P20700 · LMNB1_HUMAN
- ProteinLamin-B1
- GeneLMNB1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids586 (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:28716252, PubMed:32910914).
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:28716252, PubMed:32910914).
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:28716252, PubMed:32910914).
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:28716252, PubMed:32910914).
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:28716252, PubMed:32910914).
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 | membrane | |
Cellular Component | nuclear envelope | |
Cellular Component | nuclear inner membrane | |
Cellular Component | nuclear lamina | |
Cellular Component | nuclear matrix | |
Cellular Component | nuclear membrane | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | phospholipase binding | |
Molecular Function | sequence-specific double-stranded DNA binding | |
Molecular Function | structural constituent of cytoskeleton | |
Molecular Function | structural constituent of nuclear lamina | |
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 |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLamin-B1
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP20700
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Leukodystrophy, demyelinating, autosomal dominant, adult-onset (ADLD)
- Note
- DescriptionA slowly progressive and fatal demyelinating leukodystrophy, presenting in the fourth or fifth decade of life. Clinically characterized by early autonomic abnormalities, pyramidal and cerebellar dysfunction, and symmetric demyelination of the CNS. It differs from multiple sclerosis and other demyelinating disorders in that neuropathology shows preservation of oligodendroglia in the presence of subtotal demyelination and lack of astrogliosis.
- See alsoMIM:169500
Natural variants in ADLD
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_085497 | 29 | R>W | in ADLD; uncertain significance; no effect on localization to nuclear lamina; dbSNP:rs1295707923 |
Microcephaly 26, primary, autosomal dominant (MCPH26)
- Note
- DescriptionA form of microcephaly, a disease defined as a head circumference more than 3 standard deviations below the age, sex and ethnically matched mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. MCPH26 is an autosomal dominant, progressive form apparent at birth or in early infancy. It is associated with relative short stature, variable severity of intellectual disability, and neurological features as the core symptoms. Brain imaging shows a simplified gyral pattern of the cortex and abnormal corpus callosum in some patients.
- See alsoMIM:619179
Natural variants in MCPH26
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_085498 | 33 | K>E | in MCPH26; decreased localization to nuclear lamina; increased aggregation; changed nuclear envelope organization; dbSNP:rs1750497172 | |
VAR_085500 | 33 | missing | in MCPH26; increased aggregation; changed nuclear envelope organization | |
VAR_085501 | 42 | R>W | in MCPH26; decreased localization to nuclear lamina; changed nuclear envelope organization; increased aggregation; dbSNP:rs1245844735 | |
VAR_085502 | 90 | R>P | in MCPH26; increased aggregation; changed nuclear envelope organization; dbSNP:rs1750506249 | |
VAR_085503 | 152 | A>G | in MCPH26; decreased protein abundance; changed localization to nuclear lamina; changed nuclear envelope organization; dbSNP:rs935132421 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_085497 | 29 | in ADLD; uncertain significance; no effect on localization to nuclear lamina; dbSNP:rs1295707923 | |||
Sequence: R → W | ||||||
Natural variant | VAR_085498 | 33 | in MCPH26; decreased localization to nuclear lamina; increased aggregation; changed nuclear envelope organization; dbSNP:rs1750497172 | |||
Sequence: K → E | ||||||
Natural variant | VAR_085499 | 33 | no effect on localization to nuclear lamina; dbSNP:rs1303994586 | |||
Sequence: K → T | ||||||
Natural variant | VAR_085500 | 33 | in MCPH26; increased aggregation; changed nuclear envelope organization | |||
Sequence: Missing | ||||||
Natural variant | VAR_085501 | 42 | in MCPH26; decreased localization to nuclear lamina; changed nuclear envelope organization; increased aggregation; dbSNP:rs1245844735 | |||
Sequence: R → W | ||||||
Natural variant | VAR_085502 | 90 | in MCPH26; increased aggregation; changed nuclear envelope organization; dbSNP:rs1750506249 | |||
Sequence: R → P | ||||||
Natural variant | VAR_085503 | 152 | in MCPH26; decreased protein abundance; changed localization to nuclear lamina; changed nuclear envelope organization; dbSNP:rs935132421 | |||
Sequence: A → G | ||||||
Natural variant | VAR_071077 | 436 | found in a family with amyotrophic lateral sclerosis carrying a probable causative mutation in MATR3; uncertain significance; dbSNP:rs1380634377 | |||
Sequence: A → V | ||||||
Natural variant | VAR_031646 | 501 | in dbSNP:rs36105360 | |||
Sequence: A → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 581 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data), cross-link, disulfide bond, glycosylation, lipidation, propeptide.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000063816 | 2-583 | UniProt | Lamin-B1 | |||
