TRIB3: Difference between revisions

TRIB3
Identifiers
Aliases	TRIB3, C20orf97, NIPK, SINK, SKIP3, TRB3, tribbles pseudokinase 3
External IDs	OMIM: 607898; MGI: 1345675; HomoloGene: 10902; GeneCards: TRIB3; OMA:TRIB3 - orthologs
Gene location (Human)
Chr.	Chromosome 20 (human)
End	397,559 bp
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)
End	152,185,952 bp
RNA expression pattern
	Top expressed in
	right lobe of liver; ; pancreatic ductal cell; ; gonad; ; islet of Langerhans; ; stromal cell of endometrium; ; upper lobe of left lung; ; optic nerve; ; body of pancreas; ; parotid gland; ; anterior pituitary;
	Top expressed in
	lumbar spinal ganglion; ; endothelial cell of lymphatic vessel; ; calvaria; ; yolk sac; ; submandibular gland; ; seminal vesicula; ; ascending aorta; ; semi-lunar valve; ; aortic valve; ; olfactory epithelium;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	transcription corepressor activity; ubiquitin-protein transferase regulator activity; protein kinase inhibitor activity; kinase activity; protein binding; mitogen-activated protein kinase kinase binding; ATP binding; protein kinase binding; ubiquitin protein ligase binding;
Cellular component	cytosol; plasma membrane; nucleus;
Biological process	negative regulation of fat cell differentiation; regulation of transcription, DNA-templated; negative regulation of fatty acid biosynthetic process; negative regulation of protein kinase activity; negative regulation of transcription by RNA polymerase II; transcription, DNA-templated; response to endoplasmic reticulum stress; protein phosphorylation; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; positive regulation of ubiquitin-protein transferase activity; cellular response to insulin stimulus; regulation of MAP kinase activity; positive regulation of protein binding; negative regulation of transcription, DNA-templated; regulation of glucose transmembrane transport; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; apoptotic process; regulation of lipid metabolic process; negative regulation of protein kinase B signaling; regulation of autophagy;
	Sources:Amigo / QuickGO
Orthologs
	57761
	228775
	ENSG00000101255
	ENSMUSG00000032715
	Q96RU7
	Q8K4K2
NM_021158; NM_001301188; NM_001301190; NM_001301193; NM_001301196;
	NM_001301201
	NM_144554; NM_175093
NP_001288117; NP_001288119; NP_001288122; NP_001288125; NP_001288130;
	NP_066981
	NP_780302
	Wikidata
View/Edit Human	View/Edit Mouse

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Latest revision as of 15:06, 16 July 2024

Tribbles homolog 3 is a protein that in humans is encoded by the TRIB3 gene.^[5]^[6]^[7]

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.^[7] TRIB3 has recently been associated with neuronal signalling, and like TRIB1 and TRIB2, could be considered as a potential allosteric drug target.^[8]^[9]

Interactions

TRIB3 has been shown to interact with:

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000101255 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000032715 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b 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. Bibcode:2003Sci...300.1574D. doi:10.1126/science.1079817. PMID 12791994. S2CID 43360696.
^ 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. PMC 11136108. PMID 16715410. S2CID 24556931.
^ ^a ^b "Entrez Gene: TRIB3 tribbles homolog 3 (Drosophila)".
^ 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. 27 (9): S0962-8924(16)30178-7. doi:10.1016/j.tcb.2016.11.002. PMC 5382568. PMID 27908682.
^ 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.
^ ^a ^b ^c ^d 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.
^ 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.
^ 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.

Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature. 414 (6866): 865–71. Bibcode:2001Natur.414..865D. doi:10.1038/414865a. PMID 11780052.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Wu M, Xu LG, Zhai Z, Shu HB (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.
Bowers AJ, Scully S, Boylan JF (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.
Huang J, Teng L, Liu T, et al. (2003). "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. doi:10.1016/j.bbrc.2003.08.069. PMID 13679039.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Kiss-Toth E, Bagstaff SM, Sung HY, et al. (2004). "Human tribbles, a protein family controlling mitogen-activated protein kinase cascades". J. Biol. Chem. 279 (41): 42703–8. doi:10.1074/jbc.M407732200. hdl:2262/33449. PMID 15299019.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Ohoka N, Yoshii S, Hattori T, et al. (2005). "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. doi:10.1038/sj.emboj.7600596. PMC 556400. PMID 15775988.
Ord D, Ord T (2005). "Characterization of human NIPK (TRB3, SKIP3) gene activation in stressful conditions". Biochem. Biophys. Res. Commun. 330 (1): 210–8. doi:10.1016/j.bbrc.2005.02.149. PMID 15781252.
Prudente S, Hribal ML, Flex E, et al. (2005). "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. doi:10.2337/diabetes.54.9.2807. PMID 16123373.
Schwarzer R, Dames S, Tondera D, et al. (2006). "TRB3 is a PI 3-kinase dependent indicator for nutrient starvation". Cell. Signal. 18 (6): 899–909. doi:10.1016/j.cellsig.2005.08.002. PMID 16129579.
Stelzl U, Worm U, Lalowski M, et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
Matsushima R, Harada N, Webster NJ, et al. (2006). "Effect of TRB3 on insulin and nutrient-stimulated hepatic p70 S6 kinase activity". J. Biol. Chem. 281 (40): 29719–29. doi:10.1074/jbc.M511636200. PMID 16887816.
Koh HJ, Arnolds DE, Fujii N, et al. (2007). "Skeletal muscle-selective knockout of LKB1 increases insulin sensitivity, improves glucose homeostasis, and decreases TRB3". Mol. Cell. Biol. 26 (22): 8217–27. doi:10.1128/MCB.00979-06. PMC 1636784. PMID 16966378.

This article on a gene on human chromosome 20 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000101255 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000032715 – 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.

[pmid12791994-5] 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. Bibcode:2003Sci...300.1574D. doi:10.1126/science.1079817. PMID 12791994. S2CID 43360696.

[pmid16715410-6] 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. PMC 11136108. PMID 16715410. S2CID 24556931.

[entrez-7] "Entrez Gene: TRIB3 tribbles homolog 3 (Drosophila)".

[pmid27908682-8] 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. 27 (9): S0962-8924(16)30178-7. doi:10.1016/j.tcb.2016.11.002. PMC 5382568. PMID 27908682.

[pmid26517930-9] 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.

[pmid18276110-10] 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.

[pmid12743605-11] 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.

[pmid12736262-12] 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.

