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RH69304p (Tribbles) (EC 2.7.11.-)

 TRIB_DROME              Reviewed;         484 AA.
Q9V3Z1;
31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
23-MAY-2018, entry version 161.
RecName: Full=Tribbles {ECO:0000303|PubMed:10837248};
Name=trbl {ECO:0000303|PubMed:10837248,
ECO:0000312|FlyBase:FBgn0028978};
ORFNames=CG5408 {ECO:0000312|FlyBase:FBgn0028978};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
[1] {ECO:0000312|EMBL:AAF26374.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND
DISRUPTION PHENOTYPE.
PubMed=10837248; DOI=10.1016/S0960-9822(00)00502-9;
Seher T.C., Leptin M.;
"Tribbles, a cell cycle brake that coordinates proliferation and
morphogenesis during Drosophila gastrulation.";
Curr. Biol. 10:623-629(2000).
[2] {ECO:0000312|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3] {ECO:0000312|Proteomes:UP000000803}
GENOME REANNOTATION.
STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4] {ECO:0000312|EMBL:AAO45190.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley {ECO:0000312|EMBL:AAO45190.1}; TISSUE=Head;
Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.,
Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
George R., Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G.,
Miranda A., Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S.,
Patel S., Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M.,
Celniker S.;
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000305}
FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=10850493;
Mata J., Curado S., Ephrussi A., Roerth P.;
"Tribbles coordinates mitosis and morphogenesis in Drosophila by
regulating string/CDC25 proteolysis.";
Cell 101:511-522(2000).
[6] {ECO:0000305}
FUNCTION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF LYS-266.
PubMed=10850494;
Grosshans J., Wieschaus E.;
"A genetic link between morphogenesis and cell division during
formation of the ventral furrow in Drosophila.";
Cell 101:523-531(2000).
[7] {ECO:0000305}
FUNCTION, INTERACTION WITH SLBO, AND DISRUPTION PHENOTYPE.
PubMed=10949024;
Roerth P., Szabo K., Texido G.;
"The level of C/EBP protein is critical for cell migration during
Drosophila oogenesis and is tightly controlled by regulated
degradation.";
Mol. Cell 6:23-30(2000).
[8] {ECO:0000305}
FUNCTION.
PubMed=15581871; DOI=10.1016/j.ydbio.2004.08.043;
Fichelson P., Gho M.;
"Mother-daughter precursor cell fate transformation after Cdc2 down-
regulation in the Drosophila bristle lineage.";
Dev. Biol. 276:367-377(2004).
[9] {ECO:0000305}
FUNCTION.
PubMed=18430923; DOI=10.1534/genetics.107.084582;
LaFerriere H., Guarnieri D.J., Sitaraman D., Diegelmann S.,
Heberlein U., Zars T.;
"Genetic dissociation of ethanol sensitivity and memory formation in
Drosophila melanogaster.";
Genetics 178:1895-1902(2008).
[10] {ECO:0000305}
FUNCTION.
PubMed=23290551; DOI=10.1016/j.cub.2012.11.036;
Farrell J.A., O'Farrell P.H.;
"Mechanism and regulation of Cdc25/Twine protein destruction in
embryonic cell-cycle remodeling.";
Curr. Biol. 23:118-126(2013).
[11] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS
OF ARG-154; ASP-264 AND GLU-286.
PubMed=23305818; DOI=10.1016/j.ydbio.2012.12.016;
Masoner V., Das R., Pence L., Anand G., LaFerriere H., Zars T.,
Bouyain S., Dobens L.L.;
"The kinase domain of Drosophila Tribbles is required for turnover of
fly C/EBP during cell migration.";
Dev. Biol. 375:33-44(2013).
[12]
FUNCTION, INTERACTION WITH AKT1, SUBCELLULAR LOCATION, DISRUPTION
PHENOTYPE, AND MUTAGENESIS OF ASP-264.
PubMed=25329475; DOI=10.1371/journal.pone.0109530;
Das R., Sebo Z., Pence L., Dobens L.L.;
"Drosophila tribbles antagonizes insulin signaling-mediated growth and
metabolism via interactions with Akt kinase.";
PLoS ONE 9:E109530-E109530(2014).
[13]
ERRATUM.
Das R., Sebo Z., Pence L., Dobens L.L.;
PLoS ONE 10:E123150-E123150(2014).
[14]
FUNCTION, INTERACTION WITH AKT1, SUBCELLULAR LOCATION, DISRUPTION
PHENOTYPE, AND MUTAGENESIS OF ARG-141 AND ASP-264.
