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
External IDs	MGI: 96795 HomoloGene: 55912 GeneCards: LMNB1
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	4001	16906
Ensembl	ENSG00000113368	ENSMUSG00000024590
UniProt	P20700	P14733
RefSeq (mRNA)	NM_001198557 NM_005573	NM_010721
RefSeq (protein)	NP_005564.1	NP_034851.2
Location (UCSC)	Chr 5: 126.78 – 126.84 Mb	Chr 18: 56.71 – 56.75 Mb
PubMed search	[1]	[2]
Wikidata

View/Edit Human

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Lamin-B1 is a protein that in humans is encoded by the LMNB1 gene.^[3][4][5]

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.^[5] 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.^[6][7]

See also

• Lamin B

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. 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.
4. 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.
5. "Entrez Gene: LMNB1 lamin B1".
6. Furukawa, K; Kondo T (Feb 1998). "Identification of the lamina-associated-polypeptide-2-binding domain of B-type lamin". Eur. J. Biochem. GERMANY. 251 (3): 729–33. doi:10.1046/j.1432-1327.1998.2510729.x. ISSN 0014-2956. PMID 9490046.
7. 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. UNITED STATES. 73 (7): 1267–79. doi:10.1016/0092-8674(93)90355-T. ISSN 0092-8674. PMID 8324822.

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.
• 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.
• 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. 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. 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. 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. 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.
• 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.