TOB1

Protein Tob1 is a protein that in humans is encoded by the TOB1 gene.

TOB1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2D5R, 2Z15, 5CI8, 5CI9
Identifiers
Aliases	TOB1, APRO6, PIG49, TOB, TROB, TROB1, transducer of ERBB2, 1, APRO5
External IDs	OMIM: 605523; MGI: 1349721; HomoloGene: 31334; GeneCards: TOB1; OMA:TOB1 - orthologs
Gene location (Human) Chr. Chromosome 17 (human) Band 17q21.33 Start 50,862,223 bp End 50,867,978 bp
Gene location (Mouse) Chr. Chromosome 11 (mouse) Band 11|11 D Start 94,102,280 bp End 94,106,321 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in mucosa of paranasal sinus germinal epithelium skin of thigh Skeletal muscle tissue of biceps brachii seminal vesicula Epithelium of choroid plexus trachea vastus lateralis muscle cardia Skeletal muscle tissue of rectus abdominis Top expressed in extensor digitorum longus muscle plantaris muscle pineal gland submandibular gland parotid gland seminal vesicula intercostal muscle triceps brachii muscle digastric muscle sternocleidomastoid muscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function receptor tyrosine kinase binding SMAD binding protein binding transcription corepressor activity Cellular component CCR4-NOT complex cytoplasm nucleus Biological process positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay negative regulation of osteoblast differentiation negative regulation of nuclear-transcribed mRNA poly(A) tail shortening negative regulation of nucleic acid-templated transcription negative regulation of BMP signaling pathway negative regulation of translation positive regulation of nuclear-transcribed mRNA poly(A) tail shortening BMP signaling pathway negative regulation of cell population proliferation positive regulation of signal transduction regulation of SMAD protein signal transduction regulation of gene expression Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10140 22057 Ensembl ENSG00000141232 ENSMUSG00000037573 UniProt P50616 Q61471 RefSeq (mRNA) NM_005749 NM_001243877 NM_001243885 NM_009427 RefSeq (protein) NP_001230806 NP_001230814 NP_005740 NP_033453 Location (UCSC) Chr 17: 50.86 – 50.87 Mb Chr 11: 94.1 – 94.11 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Function

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 suppresses cell growth in tissue culture. The protein undergoes phosphorylation 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.

Interactions

TOB1 has been shown to interact with:

• CNOT7,
• MAPK1
• MARCKS,
• Mitogen-activated protein kinase 9, and
• RPS6KA1.