PubMed=29025897; DOI=10.1242/dmm.030619;
Fischer Z., Das R., Shipman A., Fan J.Y., Pence L., Bouyain S.,
Dobens L.L.;
"A Drosophila model of insulin resistance associated with the human
Trib3 Q/R polymorphism.";
Dis. Model. Mech. 10:1453-1464(2017).
[15]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=28669782; DOI=10.1016/j.nlm.2017.06.006;
LaFerriere H., Zars T.;
"The Drosophila melanogaster tribbles pseudokinase is necessary for
proper memory formation.";
Neurobiol. Learn. Mem. 144:68-76(2017).
-!- FUNCTION: Adapter protein that negatively regulates different
signaling pathways to coordinate cell differentiation,
proliferation, migration and growth (PubMed:10837248,
PubMed:10850493, PubMed:10850494, PubMed:10949024,
PubMed:23305818, PubMed:25329475). Functions by binding to key
regulatory proteins and either blocks their activity or regulates
their turnover by the proteasome (PubMed:10837248,
PubMed:10850493, PubMed:10850494, PubMed:10949024,
PubMed:23305818, PubMed:25329475). In various developing tissues
functions as a cell cycle regulator that mediates cell
proliferation according to the requirements of the developmental
program (PubMed:10850493, PubMed:10850494, PubMed:10837248,
PubMed:15581871). Acts by inducing the proteasomal degradation of
the CD25 mitotic activators stg and twe at critical stages of
development to delay entry into mitosis and thus mediate cell
proliferation (PubMed:10850493, PubMed:10850494, PubMed:10837248,
PubMed:15581871, PubMed:23290551, PubMed:29025897). During
gastrulation, negatively regulates stg to delay mitosis in the
ventral region of the embryonic mesoderm thus allowing
invagination to be completed before cell division takes place
(PubMed:10837248, PubMed:10850493, PubMed:10850494). Delaying stg-
dependent mitosis during bristle development and in migrating
germline pole cells also arrests their cell divisions, whereas in
cystocytes it promotes their cell divisions (PubMed:10837248,
PubMed:10850493, PubMed:15581871). Involved in the regulation of
the mid-blastula transition; promotes the destruction of twe
resulting in the cell cycle arrest in G2 of cycle 14 which delays
mitosis and thus reduces cell proliferation allowing cell fate
specification and morphogenesis to take place (PubMed:23290551).
In germline cells, blocks border cell migration during oogenesis
by binding to slbo/C/EBP and promoting its ubiquitination and
degradation by the proteasome (PubMed:23305818, PubMed:10949024,
PubMed:29025897). May function in a negative feedback loop with
slbo to coordinate proper border cell migration (PubMed:23305818).
During tissue growth negatively regulates insulin signaling by
binding to Akt1 and blocking its phosphorylation-dependent
activation (PubMed:25329475, PubMed:29025897). However it may also
function downstream in the insulin signaling pathway, acting with
Akt1 to direct foxo degradation (PubMed:25329475). Essential for
the proper formation of operant place and aversive olfactory
memories (PubMed:18430923, PubMed:28669782).
{ECO:0000269|PubMed:10837248, ECO:0000269|PubMed:10850493,
ECO:0000269|PubMed:10850494, ECO:0000269|PubMed:10949024,
ECO:0000269|PubMed:15581871, ECO:0000269|PubMed:18430923,
ECO:0000269|PubMed:23290551, ECO:0000269|PubMed:23305818,
ECO:0000269|PubMed:25329475, ECO:0000269|PubMed:28669782,
ECO:0000269|PubMed:29025897}.
-!- SUBUNIT: Interacts with slbo (PubMed:10949024). Interacts with
Akt1 (PubMed:29025897, PubMed:25329475).
{ECO:0000269|PubMed:10949024, ECO:0000269|PubMed:25329475,
ECO:0000269|PubMed:29025897}.
-!- INTERACTION:
Q9VXS3:Dmel\CG12708; NbExp=4; IntAct=EBI-113217, EBI-174844;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23305818,
ECO:0000269|PubMed:25329475, ECO:0000269|PubMed:29025897}.
Cytoplasm {ECO:0000269|PubMed:23305818,
ECO:0000269|PubMed:25329475, ECO:0000269|PubMed:29025897}.
Cytoplasm, cell cortex {ECO:0000269|PubMed:29025897}. Note=Weakly
cytoplasmic (PubMed:29025897). In the main body follicle cells,
strong nuclear accumulation at stage 10 that decreases to low
levels in the cytoplasm by stage 12 (PubMed:23305818). In border
cells, high levels of expression detected prior to border cell
(BC) delamination (from stages 7 to 8) (PubMed:23305818). At stage
9, expression levels remains high in BC as their migration begins
but decreases throughout migration. By stage 10 levels are low in
BC nuclei when they arrive at the nurse cell/oocyte boundary
(PubMed:23305818). {ECO:0000269|PubMed:23305818,
ECO:0000269|PubMed:29025897}.
