TOB1

From Wikipedia, the free encyclopedia

Transducer of ERBB2, 1

PDB rendering based on 2d5r.

Available structures: 2d5r

Identifiers

Symbol(s)

TOB1; APRO6; MGC104792; MGC34446; PIG49; TOB; TROB; TROB1

External IDs

OMIM: 605523 MGI: 1349721 HomoloGene: 31334

Gene ontology
Molecular Function:	• transcription corepressor activity • SH3/SH2 adaptor activity • SMAD binding
Cellular Component:	• cytoplasm
Biological Process:	• SMAD protein nuclear translocation • negative regulation of cell proliferation • negative regulation of BMP signaling pathway • negative regulation of osteoblast differentiation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_005749 (mRNA)
NP_005740 (protein)

NM_009427 (mRNA)
NP_033453 (protein)

Location

Chr 17: 46.3 - 46.3 Mb

Chr 11: 94.03 - 94.03 Mb

Pubmed search

[1]

[2]

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]

[edit] References

^ ^a ^b Entrez Gene: TOB1 transducer of ERBB2, 1.

[edit] 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.