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Protein

Lamin-B1

Gene

Lmnb1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin.

GO - Molecular functioni

  • JUN kinase binding Source: BHF-UCL
  • phospholipase binding Source: BHF-UCL
  • structural molecule activity Source: InterPro

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-1221632. Meiotic synapsis.
R-MMU-1221633. Meiotic Synapsis.
R-MMU-2559584. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
R-MMU-352238. Breakdown of the nuclear lamina.

Names & Taxonomyi

Protein namesi
Recommended name:
Lamin-B1
Gene namesi
Name:Lmnb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:96795. Lmnb1.

Subcellular locationi

GO - Cellular componenti

  • lamin filament Source: MGI
  • membrane Source: MGI
  • nuclear envelope Source: BHF-UCL
  • nuclear inner membrane Source: UniProtKB-SubCell
  • nuclear matrix Source: MGI
  • nuclear membrane Source: MGI
  • nucleoplasm Source: BHF-UCL
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 585584Lamin-B1PRO_0000063817Add
BLAST
Propeptidei586 – 5883Removed in mature formBy similarityPRO_0000403467

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei3 – 31PhosphothreonineBy similarity
Modified residuei5 – 51PhosphothreonineBy similarity
Modified residuei17 – 171PhosphoserineCombined sources
Modified residuei21 – 211PhosphothreonineCombined sources
Modified residuei24 – 241PhosphoserineCombined sources
Cross-linki103 – 103Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei112 – 1121N6-acetyllysineCombined sources
Modified residuei127 – 1271PhosphoserineBy similarity
Cross-linki146 – 146Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei158 – 1581N6-acetyllysineBy similarity
Modified residuei159 – 1591PhosphoserineBy similarity
Cross-linki242 – 242Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki262 – 262Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei272 – 2721N6-acetyllysineCombined sources
Disulfide bondi318 – 318InterchainBy similarity
Modified residuei331 – 3311N6-acetyllysineCombined sources
Modified residuei376 – 3761PhosphoserineBy similarity
Modified residuei484 – 4841N6-acetyllysineBy similarity
Modified residuei585 – 5851Cysteine methyl esterBy similarity
Lipidationi585 – 5851S-farnesyl cysteineBy similarity

Post-translational modificationi

B-type lamins undergo a series of modifications, such as farnesylation and phosphorylation. Increased phosphorylation of the lamins occurs before envelope disintegration and probably plays a role in regulating lamin associations.

Keywords - PTMi

Acetylation, Disulfide bond, Isopeptide bond, Lipoprotein, Methylation, Phosphoprotein, Prenylation, Ubl conjugation

Proteomic databases

EPDiP14733.
MaxQBiP14733.
PaxDbiP14733.
PRIDEiP14733.

2D gel databases

REPRODUCTION-2DPAGEIPI00230394.
SWISS-2DPAGEP14733.

PTM databases

iPTMnetiP14733.
PhosphoSiteiP14733.

Expressioni

Gene expression databases

BgeeiP14733.
CleanExiMM_LMNB1.
GenevisibleiP14733. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with lamin-associated polypeptides IA, IB and 2 (By similarity).By similarity

GO - Molecular functioni

  • JUN kinase binding Source: BHF-UCL
  • phospholipase binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi201177. 6 interactions.
IntActiP14733. 8 interactions.
MINTiMINT-1726964.
STRINGi10090.ENSMUSP00000025486.

Structurei

3D structure databases

ProteinModelPortaliP14733.
SMRiP14733. Positions 312-386, 432-549.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini435 – 547113LTDAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 3534HeadAdd
BLAST
Regioni36 – 387352RodAdd
BLAST
Regioni36 – 7035Coil 1AAdd
BLAST
Regioni71 – 8212Linker 1Add
BLAST
Regioni83 – 216134Coil 1BAdd
BLAST
Regioni217 – 24428Linker 2Add
BLAST
Regioni245 – 387143Coil 2Add
BLAST
Regioni388 – 588201TailAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi416 – 4216Nuclear localization signalSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi553 – 5619Glu-rich (highly acidic; could be involved in chromatin binding)

Sequence similaritiesi

Belongs to the intermediate filament family.Curated
Contains 1 LTD domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0977. Eukaryota.
ENOG410Y2H6. LUCA.
GeneTreeiENSGT00830000128282.
HOGENOMiHOG000007711.
HOVERGENiHBG013015.
InParanoidiP14733.
KOiK07611.
OMAiEMNTSSV.
OrthoDBiEOG7MD4PW.
PhylomeDBiP14733.
TreeFamiTF101181.

