TRIB3

Short description: Protein-coding gene in the species Homo sapiens

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:

AKT1,^[1]
CSNK2B,^[6]
Fibronectin^[6]
MCM3AP,^[7]
RELA,^[8]
SIAH1,^[6] and
TIAF1.^[6]

References

↑ ^1.0 ^1.1 "TRB3: a tribbles homolog that inhibits Akt/PKB activation by insulin in liver". Science 300 (5625): 1574–7. Jun 2003. doi:10.1126/science.1079817. PMID 12791994. Bibcode: 2003Sci...300.1574D.
↑ "Tribbles: novel regulators of cell function; evolutionary aspects". Cell Mol Life Sci 63 (14): 1632–41. Aug 2006. doi:10.1007/s00018-006-6007-9. PMID 16715410.
↑ ^3.0 ^3.1 "Entrez Gene: TRIB3 tribbles homolog 3 (Drosophila)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=57761.
↑ "Tribbles in the 21st Century: The Evolving Roles of Tribbles Pseudokinases in Biology and Disease.". Trends in Cell Biology 27 (9): S0962-8924(16)30178-7. 2016. doi:10.1016/j.tcb.2016.11.002. PMID 27908682.
↑ "Tribbles pseudokinases: novel targets for chemical biology and drug discovery?". Biochemical Society Transactions 43 (5): 1095–1103. 2015. doi:10.1042/BST20150109. PMID 26517930.
↑ ^6.0 ^6.1 ^6.2 ^6.3 "E3 ubiquitin ligase SIAH1 mediates ubiquitination and degradation of TRB3". Cell. Signal. 20 (5): 942–8. May 2008. doi:10.1016/j.cellsig.2008.01.010. PMID 18276110.
↑ "SKIP3, a novel Drosophila tribbles ortholog, is overexpressed in human tumors and is regulated by hypoxia". Oncogene 22 (18): 2823–35. May 2003. doi:10.1038/sj.onc.1206367. PMID 12743605.
↑ "SINK is a p65-interacting negative regulator of NF-kappaB-dependent transcription". J. Biol. Chem. 278 (29): 27072–9. July 2003. doi:10.1074/jbc.M209814200. PMID 12736262.

"Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1–2): 171–4. 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
"Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1–2): 149–56. 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
"The DNA sequence and comparative analysis of human chromosome 20.". Nature 414 (6866): 865–71. 2002. doi:10.1038/414865a. PMID 11780052. Bibcode: 2001Natur.414..865D.
"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. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
"SINK is a p65-interacting negative regulator of NF-kappaB-dependent transcription.". J. Biol. Chem. 278 (29): 27072–9. 2003. doi:10.1074/jbc.M209814200. PMID 12736262.
"SKIP3, a novel Drosophila tribbles ortholog, is overexpressed in human tumors and is regulated by hypoxia.". Oncogene 22 (18): 2823–35. 2003. doi:10.1038/sj.onc.1206367. PMID 12743605.
"Identification of a novel serine/threonine kinase that inhibits TNF-induced NF-kappaB activation and p53-induced transcription.". Biochem. Biophys. Res. Commun. 309 (4): 774–8. 2003. doi:10.1016/j.bbrc.2003.08.069. PMID 13679039.
"Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. 2004. doi:10.1038/ng1285. PMID 14702039.
"Human tribbles, a protein family controlling mitogen-activated protein kinase cascades.". J. Biol. Chem. 279 (41): 42703–8. 2004. doi:10.1074/jbc.M407732200. PMID 15299019.
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334.
"TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death.". EMBO J. 24 (6): 1243–55. 2005. doi:10.1038/sj.emboj.7600596. PMID 15775988.
"Characterization of human NIPK (TRB3, SKIP3) gene activation in stressful conditions.". Biochem. Biophys. Res. Commun. 330 (1): 210–8. 2005. doi:10.1016/j.bbrc.2005.02.149. PMID 15781252.
"The functional Q84R polymorphism of mammalian Tribbles homolog TRB3 is associated with insulin resistance and related cardiovascular risk in Caucasians from Italy.". Diabetes 54 (9): 2807–11. 2005. doi:10.2337/diabetes.54.9.2807. PMID 16123373.
"TRB3 is a PI 3-kinase dependent indicator for nutrient starvation.". Cell. Signal. 18 (6): 899–909. 2006. doi:10.1016/j.cellsig.2005.08.002. PMID 16129579.
"A human protein-protein interaction network: a resource for annotating the proteome.". Cell 122 (6): 957–68. 2005. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
"Effect of TRB3 on insulin and nutrient-stimulated hepatic p70 S6 kinase activity.". J. Biol. Chem. 281 (40): 29719–29. 2006. doi:10.1074/jbc.M511636200. PMID 16887816.
"Skeletal muscle-selective knockout of LKB1 increases insulin sensitivity, improves glucose homeostasis, and decreases TRB3.". Mol. Cell. Biol. 26 (22): 8217–27. 2007. doi:10.1128/MCB.00979-06. PMID 16966378.

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Original source: https://en.wikipedia.org/wiki/TRIB3. Read more

[pmid12791994-1] 1.0 ^1.1 "TRB3: a tribbles homolog that inhibits Akt/PKB activation by insulin in liver". Science 300 (5625): 1574–7. Jun 2003. doi:10.1126/science.1079817. PMID 12791994. Bibcode: 2003Sci...300.1574D.

[pmid16715410-2] "Tribbles: novel regulators of cell function; evolutionary aspects". Cell Mol Life Sci 63 (14): 1632–41. Aug 2006. doi:10.1007/s00018-006-6007-9. PMID 16715410.

[entrez-3] 3.0 ^3.1 "Entrez Gene: TRIB3 tribbles homolog 3 (Drosophila)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=57761.

[pmid27908682-4] "Tribbles in the 21st Century: The Evolving Roles of Tribbles Pseudokinases in Biology and Disease.". Trends in Cell Biology 27 (9): S0962-8924(16)30178-7. 2016. doi:10.1016/j.tcb.2016.11.002. PMID 27908682.

[pmid26517930-5] "Tribbles pseudokinases: novel targets for chemical biology and drug discovery?". Biochemical Society Transactions 43 (5): 1095–1103. 2015. doi:10.1042/BST20150109. PMID 26517930.

[pmid18276110-6] 6.0 ^6.1 ^6.2 ^6.3 "E3 ubiquitin ligase SIAH1 mediates ubiquitination and degradation of TRB3". Cell. Signal. 20 (5): 942–8. May 2008. doi:10.1016/j.cellsig.2008.01.010. PMID 18276110.

[pmid12743605-7] "SKIP3, a novel Drosophila tribbles ortholog, is overexpressed in human tumors and is regulated by hypoxia". Oncogene 22 (18): 2823–35. May 2003. doi:10.1038/sj.onc.1206367. PMID 12743605.

[pmid12736262-8] "SINK is a p65-interacting negative regulator of NF-kappaB-dependent transcription". J. Biol. Chem. 278 (29): 27072–9. July 2003. doi:10.1074/jbc.M209814200. PMID 12736262.

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v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

TRIB3

Topic: Biology

Contents

Function

Interactions

References

Further reading