Lamin B1

LMNB1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2KPW, 3JT0, 3TYY, 3UMN
Identifiers
Aliases	LMNB1, ADLD, LMN, LMN2, LMNB, lamin B1, MCPH26
External IDs	OMIM: 150340; MGI: 96795; HomoloGene: 55912; GeneCards: LMNB1; OMA:LMNB1 - orthologs
Gene location (Human) Chr. Chromosome 5 (human)[1] Band 5q23.2 Start 126,776,623 bp[1] End 126,837,020 bp[1]
Gene location (Mouse) Chr. Chromosome 18 (mouse)[2] Band 18 D3|18 30.84 cM Start 56,840,885 bp[2] End 56,886,496 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ventricular zone ganglionic eminence monocyte rectum appendix mucosa of transverse colon bone marrow blood bone marrow cells buccal mucosa cell Top expressed in ventricular zone granulocyte tail of embryo epiblast abdominal wall genital tubercle thymus yolk sac ganglionic eminence medial ganglionic eminence More reference expression data BioGPS More reference expression data
Gene ontology Molecular function phospholipase binding structural molecule activity protein binding double-stranded DNA binding sequence-specific double-stranded DNA binding Cellular component nuclear matrix nuclear inner membrane nuclear membrane membrane intermediate filament lamin filament nucleoplasm nucleus nuclear envelope Biological process interleukin-12-mediated signaling pathway Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4001 16906 Ensembl ENSG00000113368 ENSMUSG00000024590 UniProt P20700 P14733 RefSeq (mRNA) NM_001198557 NM_005573 NM_010721 RefSeq (protein) NP_001185486 NP_005564 NP_034851 Location (UCSC) Chr 5: 126.78 – 126.84 Mb Chr 18: 56.84 – 56.89 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Lamin-B1 is a protein that in humans is encoded by the LMNB1 gene.[5][6][7]

The nuclear lamina consists of a two-dimensional matrix of proteins located next to the inner nuclear membrane. The lamin family of proteins make up the matrix and are highly conserved in evolution. During mitosis, the lamina matrix is reversibly disassembled as the lamin proteins are phosphorylated. Lamin proteins are thought to be involved in nuclear stability, chromatin structure, and gene expression. Vertebrate lamins consist of two types, A and B. This gene encodes one of the two B type proteins, B1.[7] Lamin B, along with heterochromatin, is anchored to the inner surface of the nuclear membrane by the lamin B receptor.

Interactions

LMNB1 has been shown to interact with Thymopoietin.[8][9] When double-strand breaks are induced in DNA by ionizing radiation, lamin B1 promotes repair of the breaks, as well as cell survival, by maintaining the level of the RAD51 protein that is employed in homologous recombinational repair.[10]

Pathology

Mutations affecting the LMNB1 gene cause autosomal dominant adult-onset demyelinating leukodystrophy.

See also

• Lamin B2

References

1. GRCh38: Ensembl release 89: ENSG00000113368 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000024590 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Lin F, Worman HJ (Nov 1995). "Structural organization of the human gene (LMNB1) encoding nuclear lamin B1". Genomics. 27 (2): 230–6. doi:10.1006/geno.1995.1036. PMID 7557986.
6. Wydner KL, McNeil JA, Lin F, Worman HJ, Lawrence JB (Feb 1997). "Chromosomal assignment of human nuclear envelope protein genes LMNA, LMNB1, and LBR by fluorescence in situ hybridization". Genomics. 32 (3): 474–8. doi:10.1006/geno.1996.0146. PMID 8838815.
7. "Entrez Gene: LMNB1 lamin B1".
8. Furukawa K, Kondo T (Feb 1998). "Identification of the lamina-associated-polypeptide-2-binding domain of B-type lamin". Eur. J. Biochem. 251 (3). GERMANY: 729–33. doi:10.1046/j.1432-1327.1998.2510729.x. ISSN 0014-2956. PMID 9490046.
9. Foisner R, Gerace L (Jul 1993). "Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation". Cell. 73 (7). UNITED STATES: 1267–79. doi:10.1016/0092-8674(93)90355-T. ISSN 0092-8674. PMID 8324822. S2CID 10641633.
10. Liu NA, Sun J, Kono K, Horikoshi Y, Ikura T, Tong X, Haraguchi T, Tashiro S. Regulation of homologous recombinational repair by lamin B1 in radiation-induced DNA damage. FASEB J. 2015 Jun;29(6):2514-25. doi: 10.1096/fj.14-265546. Epub 2015 Mar 2. PMID 25733566

