLM
