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TRIB1 (tribbles pseudokinase 1)

Written2015-03Jessica Johnston, Endre Kiss-Toth
Department of Cardiovascular Science, University of Sheffield, Sheffield, Beech Hill Road, Sheffield S10 2RX, United Kingdom

Abstract Review on TRIB1, with data on DNA, on the protein encoded, and where the gene is implicated.

Keywords TRIB1

(Note : for Links provided by Atlas : click)


Alias_namestribbles homolog 1 (Drosophila)
Alias_symbol (synonym)C8FW
Other aliasGIG-2
LocusID (NCBI) 10221
Atlas_Id 43539
Location 8q24.13; Transcript (including UTRs) chr8:126,442,563-126,450,644 Coding region: chr8:126,443,145-126,448,713.  [Link to chromosome band 8q24]
Location_base_pair Starts at 126444451 and ends at 126450647 bp from pter ( according to hg19-Feb_2009)  [Mapping TRIB1.png]
Fusion genes
(updated 2016)
LOC100507412 (-) / TRIB1 (8q24.13)TRIB1 (8q24.13) / NSMCE2 (8q24.13)TRIB1 (8q24.13) / SLC25A32 (8q22.3)
Note The tribbles family of genes encode a group of highly conserved pseudokinase proteins, which are thought to act as adaptors in several signalling pathways that are intimately involved in the regulation of a number of key cellular processes, including MAPK, and PI3K pathways. Tribbles have also been shown to interact with ubiquitin ligases, thereby promoting degradation of target proteins. Tribbles have been implicated in a number of diseases including leukaemia, metabolic syndromes and cardiovascular disease.
Tribbles proteins were first discovered in Drosophila as a negative regulator of string/cdc25, where when over-expressed directly inhibited mitosis (Grosshans and Wieschaus 2000). Simultaneously, TRIBs were found to promote the degradation of string via the proteasome pathway and showed that overexpression of tribbles in imaginal disc cells blocked the cell cycle at G2 resulting in abnormal wing morphology (Mata, et al 2000). Since then three highly conserved mammalian homologues have been indentified; Trib1, Trib2 and Trib3.


  There are two validated transcripts of TRIB1 (NM_025195 and NM_001282985) coding for isoforms 1 and 2 respectively. Isoform 2 has a shorter 5'UTR (untranslated region) and 5' coding region compared to isoform 1 and initiates translation further downstream. UTRs and exons are represented by the red and grey boxes respectively. Image drawn by FancyGene (Rambaldi and Ciccarelli 2009).
Transcription There are two protein coding transcripts of TRIB1; TRIB1-001 and TRIB1-002.
TRIB1-001 (Isoform 1); Transcript size: 3,635bp; Exon count: 3.
TRIB1-002 (Isoform 2); Transcript size: 1,332 bp; Exon count: 2