-!- TISSUE SPECIFICITY: Expressed throughout the brain with highest
levels of expression detected in the cell body rind and lower
levels of expression detected in the neurophil (at protein level).
{ECO:0000269|PubMed:28669782}.
-!- DEVELOPMENTAL STAGE: Zygotic expression first occurs in the
prospective embryonic mesoderm, and later in the ectoderm as well
(PubMed:10837248). Expression decreases over embryogenesis
(PubMed:10837248). High levels of expression in embryos at the
beginning of cycle 14 (PubMed:10850494). During cellularization,
expression declines but persists throughout gastrulation and until
late embryogenesis (PubMed:10850494). In stage 5 embryos,
ubiquitously expressed with increased expression in the ventral
region (PubMed:10850493). During gastrulation, highest levels of
expression are in the ventral cells (PubMed:10850494).
{ECO:0000269|PubMed:10837248, ECO:0000269|PubMed:10850493,
ECO:0000269|PubMed:10850494}.
-!- DOMAIN: The protein kinase domain is predicted to be catalytically
inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- DISRUPTION PHENOTYPE: Low viability with only 14% of mutants
survive to adulthood (PubMed:10850493). The egg chambers of
surviving females often have only eight germline cysts half of
which have an oocyte and the other half do not (PubMed:10850493).
Early stage 9 to stage 10 embryos, display increased levels of
slbo (PubMed:10949024). RNAi-mediated knockdown in embryos
produces premature mitosis in part or all of the ventral region,
resulting in many mutants displaying defects in gastrulation
including partial invagination of the mesoderm (PubMed:10837248).
RNAi-mediated knockdown results in an increase in phosphorylated
Akt1 but has no effect on total Akt1 levels (PubMed:25329475,
PubMed:29025897). RNAi-mediated knockdown in the fat body
increases lipid accumulation, larval weight, fat body cell size
and the size of fat body nuclei (PubMed:25329475). The increase in
larval weight results in delayed pupariation (PubMed:25329475).
Flies also display an increase in triglyceride levels which is
consistent with the increase in the number and size of lipid
bodies (PubMed:25329475). RNAi-mediated knockdown in the fat body
does not result in a significant change in triglyceride levels but
flies display an increase in glycogen levels and an increase in
lipid droplet size (PubMed:29025897). No effect on glucose or
trehalose levels in the hemolymph (PubMed:25329475,
PubMed:29025897). RNAi-mediated knockdown in late stage border
cells, partially reduced border cell migration (PubMed:23305818).
{ECO:0000269|PubMed:10837248, ECO:0000269|PubMed:10850493,
ECO:0000269|PubMed:10949024, ECO:0000269|PubMed:23305818,
ECO:0000269|PubMed:25329475, ECO:0000269|PubMed:29025897}.
-!- MISCELLANEOUS: 'tribbles' is named after fictional small round
organisms from the Star Trek universe that proliferate
uncontrollably. {ECO:0000303|PubMed:10837248}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. Tribbles subfamily. {ECO:0000305}.
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EMBL; AF204688; AAF26374.1; -; mRNA.
EMBL; AE014296; AAF51590.1; -; Genomic_DNA.
EMBL; BT004834; AAO45190.1; -; mRNA.
RefSeq; NP_524672.1; NM_079933.4.
UniGene; Dm.1418; -.
IntAct; Q9V3Z1; 3.
STRING; 7227.FBpp0077893; -.
PaxDb; Q9V3Z1; -.
PRIDE; Q9V3Z1; -.
EnsemblMetazoa; FBtr0078235; FBpp0077893; FBgn0028978.
GeneID; 43999; -.
KEGG; dme:Dmel_CG5408; -.
UCSC; CG5408-RA; d. melanogaster.
CTD; 43999; -.
FlyBase; FBgn0028978; trbl.
eggNOG; KOG0583; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00900000140868; -.
KO; K08814; -.
OMA; FYFIDEA; -.
OrthoDB; EOG091G05V6; -.
Reactome; R-DME-1257604; PIP3 activates AKT signaling.
Reactome; R-DME-165158; Activation of AKT2.
Reactome; R-DME-199418; Negative regulation of the PI3K/AKT network.
Reactome; R-DME-389357; CD28 dependent PI3K/Akt signaling.
Reactome; R-DME-5218920; VEGFR2 mediated vascular permeability.
GenomeRNAi; 43999; -.
