P21619 · LMNB2_MOUSE
- ProteinLamin-B2
- GeneLmnb2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids596 (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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Aspect | Term | |
---|---|---|
Cellular Component | lamin filament | |
Cellular Component | nuclear envelope | |
Cellular Component | nuclear lamina | |
Cellular Component | nuclear periphery | |
Cellular Component | nucleus | |
Molecular Function | structural constituent of cytoskeleton | |
Biological Process | heterochromatin formation | |
Biological Process | nuclear envelope organization | |
Biological Process | nuclear migration | |
Biological Process | nuclear pore localization | |
Biological Process | protein localization to nuclear envelope |
Names & Taxonomy
Protein names
- Recommended nameLamin-B2
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 accessionP21619
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue, cross-link, glycosylation, lipidation, propeptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000063821 | 1-593 | Lamin-B2 | |||
Sequence: MASLPPHAGPATPLSPTRLSRLQEKEELRELNDRLAHYIDRVRALELENDRLLLRISEKEEVTTREVSGIKTLYESELADARRVLDETARERARLQIEIGKVQAELEEARKSAKKREGELTVAQGRVKDLESLFHRSEAELATALSDKQGLETEVAELRAQLAKAEDGHAVAKKQLEKETLMRVDLENRCQSLQEELAFSKSVFEEEVRETRRRHERRLVEVDSSRQQEYDFKMAQALEDLRSQHDEQVRLYRVELEQTYQAKLDNAKLLSDQNDKAAHAAREELKEARMRVESLSYQLLGLQKQASAAENHIHELEEALAGERDKFRKMLDAKEQEMTEVRDAMQQQLAEYQELLDIKLALDMEISAYRKLLEGEEERLKLSPSPSSRITISRATSSSSSSSGVGMSVGQGRGKRRRLETEDTSGSPSRASRVSSGSRLAQQTVATGVVNIDEVDPEGRFVRLKNSSDKDQSLGNWRIKRQVLEGEDIAYKFTPKYVLRAGQTVTVWAAGAGATHSPPSTLVWKSQTNWGPGESFRTALVSADGEEVAVKAAKHSSVQGRENGEEEEEEEAEFGEEDLFHQQGDPRTTSRGC | ||||||
Modified residue | 12 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 15 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 59 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Cross-link | 59 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | ||||||
Cross-link | 173 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 233 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 294 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 385 | Phosphoserine | ||||
Sequence: S | ||||||
Glycosylation | 391 | O-linked (GlcNAc) threonine | ||||
Sequence: T | ||||||
Modified residue | 398 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 400 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 402 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 413 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Cross-link | 465 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 473 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 593 | Cysteine methyl ester | ||||
Sequence: C | ||||||
Lipidation | 593 | S-farnesyl cysteine | ||||
Sequence: C | ||||||
Propeptide | PRO_0000403471 | 594-596 | Removed in mature form | |||
Sequence: RLM |
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-15 and Ser-385 at the onset of mitosis drives lamin disassembly and nuclear envelope breakdown (By similarity).
Phosphorylation by CDK1 at Ser-15 and Ser-385 at the onset of mitosis drives lamin disassembly and nuclear envelope breakdown (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Dimer (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 TMEM43 (PubMed:18230648).
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 TMEM43 (PubMed:18230648).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-20 | Disordered | ||||
Sequence: MASLPPHAGPATPLSPTRLS | ||||||
Region | 1-26 | Head | ||||
Sequence: MASLPPHAGPATPLSPTRLSRLQEKE | ||||||
Domain | 24-380 | IF rod | ||||
Sequence: EKEELRELNDRLAHYIDRVRALELENDRLLLRISEKEEVTTREVSGIKTLYESELADARRVLDETARERARLQIEIGKVQAELEEARKSAKKREGELTVAQGRVKDLESLFHRSEAELATALSDKQGLETEVAELRAQLAKAEDGHAVAKKQLEKETLMRVDLENRCQSLQEELAFSKSVFEEEVRETRRRHERRLVEVDSSRQQEYDFKMAQALEDLRSQHDEQVRLYRVELEQTYQAKLDNAKLLSDQNDKAAHAAREELKEARMRVESLSYQLLGLQKQASAAENHIHELEEALAGERDKFRKMLDAKEQEMTEVRDAMQQQLAEYQELLDIKLALDMEISAYRKLLEGEEERL | ||||||
