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

TOB1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesTOB1, APRO6, PIG49, TOB, TROB, TROB1, transducer of ERBB2, 1, APRO5
External IDsOMIM: 605523; MGI: 1349721; HomoloGene: 31334; GeneCards: TOB1; OMA:TOB1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
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

Function

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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

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TOB1 has been shown to interact with:

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000141232Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000037573Ensembl, 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

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