Further reading

• Gruenbaum Y, Wilson KL, Harel A, et al. (2000). "Review: nuclear lamins--structural proteins with fundamental functions". J. Struct. Biol. 129 (2–3): 313–23. doi:10.1006/jsbi.2000.4216. PMID 10806082.
• Worman HJ, Courvalin JC (2000). "The inner nuclear membrane". J. Membr. Biol. 177 (1): 1–11. doi:10.1007/s002320001096. PMID 10960149. S2CID 20121844.
• Djabali K, Portier MM, Gros F, et al. (1991). "Network antibodies identify nuclear lamin B as a physiological attachment site for peripherin intermediate filaments". Cell. 64 (1): 109–21. doi:10.1016/0092-8674(91)90213-I. PMID 1986862. S2CID 6246606.
• Foisner R, Traub P, Wiche G (1991). "Protein kinase A- and protein kinase C-regulated interaction of plectin with lamin B and vimentin". Proc. Natl. Acad. Sci. U.S.A. 88 (9): 3812–6. Bibcode:1991PNAS...88.3812F. doi:10.1073/pnas.88.9.3812. PMC 51543. PMID 2023931.
• Pollard KM, Chan EK, Grant BJ, et al. (1990). "In vitro posttranslational modification of lamin B cloned from a human T-cell line". Mol. Cell. Biol. 10 (5): 2164–75. doi:10.1128/mcb.10.5.2164. PMC 360564. PMID 2325650.
• Müller WE, Okamoto T, Reuter P, et al. (1990). "Functional characterization of Tat protein from human immunodeficiency virus. Evidence that Tat links viral RNAs to nuclear matrix". J. Biol. Chem. 265 (7): 3803–8. doi:10.1016/S0021-9258(19)39665-6. PMID 2406262.
• Müller WE, Wenger R, Reuter P, et al. (1989). "Association of Tat protein and viral mRNA with nuclear matrix from HIV-1-infected H9 cells". Biochim. Biophys. Acta. 1008 (2): 208–12. doi:10.1016/0167-4781(80)90011-1. PMID 2544227.
• Eldridge R, Anayiotos CP, Schlesinger S, et al. (1984). "Hereditary adult-onset leukodystrophy simulating chronic progressive multiple sclerosis". N. Engl. J. Med. 311 (15): 948–53. doi:10.1056/NEJM198410113111504. PMID 6472420.
• Ye Q, Worman HJ (1995). "Protein-protein interactions between human nuclear lamins expressed in yeast". Exp. Cell Res. 219 (1): 292–8. doi:10.1006/excr.1995.1230. PMID 7628545.
• Goss VL, Hocevar BA, Thompson LJ, et al. (1994). "Identification of nuclear beta II protein kinase C as a mitotic lamin kinase". J. Biol. Chem. 269 (29): 19074–80. doi:10.1016/S0021-9258(17)32276-7. PMID 8034666.
• Broers JL, Machiels BM, Kuijpers HJ, et al. (1997). "A- and B-type lamins are differentially expressed in normal human tissues". Histochem. Cell Biol. 107 (6): 505–17. doi:10.1007/s004180050138. PMID 9243284. S2CID 24088247.
• Maison C, Pyrpasopoulou A, Theodoropoulos PA, Georgatos SD (1997). "The inner nuclear membrane protein LAP1 forms a native complex with B-type lamins and partitions with spindle-associated mitotic vesicles". EMBO J. 16 (16): 4839–50. doi:10.1093/emboj/16.16.4839. PMC 1170119. PMID 9305626.
• Lin F, Worman HJ (1997). "Expression of nuclear lamins in human tissues and cancer cell lines and transcription from the promoters of the lamin A/C and B1 genes". Exp. Cell Res. 236 (2): 378–84. doi:10.1006/excr.1997.3735. PMID 9367621.
• Vodicka MA, Koepp DM, Silver PA, Emerman M (1998). "HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection". Genes Dev. 12 (2): 175–85. doi:10.1101/gad.12.2.175. PMC 316441. PMID 9436978.
• Furukawa K, Kondo T (1998). "Identification of the lamina-associated-polypeptide-2-binding domain of B-type lamin". Eur. J. Biochem. 251 (3): 729–33. doi:10.1046/j.1432-1327.1998.2510729.x. PMID 9490046.
• Kowluru A (2000). "Evidence for the carboxyl methylation of nuclear lamin-B in the pancreatic beta cell". Biochem. Biophys. Res. Commun. 268 (2): 249–54. doi:10.1006/bbrc.2000.2107. PMID 10679189.