Note TRIB1-001: 372 amino acids; TRIB1-002: 206 amino acids
  Protein structure of Tribbles 1: TRIB1 has a N terminal, pseudokinase and C terminal domains. It contains four protein motifs; a putative PEST sequence, a kinase dead catalytic loop, a MEK1 binding and COP1 binding motif. The characteristic amino acid sequence for each motif is shown along with location.
Description TRIB1 contain a N terminal (NT) domain of 60-80 residues and a C-terminal domain of 35-40 residues and a characteristic single central Ser/Thr kinase-like (pseudokinase) domain. TRIB1 contains features consistent with its emerging role as a protein adaptor in signalling pathways.
N-Terminal Domain The NT fragment of TRIB1 is proline and serine rich, mostly in the sequence adjacent to the kinase-like domain. The abundance of these amino acids are a characteristic of PEST proteins that are involved in controlling the half life of proteins by altering their susceptibility to degradation. Other functions of these types of proteins include the anchoring of SH3 or WW domains of other proteins or acting as a substrate for proline dependent phosphorylation. TRIB1 contains possible phosphorylation sites for proline-dependent kinases (Hegedus, et al 2007).
TRIB1 also contains two evolutionary conserved motifs. The first consists of a putative nuclear localisation signal, [K/R]2X2[D/E]X[D/E]. The second motif contains a G-S-P consensus pattern found close to the kinase-like domain. The G-S-P motif is present in human SNIP1 (Smad nuclear interacting protein) which functionally associates with BGR1, which interacts with the Drosophila homologue of Slbo, C/EBP transcription factors (Beausoleil, et al 2004, Kadam, et al 2000). C/EBP transcription factors have been shown to functionally and physically interact with TRIB1 promoting their degradation (Yoshida, et al 2013).
Kinase-like domain TRIB1 contains a Ser/Thr kinase-like domain that is composed of some of the motifs present in catalytically active kinases such as a Lysine crucial for ATP binding whilst others are missing. Despite this evidence would suggest TRIB1 no to possess kinase activity. However this domain is highly conserved during evolution suggesting it is important for the role of TRIB1(Hegedus, et al 2007).
C-Terminal Domain The CT domain is around 35-45 amino acids long and is rich in charged amino acids important for protein interactions. Two important motifs have been identified in the CT domain; a hexapeptide motif [D/E]QXVP[D/E] as a COP1 (E3 ubiqutin ligase) binding site, essential for proteasome mediated degradation of C/EBP? family members and a MEK 1 binding site (ILLHPWF) (Hegedus, et al 2007).
Post translational modifications Several post translational modifications of TRIB1 have been reported and validated by mass spectrometry and listed in the PhosphoSitePlus database (Hornbeck, et al 2012).
Expression TRIB1 expression is ubiquitious with highest expression in the thyroid and myeloid cells (Figure?). TRIB1 is thought to expressed in a cell-type specific manner (Sung, et al 2006).
  The tissue specific expression of human TRIB1 mRNA is shown. Data and figure taken from BioGPS. Additional microarray expression data from the Human Gene Expression Atlas from the Genomics Institute of the Novartis Research Foundation (GNF) can be found on the UCSC browser ( (Su, et al 2004, Wu, et al 2009).
Localisation Numerous over-expression experiments have shown TRIB1 to be located in the nucleus. It contains a putative nuclear localisation signal (Yokoyama, et al 2010).
Function TRIB1 has been shown to interact with a number of proteins as detailed herein (Table1):
MEK-1 and MKK4 Co-immunoprecipitation experiments have shown specific interactions with MEK1 (an ERK activator MAPKK) and MKK4 (a JNK activator MAPKK). Interactions with Tribbles control the extent and specificity of MAPK activation and are dependent on levels of TRIB expression (Kiss-Toth, et al 2004, Sung, et al 2007).
MEK1 phosphorylates ERK which in turn promotes cell proliferation and suppression of apoptosis. The interaction between TRIB1 (via ILLHPWF motif) and MEK1
enhances ERK phosphorylation as mutants lacking the motif were unable to do so (Yokoyama, et al 2010) .
TRIB1 also interacts with MKK4, a JNK activator and implicated in the migration and proliferation of smooth muscle and involved in the pathogenesis of atherosclerosis. The nuclear localisation of TRIB1-MKK4 complex is dependent on the NT domain of TRIB1, however the central kinase-like domain of TRIB1 is sufficient for its interaction with MKK4 but the interaction is no longer preferentially nuclear (Sung, et al 2007).
COP1 AND C/EBPalpha TRIB1 contains a COP1 binding site at the carboxy terminus. COP1 is an E3 ubiquitin ligase that promotes the transfer of ubiquitin to target substrates for degradation via the proteasome. One of the prinicipal targets of COP1 are the family of transcription proteins CCAT/enhancer binding proteins (C/EBPs). It is thought TRIB1 acts to negatively regulate C/EBP proteins by acting as adaptors to recruit COP1 to C/EBP family members thereby promoting ubiquitination and degradation. Studies have shown that COP1 requires TRIB1 for its action of C/EBP? (Yoshida, et al 2013).
Homology TRIB1 homologues have been indentified in different species including mouse, frog and zebrafish. Table 2 illustrates some of the TRIB1 homologues.


Note A somatic point mutation of TRIB1 has been reported in Down syndrome (DS)- related acute megakaryocytic leukaemia (AMKL) (Yokoyama, et al 2012). A G:T point mutation was found in the pseudokinase domain resulting in an amino acid change from arginine to leucine (R107L). When the mutation was expressed in mouse bone marrow cells and transferred into lethally irradiated recipient mice there was a more rapid development of AML and enhancement of ERK phosporylation suggesting a gain of function mutation. Yokoyama, et al (2012) suggests that the mutation of TRIB1 is an early event in leukaemogenesis.
A wide range of allelic variants of TRIB1 have been reported. There are several genetic and protein variations of TRIB1 listed on Ensembl.
Table (3) shows the types of genetic variation of TRIB1. Data taken from:;g=ENSG00000173334;r=8:126442563-126450647
Protein variants of TRIB1: Table 4 shows the protein variants of TRIB1. Each variant is listed in order according to residue number. The table also lists SIFT and Poly-Phen scores for the variations. SIFT predicts whether an amino acid substitution is likely to affect protein function based on the sequence homology and the physico-chemical similarity between the alternate amino acids. Each variant is accompanied with a score and predictive consequence that is based on the probability that the amino acid change is tolerable. A score closer to 0 is more likely to be deleterious. A score of <0.05 are deleterious and all others are 'tolerated'. PolyPhen predicts the effect of an amino acid substitution on the structure and function of a protein using sequence homology. A PolyPhen score represent the probability that a substitution is damaging, scores nearer to 1 are more confidently to be predicted to be deleterious (opposite to SIFT score). Each score is colour coded according to damage (SIFT; Red= deleterious, Green= tolerated. PolyPhen; Red= probably damaging, Orange= possibly damaging, Green= benign) (Adzhubei, et al 2010, Gonzalez-Perez and Lopez-Bigas 2011, Kumar, et al 2009). Data taken from:;g=ENSG00000173334;r=8:126442563-126450647;t=ENST00000311922
  Table 3: Genetic variations of TRIB1
Somatic [Table 4: Protein variants of TRIB1]

Implicated in

Entity Smooth muscle cells
Note TRIB1 is selectively over-expressed in chronically inflamed human atherosclerotic arteries and regulates vascular smooth muscle cell (VSMC) chemotaxis and proliferation, a characteristic feature of atherosclerosis via the JNK pathway (Sung, et al 2007).
Entity Macrophages
Note Trib1 is expressed in plaque resident macrophages in murine experimental atherosclerosis. The expression of Trib1 could be upregulated by IL-1, a major contributor to plaque development as the percentage of Trib1 expressing macrophages significantly decreases in ApoE -/- IL1R-/- double knockout mice compared to ApoE-/- controls. Overexpression of Trib1 in macrophages in vitro also leads to a significant attenuation (~70%) of IL-6 production and suppressed IL-12 expression induced with a pro-inflammatory stimulus (Sung, et al 2012).
It has also been shown that TRIB1 is involved in macrophage migration through interactions with C/EBP? and TNF-?. Knockdown of TRIB1 in RAW246.7 cells resulted in an increase in TNF-? production and C/EBP? expression suggesting TRIB1 may modulate TNF-? through C/EBP? (Liu, et al 2013).
Trib1 has been shown to also be involved with adipose tissue maintenance and suppression of metabolic disorders by controlling the differentiation of tissue M2-like macrophages. Trib1 deficiency results in a significant reduction of M2-like macrophages. Mice lacking Trib1 in haematopoietic cells show a reduced adipocyte tissue mass and have evidence of increased lipolysis even on a normal diet. Supplementation of M2-like macrophages causes rescue suggesting the lack of these M2-like macrophages are responsible for lipolysis. When mice are fed a high fat diet, mice lacking Trib1 in haematopoietic cells develop hypertriglyceridaemia and insulin resistance and a pro-inflammatory cytokine induction (Satoh, et al 2013).


