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Protein TMPO PDB 1gjj.png
PDB rendering based on 1gjj.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols TMPO ; CMD1T; LAP2; LEMD4; PRO0868; TP
External IDs OMIM188380 MGI106920 HomoloGene31144 GeneCards: TMPO Gene
RNA expression pattern
PBB GE TMPO 209753 s at tn.png
PBB GE TMPO 209754 s at tn.png
PBB GE TMPO 203432 at tn.png
More reference expression data
Species Human Mouse
Entrez 7112 21917
Ensembl ENSG00000120802 ENSMUSG00000019961
UniProt P42166 Q61029
RefSeq (mRNA) NM_001032283 NM_001080129
RefSeq (protein) NP_001027454 NP_001073598
Location (UCSC) Chr 12:
98.52 – 98.55 Mb
Chr 10:
91.15 – 91.17 Mb
PubMed search [1] [2]

Lamina-associated polypeptide 2 (LAP2), isoforms beta/gamma is a protein that in humans is encoded by the TMPO gene.[1][2] LAP2 is an inner nuclear membrane (INM) protein.[3]

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. 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.


Thymopoietin has been shown to interact with Barrier to autointegration factor 1,[4] AKAP8L,[5][6] LMNB1[7][8] and LMNA.[9][10]


  1. ^ Harris CA, Andryuk PJ, Cline S, Chan HK, Natarajan A, Siekierka JJ, Goldstein G (August 1994). "Three distinct human thymopoietins are derived from alternatively spliced mRNAs". Proc Natl Acad Sci U S A 91 (14): 6283–7. doi:10.1073/pnas.91.14.6283. PMC 44185. PMID 7517549. 
  2. ^ "Entrez Gene: TMPO thymopoietin". 
  3. ^ Holmer, L.; Worman, H. J. (2001). "Inner nuclear membrane proteins: Functions and targeting". Cellular and molecular life sciences : CMLS 58 (12–13): 1741–1747. doi:10.1007/PL00000813. PMID 11766875.  edit
  4. ^ Furukawa, K (August 1999). "LAP2 binding protein 1 (L2BP1/BAF) is a candidate mediator of LAP2-chromatin interaction". J. Cell. Sci. (ENGLAND) 112 (15): 2485–92. ISSN 0021-9533. PMID 10393804. 
  5. ^ Martins, S B; Eide T; Steen R L; Jahnsen T; Skålhegg B S; Collas P (November 2000). "HA95 is a protein of the chromatin and nuclear matrix regulating nuclear envelope dynamics". J. Cell. Sci. (ENGLAND) 113 (21): 3703–13. ISSN 0021-9533. PMID 11034899. 
  6. ^ Martins, Sandra; Eikvar Sissel; Furukawa Kazuhiro; Collas Philippe (January 2003). "HA95 and LAP2 beta mediate a novel chromatin-nuclear envelope interaction implicated in initiation of DNA replication". J. Cell Biol. (United States) 160 (2): 177–88. doi:10.1083/jcb.200210026. ISSN 0021-9525. PMC 2172640. PMID 12538639. 
  7. ^ Furukawa, K; Kondo T (February 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. 
  8. ^ Foisner, R; Gerace L (July 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. 
  9. ^ Markiewicz, Ewa; Dechat Thomas; Foisner Roland; Quinlan Roy A; Hutchison Christopher J (December 2002). "Lamin A/C binding protein LAP2alpha is required for nuclear anchorage of retinoblastoma protein". Mol. Biol. Cell (United States) 13 (12): 4401–13. doi:10.1091/mbc.E02-07-0450. ISSN 1059-1524. PMC 138642. PMID 12475961. 
  10. ^ Dechat, T; Korbei B; Vaughan O A; Vlcek S; Hutchison C J; Foisner R (October 2000). "Lamina-associated polypeptide 2alpha binds intranuclear A-type lamins". J. Cell. Sci. (ENGLAND) 113 (19): 3473–84. ISSN 0021-9533. PMID 10984438. 

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