Region | 27-61 | Coil 1A | ||||
Sequence: ELRELNDRLAHYIDRVRALELENDRLLLRISEKEE | ||||||
Region | 62-73 | Linker 1 | ||||
Sequence: VTTREVSGIKTL | ||||||
Region | 74-207 | Coil 1B | ||||
Sequence: YESELADARRVLDETARERARLQIEIGKVQAELEEARKSAKKREGELTVAQGRVKDLESLFHRSEAELATALSDKQGLETEVAELRAQLAKAEDGHAVAKKQLEKETLMRVDLENRCQSLQEELAFSKSVFEEE | ||||||
Region | 208-234 | Linker 2 | ||||
Sequence: VRETRRRHERRLVEVDSSRQQEYDFKM | ||||||
Region | 235-378 | Coil 2 | ||||
Sequence: AQALEDLRSQHDEQVRLYRVELEQTYQAKLDNAKLLSDQNDKAAHAAREELKEARMRVESLSYQLLGLQKQASAAENHIHELEEALAGERDKFRKMLDAKEQEMTEVRDAMQQQLAEYQELLDIKLALDMEISAYRKLLEGEEE | ||||||
Region | 376-440 | Disordered | ||||
Sequence: EEERLKLSPSPSSRITISRATSSSSSSSGVGMSVGQGRGKRRRLETEDTSGSPSRASRVSSGSRL | ||||||
Region | 379-596 | Tail | ||||
Sequence: RLKLSPSPSSRITISRATSSSSSSSGVGMSVGQGRGKRRRLETEDTSGSPSRASRVSSGSRLAQQTVATGVVNIDEVDPEGRFVRLKNSSDKDQSLGNWRIKRQVLEGEDIAYKFTPKYVLRAGQTVTVWAAGAGATHSPPSTLVWKSQTNWGPGESFRTALVSADGEEVAVKAAKHSSVQGRENGEEEEEEEAEFGEEDLFHQQGDPRTTSRGCRLM | ||||||
Compositional bias | 384-408 | Polar residues | ||||
Sequence: PSPSSRITISRATSSSSSSSGVGMS | ||||||
Motif | 415-420 | Nuclear localization signal | ||||
Sequence: KRRRLE | ||||||
Compositional bias | 425-440 | Polar residues | ||||
Sequence: SGSPSRASRVSSGSRL | ||||||
Domain | 438-559 | LTD | ||||
Sequence: SRLAQQTVATGVVNIDEVDPEGRFVRLKNSSDKDQSLGNWRIKRQVLEGEDIAYKFTPKYVLRAGQTVTVWAAGAGATHSPPSTLVWKSQTNWGPGESFRTALVSADGEEVAVKAAKHSSVQ | ||||||
Region | 552-596 | Disordered | ||||
Sequence: AAKHSSVQGRENGEEEEEEEAEFGEEDLFHQQGDPRTTSRGCRLM |
Sequence similarities
Belongs to the intermediate filament family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
P21619-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NameB2
- Length596
- Mass (Da)67,318
- Last updated2006-01-24 v2
- Checksum4FEF5A76FFDF2D96
P21619-2
- NameB3
- Differences from canonical
- 1-206: MASLPPHAGPATPLSPTRLSRLQEKEELRELNDRLAHYIDRVRALELENDRLLLRISEKEEVTTREVSGIKTLYESELADARRVLDETARERARLQIEIGKVQAELEEARKSAKKREGELTVAQGRVKDLESLFHRSEAELATALSDKQGLETEVAELRAQLAKAEDGHAVAKKQLEKETLMRVDLENRCQSLQEELAFSKSVFEE → MGESESMRGTGEGCGRDCPEAARPLMETVEGALPELRGRPLREYVKRRPRGLGKTPVEDPVKSEGAVGYPRTWNNHLRVPTREQ
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0R4J0Q5 | A0A0R4J0Q5_MOUSE | Lmnb2 | 615 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_017070 | 1-206 | in isoform B3 | |||
Sequence: MASLPPHAGPATPLSPTRLSRLQEKEELRELNDRLAHYIDRVRALELENDRLLLRISEKEEVTTREVSGIKTLYESELADARRVLDETARERARLQIEIGKVQAELEEARKSAKKREGELTVAQGRVKDLESLFHRSEAELATALSDKQGLETEVAELRAQLAKAEDGHAVAKKQLEKETLMRVDLENRCQSLQEELAFSKSVFEE → MGESESMRGTGEGCGRDCPEAARPLMETVEGALPELRGRPLREYVKRRPRGLGKTPVEDPVKSEGAVGYPRTWNNHLRVPTREQ | ||||||
Sequence conflict | 148-149 | in Ref. 1; CAA38032 | ||||
Sequence: KQ → NE | ||||||
Sequence conflict | 314 | in Ref. 6; AA sequence | ||||
Sequence: H → R | ||||||
Sequence conflict | 321 | in Ref. 1; CAA38032 | ||||
Sequence: A → R | ||||||
Sequence conflict | 344 | in Ref. 1; CAA38032 | ||||
Sequence: A → R | ||||||
Compositional bias | 384-408 | Polar residues | ||||
Sequence: PSPSSRITISRATSSSSSSSGVGMS | ||||||
Sequence conflict | 403 | in Ref. 1; CAA38032 | ||||
Sequence: Missing | ||||||
Sequence conflict | 412-413 | in Ref. 1; CAA38032 | ||||
Sequence: GR → RG | ||||||
Sequence conflict | 421-422 | in Ref. 1 | ||||
Sequence: Missing | ||||||
Compositional bias | 425-440 | Polar residues | ||||
Sequence: SGSPSRASRVSSGSRL | ||||||
Sequence conflict | 443 | in Ref. 1; CAA38032 | ||||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X54098 EMBL· GenBank· DDBJ | CAA38032.1 EMBL· GenBank· DDBJ | mRNA | ||
D13455 EMBL· GenBank· DDBJ | BAA02708.1 EMBL· GenBank· DDBJ | mRNA | ||
BC042430 EMBL· GenBank· DDBJ | AAH42430.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC051985 EMBL· GenBank· DDBJ | AAH51985.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |