TRIB3: Difference between revisions

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== Function ==
== Function ==


The protein encoded by this gene is a putative [[protein kinase]] that is induced by the transcription factor [[NF-kappaB]]. It is a [[pseudoenzyme]] that is thought to be a negative regulator of NF-kappaB, and can also sensitize cells to [[TNF]]- and [[TRAIL]]-induced [[apoptosis]]. In addition, this protein has been reported to negatively regulate the cell survival serine-threonine kinase [[AKT1]].<ref name="entrez" /> TRIB3 has recently been associated with neuronal signalling, and like [[TRIB1]] and [[TRIB2]], could be considered as a potential allosteric drug target <ref name="pmid27908682">{{cite journal |vauthors= Eyers PA, Keeshan K, Kannan N | title = Tribbles in the 21st Century: The Evolving Roles of Tribbles Pseudokinases in Biology and Disease. | journal = Trends in Cell Biology | volume = In Press | issue = 9 | pages = S0962-8924(16)30178-7 | year = 2016 | pmid = 27908682 | doi = 10.1016/j.tcb.2016.11.002| url = }}</ref><ref name="pmid26517930">{{cite journal |vauthors= Foulkes DM, Byrne DP, Eyers PA | title = Tribbles pseudokinases: novel targets for chemical biology and drug discovery? | journal = Biochemical Society Transactions | volume = 43 | issue = 5 | pages = 1095–1103 | year = 2015 | pmid = 26517930 | doi = 10.1042/BST20150109| url = }}</ref>
The protein encoded by this gene is a putative [[protein kinase]] that is induced by the transcription factor [[NF-kappaB]]. It is a [[pseudoenzyme]] that is thought to be a negative regulator of NF-kappaB, and can also sensitize cells to [[TNF]]- and [[TRAIL]]-induced [[apoptosis]]. In addition, this protein has been reported to negatively regulate the cell survival serine-threonine kinase [[AKT1]].<ref name="entrez" /> TRIB3 has recently been associated with neuronal signalling, and like [[TRIB1]] and [[TRIB2]], could be considered as a potential allosteric drug target <ref name="pmid27908682">{{cite journal |vauthors= Eyers PA, Keeshan K, Kannan N | title = Tribbles in the 21st Century: The Evolving Roles of Tribbles Pseudokinases in Biology and Disease. | journal = Trends in Cell Biology | volume = In Press | issue = 9 | pages = S0962-8924(16)30178-7 | year = 2016 | pmid = 27908682 | doi = 10.1016/j.tcb.2016.11.002| pmc=5382568}}</ref><ref name="pmid26517930">{{cite journal |vauthors= Foulkes DM, Byrne DP, Eyers PA | title = Tribbles pseudokinases: novel targets for chemical biology and drug discovery? | journal = Biochemical Society Transactions | volume = 43 | issue = 5 | pages = 1095–1103 | year = 2015 | pmid = 26517930 | doi = 10.1042/BST20150109| url = }}</ref>


==Interactions==
==Interactions==
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==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
*{{cite journal  |vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8  }}
*{{cite journal  |vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8  }}
*{{cite journal  |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3  }}
*{{cite journal  |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3  }}
*{{cite journal  |vauthors=Deloukas P, Matthews LH, Ashurst J, etal |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865–71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a }}
*{{cite journal  |vauthors=Deloukas P, Matthews LH, Ashurst J, etal |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865–71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a }}
*{{cite journal  |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 }}
*{{cite journal  |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 }}

Revision as of 18:44, 9 March 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

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n/a

RefSeq (protein)

n/a

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Tribbles homolog 3 is a protein that in humans is encoded by the TRIB3 gene.[1][2][3]

Function

The protein encoded by this gene is a putative protein kinase that is induced by the transcription factor NF-kappaB. It is a pseudoenzyme that is thought to be a negative regulator of NF-kappaB, and can also sensitize cells to TNF- and TRAIL-induced apoptosis. In addition, this protein has been reported to negatively regulate the cell survival serine-threonine kinase AKT1.[3] TRIB3 has recently been associated with neuronal signalling, and like TRIB1 and TRIB2, could be considered as a potential allosteric drug target [4][5]

Interactions

TRIB3 has been shown to interact with:

References

  1. 1.0 1.1 Du K, Herzig S, Kulkarni RN, Montminy M (Jun 2003). "TRB3: a tribbles homolog that inhibits Akt/PKB activation by insulin in liver". Science. 300 (5625): 1574–7. doi:10.1126/science.1079817. PMID 12791994.
  2. Hegedus Z, Czibula A, Kiss-Toth E (Aug 2006). "Tribbles: novel regulators of cell function; evolutionary aspects". Cell Mol Life Sci. 63 (14): 1632–41. doi:10.1007/s00018-006-6007-9. PMID 16715410.
  3. 3.0 3.1 "Entrez Gene: TRIB3 tribbles homolog 3 (Drosophila)".
  4. Eyers PA, Keeshan K, Kannan N (2016). "Tribbles in the 21st Century: The Evolving Roles of Tribbles Pseudokinases in Biology and Disease". Trends in Cell Biology. In Press (9): S0962-8924(16)30178-7. doi:10.1016/j.tcb.2016.11.002. PMC 5382568. PMID 27908682.
  5. Foulkes DM, Byrne DP, Eyers PA (2015). "Tribbles pseudokinases: novel targets for chemical biology and drug discovery?". Biochemical Society Transactions. 43 (5): 1095–1103. doi:10.1042/BST20150109. PMID 26517930.
  6. 6.0 6.1 6.2 6.3 Zhou Y, Li L, Liu Q, Xing G, Kuai X, Sun J, Yin X, Wang J, Zhang L, He F (May 2008). "E3 ubiquitin ligase SIAH1 mediates ubiquitination and degradation of TRB3". Cell. Signal. 20 (5): 942–8. doi:10.1016/j.cellsig.2008.01.010. PMID 18276110.
  7. Bowers AJ, Scully S, Boylan JF (May 2003). "SKIP3, a novel Drosophila tribbles ortholog, is overexpressed in human tumors and is regulated by hypoxia". Oncogene. 22 (18): 2823–35. doi:10.1038/sj.onc.1206367. PMID 12743605.
  8. Wu M, Xu LG, Zhai Z, Shu HB (July 2003). "SINK is a p65-interacting negative regulator of NF-kappaB-dependent transcription". J. Biol. Chem. 278 (29): 27072–9. doi:10.1074/jbc.M209814200. PMID 12736262.

Further reading