LMNB1_RAT
ID LMNB1_RAT Reviewed; 587 AA.
AC P70615;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Lamin-B1;
DE Flags: Precursor;
GN Name=Lmnb1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Testis;
RA Prakash A.B., Rao M.R.S.;
RT "Rattus norvegicus Lamin B1 sequence.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 52-67; 198-208 AND 368-378, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP PROTEIN SEQUENCE OF 259-266; 368-376 AND 474-482.
RC TISSUE=Liver;
RX PubMed=16128803; DOI=10.1111/j.1742-4658.2005.04847.x;
RA Segawa M., Niino K., Mineki R., Kaga N., Murayama K., Sugimoto K.,
RA Watanabe Y., Furukawa K., Horigome T.;
RT "Proteome analysis of a rat liver nuclear insoluble protein fraction and
RT localization of a novel protein, ISP36, to compartments in the
RT interchromatin space.";
RL FEBS J. 272:4327-4338(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126; SER-158 AND THR-576, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; U72353; AAB09600.1; -; mRNA.
DR RefSeq; NP_446357.1; NM_053905.1.
DR AlphaFoldDB; P70615; -.
DR BMRB; P70615; -.
DR SMR; P70615; -.
DR BioGRID; 250568; 14.
DR IntAct; P70615; 1.
DR MINT; P70615; -.
DR STRING; 10116.ENSRNOP00000019351; -.
DR CarbonylDB; P70615; -.
DR iPTMnet; P70615; -.
DR PhosphoSitePlus; P70615; -.
DR World-2DPAGE; 0004:P70615; -.
DR jPOST; P70615; -.
DR PaxDb; P70615; -.
DR PRIDE; P70615; -.
DR GeneID; 116685; -.
DR KEGG; rno:116685; -.
DR UCSC; RGD:620522; rat.
DR CTD; 4001; -.
DR RGD; 620522; Lmnb1.
DR eggNOG; KOG0977; Eukaryota.
DR InParanoid; P70615; -.
DR OrthoDB; 701388at2759; -.
DR PhylomeDB; P70615; -.
DR Reactome; R-RNO-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR Reactome; R-RNO-352238; Breakdown of the nuclear lamina.
DR Reactome; R-RNO-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-RNO-9013405; RHOD GTPase cycle.
DR Reactome; R-RNO-9035034; RHOF GTPase cycle.
DR PRO; PR:P70615; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005638; C:lamin filament; ISO:RGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:RGD.
DR GO; GO:0005637; C:nuclear inner membrane; ISO:RGD.
DR GO; GO:0005652; C:nuclear lamina; IDA:RGD.
DR GO; GO:0016363; C:nuclear matrix; IDA:RGD.
DR GO; GO:0031965; C:nuclear membrane; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:RGD.
DR GO; GO:0043274; F:phospholipase binding; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEP:RGD.
DR GO; GO:0071386; P:cellular response to corticosterone stimulus; IEP:RGD.
DR GO; GO:1904609; P:cellular response to monosodium L-glutamate; IDA:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
DR GO; GO:0031507; P:heterochromatin assembly; IBA:GO_Central.
DR GO; GO:0022008; P:neurogenesis; IEP:RGD.
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:0090435; P:protein localization to nuclear envelope; IBA:GO_Central.
DR GO; GO:0046677; P:response to antibiotic; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
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..584
FT /note="Lamin-B1"
FT /id="PRO_0000063818"
FT PROPEP 585..587
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000403468"
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..29
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..587
FT /note="Tail"
FT REGION 390..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..587
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 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..408
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 14
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14733"
FT MOD_RES 20
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT MOD_RES 25
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT MOD_RES 111
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P14733"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 157
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT MOD_RES 271
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20700"
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:0000250|UniProtKB:P20700"
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:0000250|UniProtKB:P20700"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT MOD_RES 576
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 584
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 584
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
FT DISULFID 317
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CROSSLNK 102
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT CROSSLNK 123
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT CROSSLNK 145
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT CROSSLNK 157
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT CROSSLNK 181
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT CROSSLNK 241
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT CROSSLNK 261
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT CROSSLNK 271
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT CROSSLNK 312
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT CROSSLNK 330
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT CROSSLNK 532
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P20700"
FT CROSSLNK 547
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P20700"
SQ SEQUENCE 587 AA; 66606 MW; 8187CA32728CC012 CRC64;
MATATPVQQR AGSRASAPAT PFSPTRLSRL QEKEELRELN DRLAVYIDKV RSLETENSAL
QLQVTEREEV RGRELTGLKA LYETELADAR RALDDTARER AKLQIELGKF KAEHDQLLLN
YAKKESDLSG AQIKLREYEA ALNSKDAALA TALGDKKSLE GDLEDLKDQI AQLEASLSAA
KKQLADETLL KVDLENRCQS LTEDLEFRKN MYEEEINETR RKHETRLVEV DSGRQIEYEY
KLAQALHEMR EQHDAQVRLY KEELEQTYHA KLENARLSSE MNTSTVNSAR GGMMESRMRI
ESLSSQLSNL QKDSRACLER IQELEDMLAK ERDNSRRMLS DKEREMAEIR DQMQQQLNDY
EQLLDVKLAL DMEISAYRKL LEGEEERLKL SPSPSSRVTV SRASSSRSVR TTRGKRKRVD
VEESEASSSV SISHSASATG NVCIEEIDVD GKFIRLKNTS EQDQPMGGWE MIRKIGDTSV
SYKYTSRYVL KAGQTVTVWA ANAGVTASPP TDLIWKNQNS WGTGEDVKVV LKNSQGEEVA
QRSTVFKTTI PEEEEEEEEE PIGVPLEEER FHQQGTPRAS NKSCAIM