PRO; PR:Q9V3Z1; -.
Proteomes; UP000000803; Chromosome 3L.
Bgee; FBgn0028978; -.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IBA:GO_Central.
GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
GO; GO:0042803; F:protein homodimerization activity; IPI:FlyBase.
GO; GO:0004860; F:protein kinase inhibitor activity; IMP:FlyBase.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0042593; P:glucose homeostasis; IMP:FlyBase.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IGI:FlyBase.
GO; GO:0010888; P:negative regulation of lipid storage; IMP:FlyBase.
GO; GO:0045839; P:negative regulation of mitotic nuclear division; IMP:FlyBase.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IMP:FlyBase.
GO; GO:0045793; P:positive regulation of cell size; IMP:FlyBase.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; IDA:FlyBase.
GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
GO; GO:0051726; P:regulation of cell cycle; IMP:FlyBase.
GO; GO:0043405; P:regulation of MAP kinase activity; IBA:GO_Central.
GO; GO:0007370; P:ventral furrow formation; IGI:FlyBase.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR024104; Tribbles/Ser_Thr_kinase_40.
PANTHER; PTHR22961; PTHR22961; 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;
Cell cycle; Complete proteome; Cytoplasm; Nucleus; Reference proteome.
CHAIN 1 484 Tribbles.
/FTId=PRO_0000442851.
DOMAIN 129 397 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MUTAGEN 141 141 R->E: Increased interaction with Akt1 and
some negative regulation of Atk1.
Increased interaction with slbo but no
effect on negative regulation of slbo-
dependent border cell migration. No
effect on interaction and negative
regulation of stg-dependent cell
divisions in the wing.
{ECO:0000269|PubMed:29025897}.
MUTAGEN 141 141 R->Q: Reduced interaction and inhibition
of Akt1 resulting in increased Akt1-
mediated growth and loss of carbohydrate
clearance from the hemolymph. No effect
on interaction with slbo and stg, and no
effect on the negative regulation of
slbo-dependent border cell migration and
stg-dependent cell divisions in the wing.
{ECO:0000269|PubMed:29025897}.
MUTAGEN 154 154 R->A: Partial loss of border cell
migration when expressed in border cells.
{ECO:0000269|PubMed:23305818}.
MUTAGEN 264 264 D->K: Reduced interaction with Akt1 and
reduced inhibition of Akt1-mediated
growth. Reduced interaction with slbo and
fails to block border cell migration. No
effect on cell division in the posterior
compartment of the wing.
{ECO:0000269|PubMed:23305818,
ECO:0000269|PubMed:25329475,
ECO:0000269|PubMed:29025897}.
MUTAGEN 266 266 K->R: No effect on mitosis. Embryos
display an early pause in the cell cycle
similar to wild-type.
{ECO:0000269|PubMed:10850494}.
MUTAGEN 286 286 E->G: Partial loss of border cell
migration when expressed in border cells.
{ECO:0000269|PubMed:23305818}.
SEQUENCE 484 AA; 54077 MW; 3E3B1D3E5645B0D7 CRC64;
MDNSSGQNSR TASSASTSKI VNYSSPVSPG VAAATSSSSS SSSSGMSSSQ EDTVLGLFTP
KKEFPNAKML QTIREKLMTP GGACDLLALG IAAEPTDQQP VKLIQQRYLI SAQPSHISAA
VAAKTPASYR HLVDLTASNL RCVDIFTGEQ FLCRIVNEPL HKVQRAYFQL QQHDEELRRS
TIYGHPLIRP VHDIIPLTKD RTYILIAPVP QERDSTGGVT GVYENLHTYI RHAKRLCETE
ARAIFHQICQ TVQVCHRNGI ILRDLKLKRF YFIDEARTKL QYESLEGSMI LDGEDDTLSD
KIGCPLYTAP ELLCPQQTYK GKPADMWSLG VILYTMLVGQ YPFYEKANCN LITVIRHGNV
QIPLTLSKSV RWLLLSLLRK DYTERMTASH IFLTPWLREQ RPFHMYLPVD VEVAEDWSDA
EEDEGTAADA MDDDEEGLCP LGDKHEYEDI GVEPLDYTRS TLQMAQNANG LSTEPEPDTD
VDMG


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H8783 Tribbles homolog 1 (TRIB1), Human, ELISA Kit 96T
CSB-EL024445BO Bovine Tribbles homolog 2(TRIB2) ELISA kit 96T
H8791 Tribbles homolog 3 (TRIB3), Mouse, ELISA Kit 96T
H8790 Tribbles homolog 3 (TRIB3), Human, ELISA Kit 96T


 

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