Sequence: ATATPVPPRMGSRAGGPTTPLSPTRLSRLQEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELGKCKAEHDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLEFRKSMYEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDLLAKEKDNSRRMLTDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEEERLKLSPSPSSRVTVSRASSSRSVRTTRGKRKRVDVEESEASSSVSISHSASATGNVCIEEIDVDGKFIRLKNTSEQDQPMGGWEMIRKIGDTSVSYKYTSRYVLKAGQTVTIWAANAGVTASPPTDLIWKNQNSWGTGEDVKVILKNSQGEEVAQRSTVFKTTIPEEEEEEEEAAGVVVEEELFHQQGTPRASNRSC | |||||||
Modified residue | 3 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 5 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 5 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 13 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 14 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 19 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 20 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 20 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 23 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 23 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 25 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 25 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 28 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 28 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 52 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 58 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 102 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 111 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Cross-link | 123 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 126 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 145 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 157 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 157 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 158 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 158 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 181 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 200 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 200 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 210 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 210 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 232 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 232 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 241 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 261 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 271 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 271 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 278 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 278 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 279 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 283 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 284 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 288 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 302 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 302 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 304 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 305 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 308 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 312 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Disulfide bond | 317 | UniProt | Interchain | ||||
Sequence: C | |||||||
Modified residue | 330 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 330 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 375 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 375 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 391 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 393 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 393 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 395 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 396 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 399 | UniProt | O-linked (GlcNAc) threonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 399 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 401 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 404 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 405 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 406 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 408 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 413 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 483 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Cross-link | 532 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 534 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 534 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 547 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 549 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 575 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 575 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 583 | UniProt | Cysteine methyl ester | ||||
Sequence: C | |||||||
Lipidation | 583 | UniProt | S-farnesyl cysteine | ||||
Sequence: C | |||||||
Propeptide | PRO_0000393945 | 584-586 | UniProt | 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. Phosphorylation by CDK1 at Ser-23 and Ser-393 at the onset of mitosis drives lamin disassembly and nuclear envelope breakdown.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Homodimer (PubMed:22265972, PubMed:33706103).
Lamin dimers then assemble into dimeric head-to-tail polymers. Ultimately, two head-to-tail polymers assemble laterally into a protofilament with a uniformly shaped rod of 3.5 nm in diameter (By similarity).
Interacts with SPAG4 and SEPT12 (PubMed:25775403).
Lamin dimers then assemble into dimeric head-to-tail polymers. Ultimately, two head-to-tail polymers assemble laterally into a protofilament with a uniformly shaped rod of 3.5 nm in diameter (By similarity).
Interacts with SPAG4 and SEPT12 (PubMed:25775403).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P20700 | CCDC88B A6NC98 | 3 | EBI-968218, EBI-347573 | |
BINARY | P20700 | CENPH Q9H3R5 | 3 | EBI-968218, EBI-1003700 | |
BINARY | P20700 | DMAP1 Q9NPF5 | 3 | EBI-968218, EBI-399105 | |
BINARY | P20700 | FAM169A Q9Y6X4 | 3 | EBI-968218, EBI-1220497 | |
BINARY | P20700 | KPNA1 P52294 | 5 | EBI-968218, EBI-358383 | |
BINARY | P20700 | KPNA5 O15131 | 3 | EBI-968218, EBI-540602 | |
BINARY | P20700 | KPNA6 O60684 | 4 | EBI-968218, EBI-359923 | |
BINARY | P20700 | LMNA P02545 | 23 | EBI-968218, EBI-351935 | |
BINARY | P20700 | LMNA P02545-1 | 5 | EBI-968218, EBI-351949 | |
BINARY | P20700 | LMNA P02545-2 | 19 | EBI-968218, EBI-351953 | |
BINARY | P20700 | LMNB2 Q03252 | 8 | EBI-968218, EBI-2830427 | |
BINARY | P20700 | M1AP Q8TC57 | 3 | EBI-968218, EBI-748182 | |
BINARY | P20700 | MAP1LC3B Q9GZQ8 | 14 | EBI-968218, EBI-373144 | |
BINARY | P20700 | PIH1D2 Q8WWB5 | 3 | EBI-968218, EBI-10232538 | |
BINARY | P20700 | PPP1R13B Q96KQ4 | 3 | EBI-968218, EBI-1105153 | |
BINARY | P20700 | SNAPIN O95295 | 3 | EBI-968218, EBI-296723 | |
BINARY | P20700 | TP53BP2 Q05BL1 | 3 | EBI-968218, EBI-11952721 | |
BINARY | P20700 | UBE2I Q7KZS0 | 3 | EBI-968218, EBI-10180829 | |
XENO | P20700 | VP24 Q05322 | 6 | EBI-968218, EBI-6153153 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-31 | Disordered | ||||
Sequence: MATATPVPPRMGSRAGGPTTPLSPTRLSRLQ | ||||||
Region | 2-34 | Head | ||||
Sequence: ATATPVPPRMGSRAGGPTTPLSPTRLSRLQEKE | ||||||
Domain | 32-388 | IF rod | ||||
Sequence: EKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELGKCKAEHDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLEFRKSMYEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDLLAKEKDNSRRMLTDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEEERL | ||||||
Region | 35-69 | Coil 1A | ||||
Sequence: ELRELNDRLAVYIDKVRSLETENSALQLQVTEREE | ||||||
Region | 70-81 | Linker 1 | ||||
Sequence: VRGRELTGLKAL | ||||||
Region | 82-215 | Coil 1B | ||||
Sequence: YETELADARRALDDTARERAKLQIELGKCKAEHDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLEFRKSMYEEE | ||||||
Region | 216-243 | Linker 2 | ||||
Sequence: INETRRKHETRLVEVDSGRQIEYEYKLA | ||||||
Region | 244-386 | Coil 2 | ||||
Sequence: QALHEMREQHDAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDLLAKEKDNSRRMLTDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEEE | ||||||
Region | 387-586 | Tail | ||||
Sequence: RLKLSPSPSSRVTVSRASSSRSVRTTRGKRKRVDVEESEASSSVSISHSASATGNVCIEEIDVDGKFIRLKNTSEQDQPMGGWEMIRKIGDTSVSYKYTSRYVLKAGQTVTIWAANAGVTASPPTDLIWKNQNSWGTGEDVKVILKNSQGEEVAQRSTVFKTTIPEEEEEEEEAAGVVVEEELFHQQGTPRASNRSCAIM | ||||||
Region | 388-432 | Disordered | ||||
Sequence: LKLSPSPSSRVTVSRASSSRSVRTTRGKRKRVDVEESEASSSVSI | ||||||
Compositional bias | 392-408 | Polar residues | ||||
Sequence: PSPSSRVTVSRASSSRS | ||||||
Motif | 415-420 | Nuclear localization signal | ||||
Sequence: KRKRVD | ||||||
Domain | 430-546 | LTD | ||||
Sequence: VSISHSASATGNVCIEEIDVDGKFIRLKNTSEQDQPMGGWEMIRKIGDTSVSYKYTSRYVLKAGQTVTIWAANAGVTASPPTDLIWKNQNSWGTGEDVKVILKNSQGEEVAQRSTVF |
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.
- Length586
- Mass (Da)66,408
- Last updated2007-01-23 v2
- Checksum73292877745722C4
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E9PBF6 | E9PBF6_HUMAN | LMNB1 | 387 | ||
A0A0D9SFY5 | A0A0D9SFY5_HUMAN | LMNB1 | 166 | ||
A0A0D9SFE5 | A0A0D9SFE5_HUMAN | LMNB1 | 329 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 382 | in Ref. 5; AAH12295 | ||||
Sequence: E → Q | ||||||
Compositional bias | 392-408 | Polar residues | ||||
Sequence: PSPSSRVTVSRASSSRS |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M34458 EMBL· GenBank· DDBJ | AAA36162.1 EMBL· GenBank· DDBJ | mRNA | ||
L37747 EMBL· GenBank· DDBJ | AAC37575.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L37737 EMBL· GenBank· DDBJ | AAC37575.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L37738 EMBL· GenBank· DDBJ | AAC37575.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L37739 EMBL· GenBank· DDBJ | AAC37575.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L37740 EMBL· GenBank· DDBJ | AAC37575.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L37741 EMBL· GenBank· DDBJ | AAC37575.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L37742 EMBL· GenBank· DDBJ | AAC37575.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L37743 EMBL· GenBank· DDBJ | AAC37575.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L37744 EMBL· GenBank· DDBJ | AAC37575.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L37745 EMBL· GenBank· DDBJ | AAC37575.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L37746 EMBL· GenBank· DDBJ | AAC37575.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK312603 EMBL· GenBank· DDBJ | BAG35493.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471086 EMBL· GenBank· DDBJ | EAW48846.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC012295 EMBL· GenBank· DDBJ | AAH12295.1 EMBL· GenBank· DDBJ | mRNA | ||
BC103723 EMBL· GenBank· DDBJ | AAI03724.1 EMBL· GenBank· DDBJ | mRNA |