| '''Tribbles homolog 2''' is an atypical [[protein kinase]] that is encoded in human by the ''TRIB2'' [[gene]].<ref name="pmid12736262">{{cite journal |vauthors=Wu M, Xu LG, Zhai Z, Shu HB | title = SINK is a p65-interacting negative regulator of NF-kappaB-dependent transcription | journal = J Biol Chem | volume = 278 | issue = 29 | pages = 27072–9 |date=Jul 2003 | pmid = 12736262 | pmc = | doi = 10.1074/jbc.M209814200 }}</ref><ref name="pmid17097562">{{cite journal |vauthors=Keeshan K, He Y, Wouters BJ, Shestova O, Xu L, Sai H, Rodriguez CG, Maillard I, Tobias JW, Valk P, Carroll M, Aster JC, Delwel R, Pear WS | title = Tribbles homolog 2 inactivates C/EBPalpha and causes acute myelogenous leukemia | journal = Cancer Cell | volume = 10 | issue = 5 | pages = 401–11 |date=Nov 2006 | pmid = 17097562 | pmc = 2839500| doi = 10.1016/j.ccr.2006.09.012 }}</ref><ref name="pmid16715410">{{cite journal |vauthors=Hegedus Z, Czibula A, Kiss-Toth E | title = Tribbles: novel regulators of cell function; evolutionary aspects | journal = Cell Mol Life Sci | volume = 63 | issue = 14 | pages = 1632–41 |date=Aug 2006 | pmid = 16715410 | pmc = | doi = 10.1007/s00018-006-6007-9 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: TRIB2 tribbles homolog 2 (Drosophila)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=28951| accessdate = }}</ref> TRIB2 is a [[pseudokinase]] member of the ([[pseudoenzyme]]) class of signaling/scaffold proteins, possessing little vestigial catalytic output in vitro.<ref name="pmid25583260">{{cite journal |vauthors= Bailey FP, et al | title = The Tribbles 2 (TRB2) pseudokinase binds to ATP and autophosphorylates in a metal-independent manner. | journal = Biochemical Society Transactions | volume = 467 | issue = 1 | pages = 47–62 | year = 2015 | pmid = 25583260 | doi = 10.1042/BJ20141441| url = }}</ref> It is known to signal to canonical MAPK pathways and to regulate the ubiquitination of substrates with important functions in the immune system. It has also been associated with various diseases, especially in vertebrate leukaemia models.<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> Like [[TRIB1]] and [[TRIB3]], TRIB2 has recently been considered as a potential allosteric drug target,<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><ref name="pmid28097887 ">{{cite journal |vauthors= Byrne DP, Foulkes DM, Eyers PA | title = Pseudokinases: update on their functions and evaluation as new drug targets. | journal = Future Medicinal Chemistry | volume = 9 | issue = 2 | pages = 245–265| year = 2017 | pmid =28097887| doi = 10.4155/fmc-2016-0207| url = }}</ref> and is a putative regulator of cancer-associated signalling and survival through AKT pSer473 modulation <ref name="pmid28276427">{{cite journal |vauthors= Hill R, Madureira PA, Ferreira B, Baptista I, Machado S, Colaço L, Dos Santos M, Liu N, Dopazo A, Ugurel S, Adrienn A, Kiss-Toth E, Isbilen M, Gure AO, Link W | title = TRIB2 confers resistance to anti-cancer therapy by activating the serine/threonine protein kinase AKT | journal = Nature Communications | volume = 8 | issue = 5 | pages = 14687 | year = 2017 | pmid = 28276427 | doi = 10.1038/ncomms14687| url = }}</ref> | | '''Tribbles homolog 2''' is an atypical [[protein kinase]] that is encoded in human by the ''TRIB2'' [[gene]].<ref name="pmid12736262">{{cite journal |vauthors=Wu M, Xu LG, Zhai Z, Shu HB | title = SINK is a p65-interacting negative regulator of NF-kappaB-dependent transcription | journal = J Biol Chem | volume = 278 | issue = 29 | pages = 27072–9 |date=Jul 2003 | pmid = 12736262 | pmc = | doi = 10.1074/jbc.M209814200 }}</ref><ref name="pmid17097562">{{cite journal |vauthors=Keeshan K, He Y, Wouters BJ, Shestova O, Xu L, Sai H, Rodriguez CG, Maillard I, Tobias JW, Valk P, Carroll M, Aster JC, Delwel R, Pear WS | title = Tribbles homolog 2 inactivates C/EBPalpha and causes acute myelogenous leukemia | journal = Cancer Cell | volume = 10 | issue = 5 | pages = 401–11 |date=Nov 2006 | pmid = 17097562 | pmc = 2839500| doi = 10.1016/j.ccr.2006.09.012 }}</ref><ref name="pmid16715410">{{cite journal |vauthors=Hegedus Z, Czibula A, Kiss-Toth E | title = Tribbles: novel regulators of cell function; evolutionary aspects | journal = Cell Mol Life Sci | volume = 63 | issue = 14 | pages = 1632–41 |date=Aug 2006 | pmid = 16715410 | pmc = | doi = 10.1007/s00018-006-6007-9 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: TRIB2 tribbles homolog 2 (Drosophila)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=28951| accessdate = }}</ref> TRIB2 is a [[pseudokinase]] member of the ([[pseudoenzyme]]) class of signaling/scaffold proteins, possessing little vestigial catalytic output in vitro.<ref name="pmid25583260">{{cite journal |vauthors= Bailey FP, et al | title = The Tribbles 2 (TRB2) pseudokinase binds to ATP and autophosphorylates in a metal-independent manner. | journal = Biochemical Society Transactions | volume = 467 | issue = 1 | pages = 47–62 | year = 2015 | pmid = 25583260 | doi = 10.1042/BJ20141441| pmc=4844368}}</ref> It is known to signal to canonical MAPK pathways and to regulate the ubiquitination of substrates with important functions in the immune system. It has also been associated with various diseases, especially in vertebrate leukaemia models.<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> Like [[TRIB1]] and [[TRIB3]], TRIB2 has recently been considered as a potential allosteric drug target,<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><ref name="pmid28097887 ">{{cite journal |vauthors= Byrne DP, Foulkes DM, Eyers PA | title = Pseudokinases: update on their functions and evaluation as new drug targets. | journal = Future Medicinal Chemistry | volume = 9 | issue = 2 | pages = 245–265| year = 2017 | pmid =28097887| doi = 10.4155/fmc-2016-0207| url = }}</ref> and is a putative regulator of cancer-associated signalling and survival through AKT pSer473 modulation <ref name="pmid28276427">{{cite journal |vauthors= Hill R, Madureira PA, Ferreira B, Baptista I, Machado S, Colaço L, Dos Santos M, Liu N, Dopazo A, Ugurel S, Adrienn A, Kiss-Toth E, Isbilen M, Gure AO, Link W | title = TRIB2 confers resistance to anti-cancer therapy by activating the serine/threonine protein kinase AKT | journal = Nature Communications | volume = 8 | issue = 5 | pages = 14687 | year = 2017 | pmid = 28276427 | doi = 10.1038/ncomms14687| pmc=5347136}}</ref> |