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+{{cs1 config|name-list-style=vanc}}
-{{PBB|geneid=57761}}
+{{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]].<ref name="pmid12791994">{{cite journal | author = Du K, Herzig S, Kulkarni RN, Montminy M | title = TRB3: a tribbles homolog that inhibits Akt/PKB activation by insulin in liver | journal = Science | volume = 300 | issue = 5625 | pages = 1574-7 | year = 2003 | month = Jun | pmid = 12791994 | pmc =  | doi = 10.1126/science.1079817 }}</ref><ref name="pmid16715410">{{cite journal | author = 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 | year = 2006 | month = Aug | pmid = 16715410 | pmc =  | doi = 10.1007/s00018-006-6007-9 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: TRIB3 tribbles homolog 3 (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=57761| accessdate = }}</ref>
+{{Infobox_gene}}
+'''Tribbles homolog 3''' is a [[protein]] that in humans is encoded by the ''TRIB3'' [[gene]].<ref name="pmid12791994">{{cite journal |vauthors=Du K, Herzig S, Kulkarni RN, Montminy M | title = TRB3: a tribbles homolog that inhibits Akt/PKB activation by insulin in liver | journal = Science | volume = 300 | issue = 5625 | pages = 1574–7 |date=Jun 2003 | pmid = 12791994 | doi = 10.1126/science.1079817 | bibcode = 2003Sci...300.1574D | s2cid = 43360696 }}</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 | doi = 10.1007/s00018-006-6007-9 | s2cid = 24556931 | pmc = 11136108 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: TRIB3 tribbles homolog 3 (Drosophila)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=57761}}</ref>
+== Function ==
-<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
-{{PBB_Summary
+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 = 27 | 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}}</ref>
-| section_title =
-| summary_text = The protein encoded by this gene is a putative protein kinase that is induced by the transcription factor NF-kappaB. The encoded protein is a negative regulator of NF-kappaB and can also sensitize cells to TNF- and TRAIL-induced apoptosis. In addition, this protein can negatively regulate the cell survival serine-threonine kinase AKT1.<ref name="entrez">{{cite web | title = Entrez Gene: TRIB3 tribbles homolog 3 (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=57761| accessdate = }}</ref>
-}}
 ==Interactions==
+TRIB3 has been shown to [[Protein-protein interaction|interact]] with:
-TRIB3 has been shown to [[Protein-protein_interaction|interact]] with [[CSNK2B]],<ref name=pmid18276110>{{cite journal | quotes = yes |last=Zhou |first=Ying |authorlink= |coauthors=Li Lu, Liu Qiongming, Xing Guichun, Kuai Xuezhang, Sun Jing, Yin Xiushan, Wang Jian, Zhang Lingqiang, He Fuchu |year=[[2008]]|month=May. |title=E3 ubiquitin ligase SIAH1 mediates ubiquitination and degradation of TRB3 |journal=Cell. Signal. |volume=20 |issue=5 |pages=942-8 |publisher= |location = England| issn = 0898-6568| pmid = 18276110 |doi = 10.1016/j.cellsig.2008.01.010 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[TIAF1]],<ref name=pmid18276110/> [[RELA]],<ref name=pmid12736262>{{cite journal | quotes = yes |last=Wu |first=Min |authorlink= |coauthors=Xu Liang-Guo, Zhai Zhonghe, Shu Hong-Bing |year=[[2003]]|month=Jul. |title=SINK is a p65-interacting negative regulator of NF-kappaB-dependent transcription |journal=J. Biol. Chem. |volume=278 |issue=29 |pages=27072-9 |publisher= |location = United States| issn = 0021-9258| pmid = 12736262 |doi = 10.1074/jbc.M209814200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[MCM3AP]],<ref name=pmid18276110/> [[ATF5]],<ref name=pmid18276110/> [[Granulin]],<ref name=pmid18276110/> [[ATF4]],<ref name=pmid12743605>{{cite journal | quotes = yes |last=Bowers |first=Alex J |authorlink= |coauthors=Scully Sheila, Boylan John F |year=[[2003]]|month=May. |title=SKIP3, a novel Drosophila tribbles ortholog, is overexpressed in human tumors and is regulated by hypoxia |journal=Oncogene |volume=22 |issue=18 |pages=2823-35 |publisher= |location = England| issn = 0950-9232| pmid = 12743605 |doi = 10.1038/sj.onc.1206367 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref><ref name=pmid18276110/> [[AKT1]],<ref name=pmid12791994>{{cite journal | quotes = yes |last=Du |first=Keyong |authorlink= |coauthors=Herzig Stephan, Kulkarni Rohit N, Montminy Marc |year=[[2003]]|month=Jun. |title=TRB3: a tribbles homolog that inhibits Akt/PKB activation by insulin in liver |journal=[[Science (journal)|Science]] |volume=300 |issue=5625 |pages=1574-7 |publisher= |location = United States| issn = | pmid = 12791994 |doi = 10.1126/science.1079817 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[Fibronectin]]<ref name=pmid18276110/> and [[SIAH1]].<ref name=pmid18276110/>
+* [[AKT1]],<ref name="pmid12791994" />
+* [[CSNK2B]],<ref name="pmid18276110">{{cite journal |vauthors=Zhou Y, Li L, Liu Q, Xing G, Kuai X, Sun J, Yin X, Wang J, Zhang L, He F | title = E3 ubiquitin ligase SIAH1 mediates ubiquitination and degradation of TRB3 | journal = Cell. Signal. | volume = 20 | issue = 5 | pages = 942–8 |date=May 2008 | pmid = 18276110 | doi = 10.1016/j.cellsig.2008.01.010 }}</ref>
+* [[Fibronectin]]<ref name=pmid18276110/>
+* [[MCM3AP]],<ref name="pmid12743605">{{cite journal |vauthors=Bowers AJ, Scully S, Boylan JF | title = SKIP3, a novel Drosophila tribbles ortholog, is overexpressed in human tumors and is regulated by hypoxia | journal = Oncogene | volume = 22 | issue = 18 | pages = 2823–35 |date=May 2003 | pmid = 12743605 | doi = 10.1038/sj.onc.1206367 | doi-access = free }}</ref>
+* [[RELA]],<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=July 2003 | pmid = 12736262 | doi = 10.1074/jbc.M209814200 | doi-access =  free}}</ref>
+* [[SIAH1]],<ref name=pmid18276110/> and
+* [[TIAF1]].<ref name=pmid18276110/>
 ==References==
 {{reflist}}
 ==Further reading==
 {{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  }}
-{{PBB_Further_reading
+*{{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  }}
-| citations =
-*{{cite journal  | author=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=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 |bibcode=2001Natur.414..865D |doi-access= free }}
-*{{cite journal  | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |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=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 |bibcode=2002PNAS...9916899M |doi-access=free }}
-*{{cite journal  | author=Deloukas P, Matthews LH, Ashurst J, ''et al.'' |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=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 |year= 2003 |pmid= 12736262 |doi= 10.1074/jbc.M209814200 |doi-access=  free}}
-*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |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 }}
+*{{cite journal  |vauthors=Bowers AJ, Scully S, Boylan JF |title=SKIP3, a novel Drosophila tribbles ortholog, is overexpressed in human tumors and is regulated by hypoxia. |journal=Oncogene |volume=22 |issue= 18 |pages= 2823–35 |year= 2003 |pmid= 12743605 |doi= 10.1038/sj.onc.1206367 |doi-access= free }}
-*{{cite journal  | author=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 |year= 2003 |pmid= 12736262 |doi= 10.1074/jbc.M209814200 }}
+*{{cite journal   |vauthors=Huang J, Teng L, Liu T, etal |title=Identification of a novel serine/threonine kinase that inhibits TNF-induced NF-kappaB activation and p53-induced transcription. |journal=Biochem. Biophys. Res. Commun. |volume=309 |issue= 4 |pages= 774–8 |year= 2003 |pmid= 13679039 |doi=10.1016/j.bbrc.2003.08.069  }}
-*{{cite journal  | author=Bowers AJ, Scully S, Boylan JF |title=SKIP3, a novel Drosophila tribbles ortholog, is overexpressed in human tumors and is regulated by hypoxia. |journal=Oncogene |volume=22 |issue= 18 |pages= 2823–35 |year= 2003 |pmid= 12743605 |doi= 10.1038/sj.onc.1206367 }}
+*{{cite journal   |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |doi-access= free }}
-*{{cite journal  | author=Huang J, Teng L, Liu T, ''et al.'' |title=Identification of a novel serine/threonine kinase that inhibits TNF-induced NF-kappaB activation and p53-induced transcription. |journal=Biochem. Biophys. Res. Commun. |volume=309 |issue= 4 |pages= 774–8 |year= 2003 |pmid= 13679039 |doi=10.1016/j.bbrc.2003.08.069  }}
+*{{cite journal   |vauthors=Kiss-Toth E, Bagstaff SM, Sung HY, etal |title=Human tribbles, a protein family controlling mitogen-activated protein kinase cascades. |journal=J. Biol. Chem. |volume=279 |issue= 41 |pages= 42703–8 |year= 2004 |pmid= 15299019 |doi= 10.1074/jbc.M407732200 |doi-access= free |hdl= 2262/33449 |hdl-access= free }}
-*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
+*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 }}
-*{{cite journal  | author=Kiss-Toth E, Bagstaff SM, Sung HY, ''et al.'' |title=Human tribbles, a protein family controlling mitogen-activated protein kinase cascades. |journal=J. Biol. Chem. |volume=279 |issue= 41 |pages= 42703–8 |year= 2004 |pmid= 15299019 |doi= 10.1074/jbc.M407732200 }}
+*{{cite journal   |vauthors=Ohoka N, Yoshii S, Hattori T, etal |title=TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death. |journal=EMBO J. |volume=24 |issue= 6 |pages= 1243–55 |year= 2005 |pmid= 15775988 |doi= 10.1038/sj.emboj.7600596  | pmc=556400 }}
-*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
+*{{cite journal  |vauthors=Ord D, Ord T |title=Characterization of human NIPK (TRB3, SKIP3) gene activation in stressful conditions. |journal=Biochem. Biophys. Res. Commun. |volume=330 |issue= 1 |pages= 210–8 |year= 2005 |pmid= 15781252 |doi= 10.1016/j.bbrc.2005.02.149 }}
-*{{cite journal  | author=Ohoka N, Yoshii S, Hattori T, ''et al.'' |title=TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death. |journal=Embo J. |volume=24 |issue= 6 |pages= 1243–55 |year= 2005 |pmid= 15775988 |doi= 10.1038/sj.emboj.7600596 }}
+*{{cite journal   |vauthors=Prudente S, Hribal ML, Flex E, etal |title=The functional Q84R polymorphism of mammalian Tribbles homolog TRB3 is associated with insulin resistance and related cardiovascular risk in Caucasians from Italy. |journal=Diabetes |volume=54 |issue= 9 |pages= 2807–11 |year= 2005 |pmid= 16123373 |doi=10.2337/diabetes.54.9.2807  |doi-access=free }}
-*{{cite journal  | author=Ord D, Ord T |title=Characterization of human NIPK (TRB3, SKIP3) gene activation in stressful conditions. |journal=Biochem. Biophys. Res. Commun. |volume=330 |issue= 1 |pages= 210–8 |year= 2005 |pmid= 15781252 |doi= 10.1016/j.bbrc.2005.02.149 }}
+*{{cite journal   |vauthors=Schwarzer R, Dames S, Tondera D, etal |title=TRB3 is a PI 3-kinase dependent indicator for nutrient starvation. |journal=Cell. Signal. |volume=18 |issue= 6 |pages= 899–909 |year= 2006 |pmid= 16129579 |doi= 10.1016/j.cellsig.2005.08.002 }}
-*{{cite journal  | author=Prudente S, Hribal ML, Flex E, ''et al.'' |title=The functional Q84R polymorphism of mammalian Tribbles homolog TRB3 is associated with insulin resistance and related cardiovascular risk in Caucasians from Italy. |journal=Diabetes |volume=54 |issue= 9 |pages= 2807–11 |year= 2005 |pmid= 16123373 |doi=10.2337/diabetes.54.9.2807  }}
+*{{cite journal   |vauthors=Stelzl U, Worm U, Lalowski M, etal |title=A human protein-protein interaction network: a resource for annotating the proteome. |journal=Cell |volume=122 |issue= 6 |pages= 957–68 |year= 2005 |pmid= 16169070 |doi= 10.1016/j.cell.2005.08.029 |hdl= 11858/00-001M-0000-0010-8592-0 |s2cid=8235923 |hdl-access= free }}
-*{{cite journal  | author=Schwarzer R, Dames S, Tondera D, ''et al.'' |title=TRB3 is a PI 3-kinase dependent indicator for nutrient starvation. |journal=Cell. Signal. |volume=18 |issue= 6 |pages= 899–909 |year= 2006 |pmid= 16129579 |doi= 10.1016/j.cellsig.2005.08.002 }}
+*{{cite journal   |vauthors=Matsushima R, Harada N, Webster NJ, etal |title=Effect of TRB3 on insulin and nutrient-stimulated hepatic p70 S6 kinase activity. |journal=J. Biol. Chem. |volume=281 |issue= 40 |pages= 29719–29 |year= 2006 |pmid= 16887816 |doi= 10.1074/jbc.M511636200 |doi-access= free }}
-*{{cite journal  | author=Stelzl U, Worm U, Lalowski M, ''et al.'' |title=A human protein-protein interaction network: a resource for annotating the proteome. |journal=Cell |volume=122 |issue= 6 |pages= 957–68 |year= 2005 |pmid= 16169070 |doi= 10.1016/j.cell.2005.08.029 }}
+*{{cite journal   |vauthors=Koh HJ, Arnolds DE, Fujii N, etal |title=Skeletal muscle-selective knockout of LKB1 increases insulin sensitivity, improves glucose homeostasis, and decreases TRB3. |journal=Mol. Cell. Biol. |volume=26 |issue= 22 |pages= 8217–27 |year= 2007 |pmid= 16966378 |doi= 10.1128/MCB.00979-06  | pmc=1636784 }}
-*{{cite journal  | author=Matsushima R, Harada N, Webster NJ, ''et al.'' |title=Effect of TRB3 on insulin and nutrient-stimulated hepatic p70 S6 kinase activity. |journal=J. Biol. Chem. |volume=281 |issue= 40 |pages= 29719–29 |year= 2006 |pmid= 16887816 |doi= 10.1074/jbc.M511636200 }}
-*{{cite journal  | author=Koh HJ, Arnolds DE, Fujii N, ''et al.'' |title=Skeletal muscle-selective knockout of LKB1 increases insulin sensitivity, improves glucose homeostasis, and decreases TRB3. |journal=Mol. Cell. Biol. |volume=26 |issue= 22 |pages= 8217–27 |year= 2007 |pmid= 16966378 |doi= 10.1128/MCB.00979-06 }}
-}}
 {{refend}}
-{{gene-20-stub}}
 {{Serine/threonine-specific protein kinases}}
+{{Enzymes}}
+{{Portal bar|Biology|border=no}}
+[[Category:EC 2.7.11]]
+{{Gene-20-stub}}
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v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme 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)