P14733 · LMNB1_MOUSE
- ProteinLamin-B1
- GeneLmnb1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids588 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLamin-B1
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP14733
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, cross-link, disulfide bond, glycosylation, lipidation, propeptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000063817 | 2-585 | Lamin-B1 | |||
Sequence: ATATPVQQQRAGSRASAPATPLSPTRLSRLQEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELGKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLADETLLKVDLENRCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDMLAKERDNSRRMLSDREREMAEIRDQMQQQLSDYEQLLDVKLALDMEISAYRKLLEGEEERLKLSPSPSSRVTVSRASSSRSVRTTRGKRKRVDVEESEASSSVSISHSASATGNVCIEEIDVDGKFIRLKNTSEQDQPMGGWEMIRKIGDTSVSYKYTSRYVLKAGQTVTVWAANAGVTASPPTDLIWKNQNSWGTGEDVKVILKNSQGEEVAQRSTVFKTTIPEEEEEEEEEPIGVAVEEERFHQQGAPRASNKSC | ||||||
Modified residue | 3 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 5 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 15 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 17 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 21 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 24 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 26 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 29 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 103 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 112 | N6-acetyllysine | ||||
Sequence: K | ||||||
Cross-link | 124 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 127 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 146 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 158 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Cross-link | 158 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | ||||||
Modified residue | 159 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 182 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 201 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 233 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 242 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 262 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 272 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Cross-link | 272 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | ||||||
Modified residue | 279 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 303 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 313 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Disulfide bond | 318 | Interchain | ||||
Sequence: C | ||||||
Modified residue | 331 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Cross-link | 331 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | ||||||
Modified residue | 376 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 394 | Phosphoserine | ||||
Sequence: S | ||||||
Glycosylation | 400 | O-linked (GlcNAc) threonine | ||||
Sequence: T | ||||||
Modified residue | 414 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 484 | N6-acetyllysine | ||||
Sequence: K | ||||||
Cross-link | 533 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 535 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 548 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 585 | Cysteine methyl ester | ||||
Sequence: C | ||||||
Lipidation | 585 | S-farnesyl cysteine | ||||
Sequence: C | ||||||
Propeptide | PRO_0000403467 | 586-588 | Removed in mature form | |||
Sequence: AIM |
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).
Phosphorylation by CDK1 at Ser-24 and Ser-394 at the onset of mitosis drives lamin disassembly and nuclear envelope breakdown (By similarity).
Keywords
- PTM
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).
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
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-28 | Polar residues | ||||
Sequence: MATATPVQQQRAGSRASAPATPLSPTRL | ||||||
Region | 1-34 | Disordered | ||||
Sequence: MATATPVQQQRAGSRASAPATPLSPTRLSRLQEK | ||||||
Region | 2-35 | Head | ||||
Sequence: ATATPVQQQRAGSRASAPATPLSPTRLSRLQEKE | ||||||
Domain | 33-389 | IF rod | ||||
Sequence: EKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELGKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLADETLLKVDLENRCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDMLAKERDNSRRMLSDREREMAEIRDQMQQQLSDYEQLLDVKLALDMEISAYRKLLEGEEERL | ||||||
Region | 36-70 | Coil 1A | ||||
Sequence: ELRELNDRLAVYIDKVRSLETENSALQLQVTEREE | ||||||
Region | 71-82 | Linker 1 | ||||
Sequence: VRGRELTGLKAL | ||||||
Region | 83-216 | Coil 1B | ||||
Sequence: YETELADARRALDDTARERAKLQIELGKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLADETLLKVDLENRCQSLTEDLEFRKNMYEEE | ||||||
Region | 217-244 | Linker 2 | ||||
Sequence: INETRRKHETRLVEVDSGRQIEYEYKLA | ||||||
Region | 245-387 | Coil 2 | ||||
Sequence: QALHEMREQHDAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDMLAKERDNSRRMLSDREREMAEIRDQMQQQLSDYEQLLDVKLALDMEISAYRKLLEGEEE | ||||||
Region | 388-588 | Tail | ||||
Sequence: RLKLSPSPSSRVTVSRASSSRSVRTTRGKRKRVDVEESEASSSVSISHSASATGNVCIEEIDVDGKFIRLKNTSEQDQPMGGWEMIRKIGDTSVSYKYTSRYVLKAGQTVTVWAANAGVTASPPTDLIWKNQNSWGTGEDVKVILKNSQGEEVAQRSTVFKTTIPEEEEEEEEEPIGVAVEEERFHQQGAPRASNKSCAIM | ||||||
Region | 391-433 | Disordered | ||||
Sequence: LSPSPSSRVTVSRASSSRSVRTTRGKRKRVDVEESEASSSVSI | ||||||
Compositional bias | 393-409 | Polar residues | ||||
Sequence: PSPSSRVTVSRASSSRS | ||||||
Motif | 416-421 | Nuclear localization signal | ||||
Sequence: KRKRVD | ||||||
Domain | 431-547 | LTD | ||||
Sequence: VSISHSASATGNVCIEEIDVDGKFIRLKNTSEQDQPMGGWEMIRKIGDTSVSYKYTSRYVLKAGQTVTVWAANAGVTASPPTDLIWKNQNSWGTGEDVKVILKNSQGEEVAQRSTVF |
Sequence similarities
Belongs to the intermediate filament family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length588
- Mass (Da)66,786
- Last updated2007-01-23 v3
- Checksum3602BCE63588A32D
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-28 | Polar residues | ||||
Sequence: MATATPVQQQRAGSRASAPATPLSPTRL | ||||||
Compositional bias | 393-409 | Polar residues | ||||
Sequence: PSPSSRVTVSRASSSRS | ||||||
Sequence conflict | 581 | in Ref. 1; CAA34677/AAC96023 | ||||
Sequence: S → W |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |