TOB1

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Transducer of ERBB2, 1
File:PBB Protein TOB1 image.jpg
PDB rendering based on 2d5r.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols TOB1 ; APRO6; MGC104792; MGC34446; PIG49; TOB; TROB; TROB1
External IDs Template:OMIM5 Template:MGI HomoloGene: 31334
RNA expression pattern
File:PBB GE TOB1 202704 at tn.png
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

Transducer of ERBB2, 1, also known as TOB1, is a human gene.[1]

This gene encodes a member of the tob/btg1 family of anti-proliferative proteins that have the potential to regulate cell growth. When exogenously expressed, this protein supresses cell growth in tissue culture. The protein undergoes phophorylation by a serine/threonine kinase, 90 kDa ribosomal S6 kinase. Interactions of this protein with the v-erb-b2 erythroblastic leukemia viral oncogene homolog 2 gene product p185 interferes with growth suppression. This protein inhibits T cell proliferation and transcription of cytokines and cyclins. The protein interacts with both mothers against decapentaplegic Drosophila homolog 2 and 4 to enhance their DNA binding activity. This interaction inhibits interleukin 2 transcription in T cells.[1]

References

  1. ↑ 1.0 1.1 "Entrez Gene: TOB1 transducer of ERBB2, 1".

Further reading

  • Sasaki S, Imai K (2002). "[Monoclonal antibody induces apoptosis against cancer cells]". Nippon Rinsho. 60 (3): 451–6. PMID 11904957.
  • Matsuda S, Kawamura-Tsuzuku J, Ohsugi M; et al. (1996). "Tob, a novel protein that interacts with p185erbB2, is associated with anti-proliferative activity". Oncogene. 12 (4): 705–13. PMID 8632892.
  • Yoshida Y, Matsuda S, Yamamoto T (1997). "Cloning and characterization of the mouse tob gene". Gene. 191 (1): 109–13. PMID 9210596.
  • Ikematsu N, Yoshida Y, Kawamura-Tsuzuku J; et al. (2000). "Tob2, a novel anti-proliferative Tob/BTG1 family member, associates with a component of the CCR4 transcriptional regulatory complex capable of binding cyclin-dependent kinases". Oncogene. 18 (52): 7432–41. doi:10.1038/sj.onc.1203193. PMID 10602502.
  • Yoshida Y, Tanaka S, Umemori H; et al. (2001). "Negative regulation of BMP/Smad signaling by Tob in osteoblasts". Cell. 103 (7): 1085–97. PMID 11163184.
  • Suzuki T, Matsuda S, Tsuzuku JK; et al. (2001). "A serine/threonine kinase p90rsk1 phosphorylates the anti-proliferative protein Tob". Genes Cells. 6 (2): 131–8. PMID 11260258.
  • Jin Cho S, La M, Ahn JK; et al. (2001). "Tob-mediated cross-talk between MARCKS phosphorylation and ErbB-2 activation". Biochem. Biophys. Res. Commun. 283 (2): 273–7. doi:10.1006/bbrc.2001.4773. PMID 11327693.
  • Yoshida Y, Hosoda E, Nakamura T, Yamamoto T (2001). "Association of ANA, a member of the antiproliferative Tob family proteins, with a Caf1 component of the CCR4 transcriptional regulatory complex". Jpn. J. Cancer Res. 92 (6): 592–6. PMID 11429045.
  • Tzachanis D, Freeman GJ, Hirano N; et al. (2001). "Tob is a negative regulator of activation that is expressed in anergic and quiescent T cells". Nat. Immunol. 2 (12): 1174–82. doi:10.1038/ni730. PMID 11694881.
  • Suzuki T, K-Tsuzuku J, Ajima R; et al. (2002). "Phosphorylation of three regulatory serines of Tob by Erk1 and Erk2 is required for Ras-mediated cell proliferation and transformation". Genes Dev. 16 (11): 1356–70. doi:10.1101/gad.962802. PMID 12050114.
  • Sasajima H, Nakagawa K, Yokosawa H (2002). "Antiproliferative proteins of the BTG/Tob family are degraded by the ubiquitin-proteasome system". Eur. J. Biochem. 269 (14): 3596–604. PMID 12135500.
  • Maekawa M, Nishida E, Tanoue T (2002). "Identification of the Anti-proliferative protein Tob as a MAPK substrate". J. Biol. Chem. 277 (40): 37783–7. doi:10.1074/jbc.M204506200. PMID 12151396.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Yoshida Y, von Bubnoff A, Ikematsu N; et al. (2004). "Tob proteins enhance inhibitory Smad-receptor interactions to repress BMP signaling". Mech. Dev. 120 (5): 629–37. PMID 12782279.
  • Iwanaga K, Sueoka N, Sato A; et al. (2004). "Alteration of expression or phosphorylation status of tob, a novel tumor suppressor gene product, is an early event in lung cancer". Cancer Lett. 202 (1): 71–9. PMID 14643028.
  • Maekawa M, Yamamoto T, Nishida E (2004). "Regulation of subcellular localization of the antiproliferative protein Tob by its nuclear export signal and bipartite nuclear localization signal sequences". Exp. Cell Res. 295 (1): 59–65. doi:10.1016/j.yexcr.2003.12.016. PMID 15051490.
  • Kawamura-Tsuzuku J, Suzuki T, Yoshida Y, Yamamoto T (2004). "Nuclear localization of Tob is important for regulation of its antiproliferative activity". Oncogene. 23 (39): 6630–8. doi:10.1038/sj.onc.1207890. PMID 15235587.
  • Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
  • Okochi K, Suzuki T, Inoue J; et al. (2005). "Interaction of anti-proliferative protein Tob with poly(A)-binding protein and inducible poly(A)-binding protein: implication of Tob in translational control". Genes Cells. 10 (2): 151–63. doi:10.1111/j.1365-2443.2005.00826.x. PMID 15676026.

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