Further reading

• Sasaki S, Imai K (Mar 2002). "[Monoclonal antibody induces apoptosis against cancer cells]". Nihon Rinsho. Japanese Journal of Clinical Medicine. 60 (3): 451–6. PMID 11904957.
• Yoshida Y, Matsuda S, Yamamoto T (May 1997). "Cloning and characterization of the mouse tob gene". Gene. 191 (1): 109–13. doi:10.1016/S0378-1119(97)00049-8. PMID 9210596.
• Ikematsu N, Yoshida Y, Kawamura-Tsuzuku J, Ohsugi M, Onda M, Hirai M, Fujimoto J, Yamamoto T (Dec 1999). "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. S2CID 35769674.
• Yoshida Y, Tanaka S, Umemori H, Minowa O, Usui M, Ikematsu N, Hosoda E, Imamura T, Kuno J, Yamashita T, Miyazono K, Noda M, Noda T, Yamamoto T (Dec 2000). "Negative regulation of BMP/Smad signaling by Tob in osteoblasts". Cell. 103 (7): 1085–97. doi:10.1016/S0092-8674(00)00211-7. PMID 11163184. S2CID 18267832.
• Suzuki T, Matsuda S, Tsuzuku JK, Yoshida Y, Yamamoto T (Feb 2001). "A serine/threonine kinase p90rsk1 phosphorylates the anti-proliferative protein Tob". Genes to Cells. 6 (2): 131–8. doi:10.1046/j.1365-2443.2001.00406.x. PMID 11260258. S2CID 21599032.
• Jin Cho S, La M, Ahn JK, Meadows GG, Joe CO (May 2001). "Tob-mediated cross-talk between MARCKS phosphorylation and ErbB-2 activation". Biochemical and Biophysical Research Communications. 283 (2): 273–7. doi:10.1006/bbrc.2001.4773. PMID 11327693.
• Yoshida Y, Hosoda E, Nakamura T, Yamamoto T (Jun 2001). "Association of ANA, a member of the antiproliferative Tob family proteins, with a Caf1 component of the CCR4 transcriptional regulatory complex". Japanese Journal of Cancer Research. 92 (6): 592–6. doi:10.1111/j.1349-7006.2001.tb01135.x. PMC 5926753. PMID 11429045.
• Tzachanis D, Freeman GJ, Hirano N, van Puijenbroek AA, Delfs MW, Berezovskaya A, Nadler LM, Boussiotis VA (Dec 2001). "Tob is a negative regulator of activation that is expressed in anergic and quiescent T cells". Nature Immunology. 2 (12): 1174–82. doi:10.1038/ni730. PMID 11694881. S2CID 38103879.
• Suzuki T, K-Tsuzuku J, Ajima R, Nakamura T, Yoshida Y, Yamamoto T (Jun 2002). "Phosphorylation of three regulatory serines of Tob by Erk1 and Erk2 is required for Ras-mediated cell proliferation and transformation". Genes & Development. 16 (11): 1356–70. doi:10.1101/gad.962802. PMC 186319. PMID 12050114.
• Sasajima H, Nakagawa K, Yokosawa H (Jul 2002). "Antiproliferative proteins of the BTG/Tob family are degraded by the ubiquitin-proteasome system". European Journal of Biochemistry. 269 (14): 3596–604. doi:10.1046/j.1432-1033.2002.03052.x. PMID 12135500.
• Maekawa M, Nishida E, Tanoue T (Oct 2002). "Identification of the Anti-proliferative protein Tob as a MAPK substrate". The Journal of Biological Chemistry. 277 (40): 37783–7. doi:10.1074/jbc.M204506200. PMID 12151396.
• Yoshida Y, von Bubnoff A, Ikematsu N, Blitz IL, Tsuzuku JK, Yoshida EH, Umemori H, Miyazono K, Yamamoto T, Cho KW (May 2003). "Tob proteins enhance inhibitory Smad-receptor interactions to repress BMP signaling". Mechanisms of Development. 120 (5): 629–37. doi:10.1016/S0925-4773(03)00020-0. PMID 12782279. S2CID 728736.
• Iwanaga K, Sueoka N, Sato A, Sakuragi T, Sakao Y, Tominaga M, Suzuki T, Yoshida Y, K-Tsuzuku J, Yamamoto T, Hayashi S, Nagasawa K, Sueoka E (Dec 2003). "Alteration of expression or phosphorylation status of tob, a novel tumor suppressor gene product, is an early event in lung cancer". Cancer Letters. 202 (1): 71–9. doi:10.1016/j.canlet.2003.08.019. PMID 14643028.
• Maekawa M, Yamamoto T, Nishida E (Apr 2004). "Regulation of subcellular localization of the antiproliferative protein Tob by its nuclear export signal and bipartite nuclear localization signal sequences". Experimental Cell Research. 295 (1): 59–65. doi:10.1016/j.yexcr.2003.12.016. PMID 15051490.
• Kawamura-Tsuzuku J, Suzuki T, Yoshida Y, Yamamoto T (Aug 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. S2CID 19519175.
• Okochi K, Suzuki T, Inoue J, Matsuda S, Yamamoto T (Feb 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 to Cells. 10 (2): 151–63. doi:10.1111/j.1365-2443.2005.00826.x. PMID 15676026. S2CID 40563615.

External links

• TOB1 human gene location in the UCSC Genome Browser.
• TOB1 human gene details in the UCSC Genome Browser.