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Tribbles homolog 3 (TRB-3) (Neuronal cell death-inducible putative kinase)

 TRIB3_MOUSE             Reviewed;         354 AA.
Q8K4K2; Q3UMQ0; Q921E7;
01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
01-FEB-2003, sequence version 2.
07-JUN-2017, entry version 145.
RecName: Full=Tribbles homolog 3;
Short=TRB-3;
AltName: Full=Neuronal cell death-inducible putative kinase;
Name=Trib3; Synonyms=Nipk, Trb3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, INDUCTION, AND INTERACTION WITH ATF4.
PubMed=12749859; DOI=10.1016/S0014-4827(03)00070-3;
Ord D., Ord T.;
"Mouse NIPK interacts with ATF4 and affects its transcriptional
activity.";
Exp. Cell Res. 286:308-320(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND INTERACTION WITH
AKT1 AND AKT2.
PubMed=12791994; DOI=10.1126/science.1079817;
Du K., Herzig S., Kulkarni R.N., Montminy M.;
"TRB3: a tribbles homolog that inhibits Akt/PKB activation by insulin
in liver.";
Science 300:1574-1577(2003).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Kiss-Toth E., Dempsey C., Jozsa V., Caunt J., Oxley K.M.,
Bagstaff S.M., Wyllie D.H., Harte M., O'Neill L.A.J., Qwarnstrom E.E.,
Dower S.K.;
"Mammalian homologs of Drosophila tribbles (htrb) control mitogen
activated protein kinase signaling.";
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and DBA/2J; TISSUE=Lung, and Placenta;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, INTERACTION WITH APOBEC3A, AND SUBCELLULAR LOCATION.
PubMed=22977230; DOI=10.1074/jbc.M112.372722;
Aynaud M.M., Suspene R., Vidalain P.O., Mussil B., Guetard D.,
Tangy F., Wain-Hobson S., Vartanian J.P.;
"Human Tribbles 3 protects nuclear DNA from cytidine deamination by
APOBEC3A.";
J. Biol. Chem. 287:39182-39192(2012).
-!- FUNCTION: Disrupts insulin signaling by binding directly to Akt
kinases and blocking their activation. May bind directly to and
mask the 'Thr-308' phosphorylation site in AKT1. Binds to ATF4 and
inhibits its transcriptional activation activity. Interacts with
the NF-kappa-B transactivator p65 RELA and inhibits its
phosphorylation and thus its transcriptional activation activity.
Interacts with MAPK kinases and regulates activation of MAP
kinases. May play a role in programmed neuronal cell death but
does not appear to affect non-neuronal cells. Does not display
kinase activity. Inhibits the transcriptional activity of
DDIT3/CHOP and is involved in DDIT3/CHOP-dependent cell death
during ER stress (By similarity). Can inhibit APOBEC3A editing of
nuclear DNA. {ECO:0000250, ECO:0000269|PubMed:12749859,
ECO:0000269|PubMed:12791994, ECO:0000269|PubMed:22977230}.
-!- SUBUNIT: Interacts with AKT1, AKT2, ATF4, MAP2K1 and MAP2K7.
Interacts with DDIT3/CHOP and inhibits its interaction with
EP300/P300 (By similarity). Interacts with APOBEC3C (By
similarity). Interacts (via N-terminus) with APOBEC3A.
{ECO:0000250, ECO:0000269|PubMed:12749859,
ECO:0000269|PubMed:12791994, ECO:0000269|PubMed:22977230}.
-!- INTERACTION:
P31750:Akt1; NbExp=5; IntAct=EBI-448962, EBI-298707;
Q06507:Atf4; NbExp=3; IntAct=EBI-448962, EBI-77383;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12749859,
ECO:0000269|PubMed:22977230}.
-!- TISSUE SPECIFICITY: Highly expressed in liver. Not detected in
heart, brain, spleen, lung, skeletal muscle, kidney or testis.
{ECO:0000269|PubMed:12749859}.
-!- INDUCTION: In liver under fasting conditions and by thapsigargin.
{ECO:0000269|PubMed:12749859, ECO:0000269|PubMed:12791994}.
-!- DOMAIN: The protein kinase domain is predicted to be catalytically
inactive.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. Tribbles subfamily. {ECO:0000305}.
-!- CAUTION: The role of this protein in Akt activation has been
demonstrated in PubMed:12749859 but Iynedjian has not been able to
reproduce the result in rat hepatocytes. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ514260; CAD55728.1; -; mRNA.
EMBL; AF358868; AAM45476.1; -; mRNA.
EMBL; AK089931; BAC41002.1; -; mRNA.
EMBL; AK132257; BAE21062.1; -; mRNA.
EMBL; AK144752; BAE26048.1; -; mRNA.
EMBL; AK146340; BAE27094.1; -; mRNA.
EMBL; AK159760; BAE35351.1; -; mRNA.
EMBL; BC012955; AAH12955.1; -; mRNA.