Family and domain databases

Gene3Di2.60.40.1260. 1 hit.
InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR027696. Lamin_B.
IPR001322. Lamin_tail_dom.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF157. PTHR23239:SF157. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF00932. LTD. 1 hit.
[Graphical view]
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
SUPFAMiSSF74853. SSF74853. 1 hit.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14733-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATATPVQQQ RAGSRASAPA TPLSPTRLSR LQEKEELREL NDRLAVYIDK
60 70 80 90 100
VRSLETENSA LQLQVTEREE VRGRELTGLK ALYETELADA RRALDDTARE
110 120 130 140 150
RAKLQIELGK FKAEHDQLLL NYAKKESDLS GAQIKLREYE AALNSKDAAL
160 170 180 190 200
ATALGDKKSL EGDLEDLKDQ IAQLEASLSA AKKQLADETL LKVDLENRCQ
210 220 230 240 250
SLTEDLEFRK NMYEEEINET RRKHETRLVE VDSGRQIEYE YKLAQALHEM
260 270 280 290 300
REQHDAQVRL YKEELEQTYH AKLENARLSS EMNTSTVNSA REELMESRMR
310 320 330 340 350
IESLSSQLSN LQKESRACLE RIQELEDMLA KERDNSRRML SDREREMAEI
360 370 380 390 400
RDQMQQQLSD YEQLLDVKLA LDMEISAYRK LLEGEEERLK LSPSPSSRVT
410 420 430 440 450
VSRASSSRSV RTTRGKRKRV DVEESEASSS VSISHSASAT GNVCIEEIDV
460 470 480 490 500
DGKFIRLKNT SEQDQPMGGW EMIRKIGDTS VSYKYTSRYV LKAGQTVTVW
510 520 530 540 550
AANAGVTASP PTDLIWKNQN SWGTGEDVKV ILKNSQGEEV AQRSTVFKTT
560 570 580
IPEEEEEEEE EPIGVAVEEE RFHQQGAPRA SNKSCAIM
Length:588
Mass (Da):66,786
Last modified:January 23, 2007 - v3
Checksum:i3602BCE63588A32D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti581 – 5811S → W in CAA34677 (PubMed:3243285).Curated
Sequence conflicti581 – 5811S → W in AAC96023 (PubMed:3243285).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16705 mRNA. Translation: CAA34677.1.
M35153 mRNA. Translation: AAC96023.1. Sequence problems.
D50080 Genomic DNA. Translation: BAA08784.1.
BC052729 mRNA. Translation: AAH52729.1.
BC058392 mRNA. Translation: AAH58392.1.
CCDSiCCDS29261.1.
PIRiS07720.
RefSeqiNP_034851.2. NM_010721.2.
UniGeneiMm.4105.

Genome annotation databases

EnsembliENSMUST00000025486; ENSMUSP00000025486; ENSMUSG00000024590.
GeneIDi16906.
KEGGimmu:16906.
UCSCiuc012bdd.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16705 mRNA. Translation: CAA34677.1.
M35153 mRNA. Translation: AAC96023.1. Sequence problems.
D50080 Genomic DNA. Translation: BAA08784.1.
BC052729 mRNA. Translation: AAH52729.1.
BC058392 mRNA. Translation: AAH58392.1.
CCDSiCCDS29261.1.
PIRiS07720.
RefSeqiNP_034851.2. NM_010721.2.
UniGeneiMm.4105.

3D structure databases

ProteinModelPortaliP14733.
SMRiP14733. Positions 312-386, 432-549.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201177. 6 interactions.
IntActiP14733. 8 interactions.
MINTiMINT-1726964.
STRINGi10090.ENSMUSP00000025486.

PTM databases

iPTMnetiP14733.
PhosphoSiteiP14733.

2D gel databases

REPRODUCTION-2DPAGEIPI00230394.
SWISS-2DPAGEP14733.

Proteomic databases

EPDiP14733.
MaxQBiP14733.
PaxDbiP14733.
PRIDEiP14733.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025486; ENSMUSP00000025486; ENSMUSG00000024590.
GeneIDi16906.
KEGGimmu:16906.
UCSCiuc012bdd.2. mouse.

Organism-specific databases

CTDi4001.
MGIiMGI:96795. Lmnb1.

Phylogenomic databases

eggNOGiKOG0977. Eukaryota.
ENOG410Y2H6. LUCA.
GeneTreeiENSGT00830000128282.
HOGENOMiHOG000007711.
HOVERGENiHBG013015.
InParanoidiP14733.
KOiK07611.
OMAiEMNTSSV.
OrthoDBiEOG7MD4PW.
PhylomeDBiP14733.
TreeFamiTF101181.

Enzyme and pathway databases

ReactomeiR-MMU-1221632. Meiotic synapsis.
R-MMU-1221633. Meiotic Synapsis.
R-MMU-2559584. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
R-MMU-352238. Breakdown of the nuclear lamina.

Miscellaneous databases

ChiTaRSiLmnb1. mouse.
PROiP14733.
SOURCEiSearch...

Gene expression databases

BgeeiP14733.
CleanExiMM_LMNB1.
GenevisibleiP14733. MM.

Family and domain databases

Gene3Di2.60.40.1260. 1 hit.
InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR027696. Lamin_B.
IPR001322. Lamin_tail_dom.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF157. PTHR23239:SF157. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF00932. LTD. 1 hit.
[Graphical view]
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
SUPFAMiSSF74853. SSF74853. 1 hit.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Amino acid sequence and molecular characterization of murine lamin B as deduced from cDNA clones."
    Hoeger T.H., Krohne G., Franke W.W.
    Eur. J. Cell Biol. 47:283-290(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Liver.
  2. Hoeger T.H.
    Submitted (OCT-1989) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Genomic structure of the mouse gene (Lmnb1) encoding nuclear lamin B1."
    Maeno H., Sugimoto K., Nakajima N.
    Genomics 30:342-346(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: C3H/He.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND THR-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Lung, Spleen and Testis.
  8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-112; LYS-272 AND LYS-331, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiLMNB1_MOUSE
AccessioniPrimary (citable) accession number: P14733
Secondary accession number(s): Q61791
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 165 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.