LMNB1
entrez
4001
canonical
uniprot
P20700
canonical
ensembl
ENSG00000113368
resolver
ensp
ENSP00000261366
resolver
enst
ENST00000261366
resolver
genesymbol
LMNB1
resolver
genesymbol_syn
LMN2
resolver
genesymbol_syn
LMNB
resolver
hgnc
HGNC:6637
resolver
uniprot
B2R6J6
resolver
uniprot
B4DZT3
resolver
uniprot
Q3SYN7
resolver
uniprot
Q96EI6
resolver
uniprot_entry
B4DZT3_HUMAN
resolver
uniprot_entry
LMNB1_HUMAN
resolver
uniprot_sec
B2R6J6
resolver
uniprot_sec
Q3SYN7
resolver
uniprot_sec
Q96EI6
resolver
amino_acid_sequence
MATATPVPPRMGSRAGGPTTPLSPTRLSRLQEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELGKCKAEHDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLEFRKSMYEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDLLAKEKDNSRRMLTDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEEERLKLSPSPSSRVTVSRASSSRSVRTTRGKRKRVDVEESEASSSVSISHSASATGNVCIEEIDVDGKFIRLKNTSEQDQPMGGWEMIRKIGDTSVSYKYTSRYVLKAGQTVTIWAANAGVTASPPTDLIWKNQNSWGTGEDVKVILKNSQGEEVAQRSTVFKTTIPEEEEEEEEAAGVVVEEELFHQQGTPRASNRSCAIM
uniprot
proteins
disease_involvement
DISEASE: Leukodystrophy, demyelinating, adult-onset, autosomal dominant, typical (ADLDTY) [MIM:169500]: A 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. {ECO:0000269|PubMed:16951681, ECO:0000269|PubMed:28716252, ECO:0000269|PubMed:32910914}. Note=The disease is caused by variants affecting the gene represented in this entry. The disease is caused by heterozygous tandem genomic duplications that result in an extra copy of the LMNB1 gene and also affect regulatory elements of other genes. {ECO:0000269|PubMed:16951681, ECO:0000269|PubMed:39078102}.; DISEASE: Leukodystrophy, demyelinating, adult-onset, autosomal dominant, atypical (ADLDAT) [MIM:621061]: An autosomal dominant, slowly progressive disorder characterized by pyramidal signs with muscle weakness, spasticity, dysarthria, dysautonomia, and demyelinating leukodystrophy affecting the cerebrum and cortico-spinal tracts while sparing the cerebellum. Patients usually do not present with autonomic symptoms. {ECO:0000269|PubMed:39078102}. Note=The disease is caused by variants affecting the gene represented in this entry. The disease is caused by abnormal LMNB1 expression due to heterozygous deletions involving regulatory elements upstream of LMNB1. It can also be caused by inverted duplications involving LMNB1, as reported in one patient. {ECO:0000269|PubMed:39078102}.; DISEASE: Microcephaly 26, primary, autosomal dominant (MCPH26) [MIM:619179]: A 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. {ECO:0000269|PubMed:32910914, ECO:0000269|PubMed:33033404}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
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). Plays a role in sperm morphological development during late stages of spermiogenesis, particularly the anchoring of the sperm head to the tail (PubMed:38870534). Component of the LMNB1/SUN5/SEPT12 bridge that connects the sperm proximal centriole to the implantation fossa, the bridge functions to prevent detachment of the proximal centriole from the posterior nucleus during spermiogenesis (PubMed:38870534). {ECO:0000269|PubMed:28716252, ECO:0000269|PubMed:32910914, ECO:0000269|PubMed:38870534}.
uniprot
proteins
mass_dalton
66408
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000269|PubMed:2684976}.; PTM: 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. {ECO:0000250|UniProtKB:P02545}.
uniprot
proteins
protein_family
Intermediate filament family
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16951681
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22265972
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
2325650
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24686783
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25775403
uniprot
proteins
pubmed
26237509
uniprot
proteins
pubmed
2684976
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28716252
uniprot
proteins
pubmed
28939839
uniprot
proteins
pubmed
32910914
uniprot
proteins
pubmed
33033404
uniprot
proteins
pubmed
33706103
uniprot
proteins
pubmed
38870534
uniprot
proteins
pubmed
39078102
uniprot
proteins
pubmed
7557986
uniprot
proteins
sequence_length
586
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus lamina {ECO:0000269|PubMed:28716252, ECO:0000269|PubMed:32910914}. Note=Expressed in the posterior part of the nucleus during mid-steps of spermiogenesis, expression becomes more localized to the implantation fossa in later stages (By similarity). Expressed at the neck region in mature sperm (By similarity). {ECO:0000250|UniProtKB:P14733}.
uniprot
proteins