CCDS; CCDS16881.1; -.
RefSeq; NP_780302.2; NM_175093.2.
UniGene; Mm.276018; -.
ProteinModelPortal; Q8K4K2; -.
SMR; Q8K4K2; -.
BioGrid; 230766; 2.
DIP; DIP-31533N; -.
IntAct; Q8K4K2; 2.
STRING; 10090.ENSMUSP00000041747; -.
iPTMnet; Q8K4K2; -.
PhosphoSitePlus; Q8K4K2; -.
PaxDb; Q8K4K2; -.
PRIDE; Q8K4K2; -.
Ensembl; ENSMUST00000040312; ENSMUSP00000041747; ENSMUSG00000032715.
GeneID; 228775; -.
KEGG; mmu:228775; -.
UCSC; uc008nff.1; mouse.
CTD; 57761; -.
MGI; MGI:1345675; Trib3.
eggNOG; KOG0583; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00880000137914; -.
HOGENOM; HOG000231872; -.
HOVERGEN; HBG067729; -.
InParanoid; Q8K4K2; -.
KO; K19518; -.
OMA; YTCKVYP; -.
OrthoDB; EOG091G07JM; -.
PhylomeDB; Q8K4K2; -.
TreeFam; TF329785; -.
Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
Reactome; R-MMU-165158; Activation of AKT2.
Reactome; R-MMU-199418; Negative regulation of the PI3K/AKT network.
Reactome; R-MMU-389357; CD28 dependent PI3K/Akt signaling.
Reactome; R-MMU-5218920; VEGFR2 mediated vascular permeability.
ChiTaRS; Trib3; mouse.
PRO; PR:Q8K4K2; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000032715; -.
CleanEx; MM_TRIB3; -.
Genevisible; Q8K4K2; MM.
GO; GO:0031965; C:nuclear membrane; ISO:MGI.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IBA:GO_Central.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004860; F:protein kinase inhibitor activity; IEA:UniProtKB-KW.
GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:BHF-UCL.
GO; GO:0055106; F:ubiquitin-protein transferase regulator activity; IDA:BHF-UCL.
GO; GO:0032869; P:cellular response to insulin stimulus; IDA:BHF-UCL.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:UniProtKB.
GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:BHF-UCL.
GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IMP:BHF-UCL.
GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; TAS:BHF-UCL.
GO; GO:0032092; P:positive regulation of protein binding; IDA:BHF-UCL.
GO; GO:0045732; P:positive regulation of protein catabolic process; IC:BHF-UCL.
GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IDA:BHF-UCL.
GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
GO; GO:0010827; P:regulation of glucose transport; IDA:BHF-UCL.
GO; GO:0043405; P:regulation of MAP kinase activity; ISS:UniProtKB.
GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR024104; Tribbles/Ser_Thr_kinase_40.
InterPro; IPR024106; Tribbles_TRB3.
PANTHER; PTHR22961; PTHR22961; 1.
PANTHER; PTHR22961:SF21; PTHR22961:SF21; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
1: Evidence at protein level;
Apoptosis; Complete proteome; Nucleus; Protein kinase inhibitor;
Reference proteome; Transcription; Transcription regulation.
CHAIN 1 354 Tribbles homolog 3.
/FTId=PRO_0000131867.
DOMAIN 68 315 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 1 127 Interaction with DDIT3/CHOP.
{ECO:0000250}.
CONFLICT 157 157 S -> P (in Ref. 5; AAH12955).
{ECO:0000305}.
CONFLICT 219 219 K -> T (in Ref. 3; AAM45476).
{ECO:0000305}.
CONFLICT 239 264 Missing (in Ref. 5). {ECO:0000305}.
CONFLICT 301 354 SERLVALGILLHPWLREDHGRVSPPQSDRREMDQVVPDGPQ
LEEAEEGEVGLYG -> CRATCGPGNPLASLVERGSRPSLS
STV (in Ref. 4; BAC41002). {ECO:0000305}.
SEQUENCE 354 AA; 39023 MW; 2CB283FC119F859F CRC64;
MRATPLAASA DVSCRKKPLE FDDNIDAKCP VLKRVRDEPE PGPLPSLLPP SPPPASDLSP
AVAPATRLGP YILLEREQGS CSYRALHCPT GTEYTCKVYP ASEAQAVLAP YARLPTHQHV
ARPTEVLLGS RLLYIFFTKT HGDLHSLVRS RRGIPESEAA GLFRQMASAV AHCHKHGLVL
RDLKLRRFVF SNCERTKLVL ENLEDACVMT GSDDSLWDKH ACPAYVGPEI LSSRPSYSGK
AADVWSLGVA LFTMLAGRYP FHDSEPVLLF GKIRRGTFAL PEGLSAPARC LIRCLLRKEP
SERLVALGIL LHPWLREDHG RVSPPQSDRR EMDQVVPDGP QLEEAEEGEV GLYG


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