Thymopoietin

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Thymopoietin
PDB rendering based on 1gjj.
Identifiers
Symbols TMPO ; TP; LAP2; CMD1T; MGC61508; PRO0868
External IDs Template:OMIM5 Template:MGI HomoloGene31144
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

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Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1] Phone:617-632-7753



Thymopoietin, also known as TMPO, is a human gene.[1]

Thymopoietin is a protein involved in the induction of CD90 in the thymus. The thymopoetin (TMPO) gene encodes three alternatively spliced mRNAs encoding proteins of 75 kDa (alpha), 51 kDa (beta) and 39 kDa (gamma) which are ubiquitously expressed in all cells. The human TMPO gene maps to chromosome band 12q22 and consists of eight exons. TMPO alpha is present diffusely expressed with the cell nucleus while TMPO beta and gamma are localized to the nuclear membrane. TMPO beta is a human homolog of the murine protein LAP2 (lamina-associated polypeptide 2). LAP2 plays a role in the regulation of nuclear architecture by binding lamin B1 and chromosomes. This interaction is regulated by phosphorylation during mitosis. Given the nuclear localization of the three TMPO isoforms, it is unlikely that these proteins play any role in CD90 induction.

References

  1. "Entrez Gene: TMPO thymopoietin".

Further reading

  • Harris CA, Andryuk PJ, Cline SW, Mathew S, Siekierka JJ, Goldstein G (1995). "Structure and mapping of the human thymopoietin (TMPO) gene and relationship of human TMPO beta to rat lamin-associated polypeptide 2". Genomics. 28 (2): 198–205. doi:10.1006/geno.1995.1131. PMID 8530026.
  • Dechat T, Vlcek S, Foisner R (2000). "Review: lamina-associated polypeptide 2 isoforms and related proteins in cell cycle-dependent nuclear structure dynamics". J. Struct. Biol. 129 (2–3): 335–45. doi:10.1006/jsbi.2000.4212. PMID 10806084.
  • Twomey JJ, Goldstein G, Lewis VM; et al. (1977). "Bioassay determinations of thymopoietin and thymic hormone levels in human plasma". Proc. Natl. Acad. Sci. U.S.A. 74 (6): 2541–5. PMID 302007.
  • Heavner GA, Audhya T, Goldstein G (1990). "Peptide analogs of thymopentin distinguish distinct thymopoietin receptor specificities on two human T cell lines". Regul. Pept. 27 (2): 257–62. PMID 2158125.
  • Audhya T, Schlesinger DH, Goldstein G (1987). "Isolation and complete amino acid sequence of human thymopoietin and splenin". Proc. Natl. Acad. Sci. U.S.A. 84 (11): 3545–9. PMID 3473468.
  • Fuccello A, Audhya T, Talle MA, Goldstein G (1984). "Immunoassay for bovine serum thymopoietin: discrimination from splenin by monoclonal antibodies". Arch. Biochem. Biophys. 228 (1): 292–8. PMID 6364989.
  • Harris CA, Andryuk PJ, Cline S; et al. (1994). "Three distinct human thymopoietins are derived from alternatively spliced mRNAs". Proc. Natl. Acad. Sci. U.S.A. 91 (14): 6283–7. PMID 7517549.
  • Hara H, Hayashi K, Ohta K; et al. (1995). "A new thymopoietin precursor gene from human thymus". Biochem. Mol. Biol. Int. 34 (5): 927–33. PMID 7703909.
  • Goldstein G, Schlesinger DH, Audhya T (1994). "Isolation and complete amino acid sequence of human thymopoietin and splenin". Proc. Natl. Acad. Sci. U.S.A. 91 (13): 6249. PMID 8016147.
  • Harris CA, Andryuk PJ, Cline SW; et al. (1996). "Structure and mapping of the human thymopoietin (TMPO) gene and relationship of human TMPO beta to rat lamin-associated polypeptide 2". Genomics. 28 (2): 198–205. doi:10.1006/geno.1995.1131. PMID 8530026.
  • Andersson B, Wentland MA, Ricafrente JY; et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
  • Berger R, Theodor L, Shoham J; et al. (1996). "The characterization and localization of the mouse thymopoietin/lamina-associated polypeptide 2 gene and its alternatively spliced products". Genome Res. 6 (5): 361–70. PMID 8743987.
  • Yu W, Andersson B, Worley KC; et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. PMID 9110174.
  • Furukawa K, Fritze CE, Gerace L (1998). "The major nuclear envelope targeting domain of LAP2 coincides with its lamin binding region but is distinct from its chromatin interaction domain". J. Biol. Chem. 273 (7): 4213–9. PMID 9461618.
  • 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. PMID 9490046.
  • Dechat T, Gotzmann J, Stockinger A; et al. (1998). "Detergent-salt resistance of LAP2alpha in interphase nuclei and phosphorylation-dependent association with chromosomes early in nuclear assembly implies functions in nuclear structure dynamics". EMBO J. 17 (16): 4887–902. doi:10.1093/emboj/17.16.4887. PMID 9707448.
  • Furukawa K (1999). "LAP2 binding protein 1 (L2BP1/BAF) is a candidate mediator of LAP2-chromatin interaction". J. Cell. Sci. 112 ( Pt 15): 2485–92. PMID 10393804.
  • Weber PJ, Eckhard CP, Gonser S; et al. (1999). "On the role of thymopoietins in cell proliferation. Immunochemical evidence for new members of the human thymopoietin family". Biol. Chem. 380 (6): 653–60. PMID 10430029.
  • Dechat T, Korbei B, Vaughan OA; et al. (2000). "Lamina-associated polypeptide 2alpha binds intranuclear A-type lamins". J. Cell. Sci. 113 Pt 19: 3473–84. PMID 10984438.
  • Martins SB, Eide T, Steen RL; et al. (2001). "HA95 is a protein of the chromatin and nuclear matrix regulating nuclear envelope dynamics". J. Cell. Sci. 113 Pt 21: 3703–13. PMID 11034899.

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