P14733 · LMNB1_MOUSE

  • Protein
    Lamin-B1
  • Gene
    Lmnb1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:28241138).
Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed:28241138).
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 (PubMed:28241138).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentlamin filament
Cellular Componentnuclear envelope
Cellular Componentnuclear inner membrane
Cellular Componentnuclear lamina
Cellular Componentnuclear matrix
Cellular Componentnuclear membrane
Cellular Componentnuclear periphery
Cellular Componentnucleoplasm
Cellular Componentnucleus
Molecular Functiondouble-stranded DNA binding
Molecular FunctionJUN kinase binding
Molecular Functionphospholipase binding
Molecular Functionsequence-specific double-stranded DNA binding
Molecular Functionstructural constituent of cytoskeleton
Molecular Functionstructural constituent of nuclear lamina
Biological Processcellular response to L-glutamate
Biological Processheterochromatin formation
Biological Processnuclear envelope organization
Biological Processnuclear migration
Biological Processnuclear pore localization
Biological Processpositive regulation of G2/M transition of mitotic cell cycle
Biological Processpositive regulation of JNK cascade
Biological Processprotein localization to nuclear envelope

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Lamin-B1

Gene names

    • Name
      Lmnb1

Organism names

  • Taxonomic identifier
  • Strains
    • C3H/He
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P14733
  • Secondary accessions
    • Q61791

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain, cross-link, disulfide bond, glycosylation, lipidation, propeptide.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylalanine
ChainPRO_00000638172-585Lamin-B1
Modified residue3Phosphothreonine
Modified residue5Phosphothreonine
Modified residue15Omega-N-methylarginine
Modified residue17Phosphoserine
Modified residue21Phosphothreonine
Modified residue24Phosphoserine
Modified residue26Phosphothreonine
Modified residue29Phosphoserine
Cross-link103Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue112N6-acetyllysine
Cross-link124Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue127Phosphoserine
Cross-link146Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue158N6-acetyllysine; alternate
Cross-link158Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Modified residue159Phosphoserine
Cross-link182Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue201Phosphoserine
Modified residue233Phosphoserine
Cross-link242Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link262Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue272N6-acetyllysine; alternate
Cross-link272Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Modified residue279Phosphoserine
Modified residue303Phosphoserine
Cross-link313Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Disulfide bond318Interchain
Modified residue331N6-acetyllysine; alternate
Cross-link331Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Modified residue376Phosphoserine
Modified residue394Phosphoserine
Glycosylation400O-linked (GlcNAc) threonine
Modified residue414Omega-N-methylarginine
Modified residue484N6-acetyllysine
Cross-link533Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue535Phosphoserine
Cross-link548Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue585Cysteine methyl ester
Lipidation585S-farnesyl cysteine
PropeptidePRO_0000403467586-588Removed in mature form

Post-translational modification

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.
Phosphorylation plays a key role in lamin organization, subcellular localization and nuclear envelope disintegration (By similarity).
Phosphorylation by CDK1 at Ser-24 and Ser-394 at the onset of mitosis drives lamin disassembly and nuclear envelope breakdown (By similarity).

Keywords

Proteomic databases

2D gel databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Homodimer (PubMed:28241138).
Lamin dimers then assemble into dimeric head-to-tail polymers (PubMed:28241138).
Ultimately, two head-to-tail polymers assemble laterally into a protofilament with a uniformly shaped rod of 3.5 nm in diameter (PubMed:28241138).
Interacts with SPAG4 and SEPT12 (By similarity).

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for compositional bias, region, domain, motif.

TypeIDPosition(s)Description
Compositional bias1-28Polar residues
Region1-34Disordered
Region2-35Head
Domain33-389IF rod
Region36-70Coil 1A
Region71-82Linker 1
Region83-216Coil 1B
Region217-244Linker 2
Region245-387Coil 2
Region388-588Tail
Region391-433Disordered
Compositional bias393-409Polar residues
Motif416-421Nuclear localization signal
Domain431-547LTD

Sequence similarities

Belongs to the intermediate filament family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    588
  • Mass (Da)
    66,786
  • Last updated
    2007-01-23 v3
  • Checksum
    3602BCE63588A32D
MATATPVQQQRAGSRASAPATPLSPTRLSRLQEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELGKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLADETLLKVDLENRCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDMLAKERDNSRRMLSDREREMAEIRDQMQQQLSDYEQLLDVKLALDMEISAYRKLLEGEEERLKLSPSPSSRVTVSRASSSRSVRTTRGKRKRVDVEESEASSSVSISHSASATGNVCIEEIDVDGKFIRLKNTSEQDQPMGGWEMIRKIGDTSVSYKYTSRYVLKAGQTVTVWAANAGVTASPPTDLIWKNQNSWGTGEDVKVILKNSQGEEVAQRSTVFKTTIPEEEEEEEEEPIGVAVEEERFHQQGAPRASNKSCAIM

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias1-28Polar residues
Compositional bias393-409Polar residues
Sequence conflict581in Ref. 1; CAA34677/AAC96023

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X16705
EMBL· GenBank· DDBJ
CAA34677.1
EMBL· GenBank· DDBJ
mRNA
M35153
EMBL· GenBank· DDBJ
AAC96023.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.
D50080
EMBL· GenBank· DDBJ
BAA08784.1
EMBL· GenBank· DDBJ
Genomic DNA
BC052729
EMBL· GenBank· DDBJ
AAH52729.1
EMBL· GenBank· DDBJ
mRNA
BC058392
EMBL· GenBank· DDBJ
AAH58392.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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