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Proc Natl Acad Sci U S A 2004 Aug 17;101(33):12130-5
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Trib1 is a lipid- and myocardial infarction-associated gene that regulates hepatic lipogenesis and VLDL production in mice
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PMID 21084752
Dense genotyping of candidate gene loci identifies variants associated with high-density lipoprotein cholesterol
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PMID 21303902
Improving the assessment of the outcome of nonsynonymous SNVs with a consensus deleteriousness score, Condel
Gonzá A, López-Bigas N
Am J Hum Genet 2011 Apr 8;88(4):440-9
PMID 21457909
A genetic link between morphogenesis and cell division during formation of the ventral furrow in Drosophila
Grosshans J, Wieschaus E
Cell 2000 May 26;101(5):523-31
PMID 10850494
Tribbles: a family of kinase-like proteins with potent signalling regulatory function
Hegedus Z, Czibula A, Kiss-Toth E
Cell Signal 2007 Feb;19(2):238-50
PMID 16963228
Trib1 and Evi1 cooperate with Hoxa and Meis1 in myeloid leukemogenesis
Jin G, Yamazaki Y, Takuwa M, Takahara T, Kaneko K, Kuwata T, Miyata S, Nakamura T
Blood 2007 May 1;109(9):3998-4005
PMID 17227832
Functional selectivity of recombinant mammalian SWI/SNF subunits
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Genes Dev 2000 Oct 1;14(19):2441-51
PMID 11018012
Tribbles homolog 2 inactivates C/EBPalpha and causes acute myelogenous leukemia
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Cancer Cell 2006 Nov;10(5):401-11
PMID 17097562
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J Biol Chem 2004 Oct 8;279(41):42703-8
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Diabetes 2011 Apr;60(4):1329-39
PMID 21386085
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Nat Protoc 2009;4(7):1073-81
PMID 19561590
Macrophage migration is controlled by Tribbles 1 through the interaction between C/EBP and TNF-
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PMID 23810419
Tribbles coordinates mitosis and morphogenesis in Drosophila by regulating string/CDC25 proteolysis
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Cell 2000 May 26;101(5):511-22
PMID 10850493
VectorBase: improvements to a bioinformatics resource for invertebrate vector genomics
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Nucleic Acids Res 2012 Jan;40(Database issue):D729-34
PMID 22135296
TRB2, a mouse Tribbles ortholog, suppresses adipocyte differentiation by inhibiting AKT and C/EBPbeta
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J Biol Chem 2007 Aug 17;282(33):24075-82
PMID 17576771
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PMID 20522600
TRB3 links the E3 ubiquitin ligase COP1 to lipid metabolism
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Human tribbles-1 controls proliferation and chemotaxis of smooth muscle cells via MAPK signaling pathways
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This paper should be referenced as such :
Johnston J, Kiss-Toth E
TRIB1 (tribbles pseudokinase 1);
Atlas Genet Cytogenet Oncol Haematol. in press
On line version :

