TOB1

Protein-coding gene in the species Homo sapiens
TOB1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2D5R, 2Z15, 5CI8, 5CI9

Identifiers
AliasesTOB1, APRO6, PIG49, TOB, TROB, TROB1, transducer of ERBB2, 1, APRO5
External IDsOMIM: 605523; MGI: 1349721; HomoloGene: 31334; GeneCards: TOB1; OMA:TOB1 - orthologs
Gene location (Human)
Chromosome 17 (human)
Chr.Chromosome 17 (human)[1]
Chromosome 17 (human)
Genomic location for TOB1
Genomic location for TOB1
Band17q21.33Start50,862,223 bp[1]
End50,867,978 bp[1]
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[2]
Chromosome 11 (mouse)
Genomic location for TOB1
Genomic location for TOB1
Band11|11 DStart94,102,280 bp[2]
End94,106,321 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr 11: 94.1 – 94.11 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Protein Tob1 is a protein that in humans is encoded by the TOB1 gene.[5][6][7]

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.[7]

Interactions

TOB1 has been shown to interact with:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000141232 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000037573 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Matsuda S, Kawamura-Tsuzuku J, Ohsugi M, Yoshida M, Emi M, Nakamura Y, Onda M, Yoshida Y, Nishiyama A, Yamamoto T (Feb 1996). "Tob, a novel protein that interacts with p185erbB2, is associated with anti-proliferative activity". Oncogene. 12 (4): 705–13. PMID 8632892.
  6. ^ Ezzeddine N, Chang TC, Zhu W, Yamashita A, Chen CY, Zhong Z, Yamashita Y, Zheng D, Shyu AB (Nov 2007). "Human TOB, an antiproliferative transcription factor, is a poly(A)-binding protein-dependent positive regulator of cytoplasmic mRNA deadenylation". Molecular and Cellular Biology. 27 (22): 7791–801. doi:10.1128/MCB.01254-07. PMC 2169145. PMID 17785442.
  7. ^ a b "Entrez Gene: TOB1 transducer of ERBB2, 1".
  8. ^ Funakoshi Y, Doi Y, Hosoda N, Uchida N, Osawa M, Shimada I, Tsujimoto M, Suzuki T, Katada T, Hoshino S (Dec 2007). "Mechanism of mRNA deadenylation: evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylases". Genes & Development. 21 (23): 3135–48. doi:10.1101/gad.1597707. PMC 2081979. PMID 18056425.
  9. ^ 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.
  10. ^ a b 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.
  11. ^ 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.
  12. ^ 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.

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.
  • v
  • t
  • e
  • 2d5r: Crystal Structure of a Tob-hCaf1 Complex
    2d5r: Crystal Structure of a Tob-hCaf1 Complex


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