External links

HGNC (Hugo)TRIB1   16891
Entrez_Gene (NCBI)TRIB1  10221  tribbles pseudokinase 1
AliasesC8FW; GIG-2; GIG2; SKIP1; 
GeneCards (Weizmann)TRIB1
Ensembl hg19 (Hinxton)ENSG00000173334 [Gene_View]  chr8:126444451-126450647 [Contig_View]  TRIB1 [Vega]
Ensembl hg38 (Hinxton)ENSG00000173334 [Gene_View]  chr8:126444451-126450647 [Contig_View]  TRIB1 [Vega]
ICGC DataPortalENSG00000173334
TCGA cBioPortalTRIB1
Genatlas (Paris)TRIB1
SOURCE (Princeton)TRIB1
Genetics Home Reference (NIH)TRIB1
Genomic and cartography
GoldenPath hg19 (UCSC)TRIB1  -     chr8:126444451-126450647 +  8q24.13   [Description]    (hg19-Feb_2009)
GoldenPath hg38 (UCSC)TRIB1  -     8q24.13   [Description]    (hg38-Dec_2013)
EnsemblTRIB1 - 8q24.13 [CytoView hg19]  TRIB1 - 8q24.13 [CytoView hg38]
Mapping of homologs : NCBITRIB1 [Mapview hg19]  TRIB1 [Mapview hg38]
Gene and transcription
Genbank (Entrez)AF205437 AF250310 AJ000480 AK001319 AK022787
RefSeq transcript (Entrez)NM_001282985 NM_025195
RefSeq genomic (Entrez)NC_000008 NC_018919 NT_008046 NW_004929340
Consensus coding sequences : CCDS (NCBI)TRIB1
Cluster EST : UnigeneHs.444947 [ NCBI ]
CGAP (NCI)Hs.444947
Alternative Splicing GalleryENSG00000173334
Gene ExpressionTRIB1 [ NCBI-GEO ]   TRIB1 [ EBI - ARRAY_EXPRESS ]   TRIB1 [ SEEK ]   TRIB1 [ MEM ]
Gene Expression Viewer (FireBrowse)TRIB1 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)10221
GTEX Portal (Tissue expression)TRIB1
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ96RU8   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ96RU8  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ96RU8
Splice isoforms : SwissVarQ96RU8
Domaine pattern : Prosite (Expaxy)PROTEIN_KINASE_DOM (PS50011)   
Domains : Interpro (EBI)Kinase-like_dom    Prot_kinase_dom    TRB1    Tribbles/Ser_Thr_kinase_40   
Domain families : Pfam (Sanger)Pkinase (PF00069)   
Domain families : Pfam (NCBI)pfam00069   
Conserved Domain (NCBI)TRIB1
DMDM Disease mutations10221
Blocks (Seattle)TRIB1
PDB (SRS)5CEK    5CEM   
PDB (PDBSum)5CEK    5CEM   
PDB (IMB)5CEK    5CEM   
Structural Biology KnowledgeBase5CEK    5CEM   
SCOP (Structural Classification of Proteins)5CEK    5CEM   
CATH (Classification of proteins structures)5CEK    5CEM   
Human Protein AtlasENSG00000173334
Peptide AtlasQ96RU8
IPIIPI00290308   IPI01013113   IPI00797829   
Protein Interaction databases
IntAct (EBI)Q96RU8
Ontologies - Pathways
Ontology : AmiGOprotein kinase activity  protein kinase inhibitor activity  protein binding  ATP binding  nucleus  cytoplasm  protein phosphorylation  negative regulation of protein kinase activity  JNK cascade  transcription factor binding  negative regulation of smooth muscle cell migration  mitogen-activated protein kinase kinase binding  ubiquitin protein ligase binding  negative regulation of lipopolysaccharide-mediated signaling pathway  positive regulation of proteasomal ubiquitin-dependent protein catabolic process  positive regulation of proteasomal ubiquitin-dependent protein catabolic process  response to lipopolysaccharide  response to lipopolysaccharide  regulation of MAP kinase activity  negative regulation of sequence-specific DNA binding transcription factor activity  negative regulation of sequence-specific DNA binding transcription factor activity  positive regulation of eosinophil differentiation  positive regulation of macrophage differentiation  negative regulation of neutrophil differentiation  negative regulation of smooth muscle cell proliferation  ubiquitin-protein transferase regulator activity  
Ontology : EGO-EBIprotein kinase activity  protein kinase inhibitor activity  protein binding  ATP binding  nucleus  cytoplasm  protein phosphorylation  negative regulation of protein kinase activity  JNK cascade  transcription factor binding  negative regulation of smooth muscle cell migration  mitogen-activated protein kinase kinase binding  ubiquitin protein ligase binding  negative regulation of lipopolysaccharide-mediated signaling pathway  positive regulation of proteasomal ubiquitin-dependent protein catabolic process  positive regulation of proteasomal ubiquitin-dependent protein catabolic process  response to lipopolysaccharide  response to lipopolysaccharide  regulation of MAP kinase activity  negative regulation of sequence-specific DNA binding transcription factor activity  negative regulation of sequence-specific DNA binding transcription factor activity  positive regulation of eosinophil differentiation  positive regulation of macrophage differentiation  negative regulation of neutrophil differentiation  negative regulation of smooth muscle cell proliferation  ubiquitin-protein transferase regulator activity  
NDEx NetworkTRIB1
Atlas of Cancer Signalling NetworkTRIB1
Wikipedia pathwaysTRIB1
Orthology - Evolution
GeneTree (enSembl)ENSG00000173334
Phylogenetic Trees/Animal Genes : TreeFamTRIB1
Homologs : HomoloGeneTRIB1
Homology/Alignments : Family Browser (UCSC)TRIB1
Gene fusions - Rearrangements
Fusion : MitelmanTRIB1/NSMCE2 [8q24.13/8q24.13]  
Fusion : MitelmanTRIB1/SLC25A32 [8q24.13/8q22.3]  [t(8;8)(q22;q24)]  
Fusion: TCGATRIB1 8q24.13 NSMCE2 8q24.13 BRCA LUAD
Fusion: TCGATRIB1 8q24.13 SLC25A32 8q22.3 BRCA
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerTRIB1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)TRIB1
Exome Variant ServerTRIB1
ExAC (Exome Aggregation Consortium)TRIB1 (select the gene name)
Genetic variants : HAPMAP10221
Genomic Variants (DGV)TRIB1 [DGVbeta]
DECIPHER (Syndromes)8:126444451-126450647  ENSG00000173334
CONAN: Copy Number AnalysisTRIB1 
ICGC Data PortalTRIB1 
TCGA Data PortalTRIB1 
Broad Tumor PortalTRIB1
OASIS PortalTRIB1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICTRIB1  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDTRIB1
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch TRIB1
DgiDB (Drug Gene Interaction Database)TRIB1
DoCM (Curated mutations)TRIB1 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)TRIB1 (select a term)
NCG5 (London)TRIB1
Cancer3DTRIB1(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry TRIB1
NextProtQ96RU8 [Medical]
Huge Navigator TRIB1 [HugePedia]
snp3D : Map Gene to Disease10221
BioCentury BCIQTRIB1
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD10221
Chemical/Pharm GKB GenePA134963922
Clinical trialTRIB1
canSAR (ICR)TRIB1 (select the gene name)
PubMed73 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
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